category accession gene organism organism_id protein_name caution degenerate-domain Q5UP71 Acanthamoeba polyphaga mimivirus (APMV) 212035 Structural PPIase-like protein L605 (Mimicyp) Lacks the conserved Arg in position 83 necessary for PPIase activity, and does not display any PPIase activity in vitro (PubMed:18342330). This protein was presumably a host PPIase stolen and converted by the virus to play a different function. {ECO:0000305|PubMed:18342330}. degenerate-domain Q5UQE9 Acanthamoeba polyphaga mimivirus (APMV) 212035 Uncharacterized peptidase C1-like protein L477 Although related to peptidase C1 family, it lacks conserved active site residues. {ECO:0000305}. degenerate-domain B0CDZ1 psbN Acaryochloris marina (strain MBIC 11017) 329726 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q3V4R9 Acidianus two-tailed virus (ATV) 315953 TnpB-like protein ORF457 Lacks the conserved Cys-residues found in other members of the transposase 35 family. {ECO:0000305}. degenerate-domain Q7J199 psbN Acorus calamus (Sweet flag) 4465 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q85FJ5 psbN Adiantum capillus-veneris (Maidenhair fern) 13818 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q17PP1 Aedes aegypti (Yellowfever mosquito) (Culex aegypti) 7159 Protein crossbronx homolog Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain A4QJE3 psbN Aethionema cordifolium (Lebanon stonecress) 434059 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A4QJM7 psbN Aethionema grandiflorum (Persian stone-cress) 72657 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P0C9D1 African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV) 561445 NifS-like protein Although related to the NifS/IscS subfamily, lacks the conserved active site, suggesting it has no transferase activity. {ECO:0000305}. degenerate-domain Q65236 African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV) 10500 NifS-like protein Although related to the NifS/IscS subfamily, lacks the conserved active site, suggesting it has no transferase activity. {ECO:0000305}. degenerate-domain P0C9C9 African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996) (ASFV) 561443 NifS-like protein Although related to the NifS/IscS subfamily, lacks the conserved active site, suggesting it has no transferase activity. {ECO:0000305}. degenerate-domain P0C9D0 African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV) 561444 NifS-like protein Although related to the NifS/IscS subfamily, lacks the conserved active site, suggesting it has no transferase activity. {ECO:0000305}. degenerate-domain Q65192 African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV) 10498 NifS-like protein Although related to the NifS/IscS subfamily, lacks the conserved active site, suggesting it has no transferase activity. {ECO:0000305}. degenerate-domain Q6EYL8 psbN Agathis robusta (Queensland kauri pine) 60854 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A1EA36 psbN Agrostis stolonifera (Creeping bentgrass) 63632 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain C0NM08 ECM14 Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum) 447093 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 488 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain C6H4F1 ECM14 Ajellomyces capsulatus (strain H143) (Darling's disease fungus) (Histoplasma capsulatum) 544712 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 488 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain C5G6U8 ECM14 Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis) 559297 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 487 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain A6TV07 katG2 Alkaliphilus metalliredigens (strain QYMF) 293826 Catalase-peroxidase 2 (CP 2) (EC 1.11.1.21) (Peroxidase/catalase 2) Could be the product of a pseudogene. The N-terminus is much shorter than in related proteins and lacks the active sites and the heme-binding sites. Moreover, the 71 first amino acids of this sequence are not homologous to other KatG sequences. {ECO:0000305}. degenerate-domain Q7GZA7 psbN Allenrolfea occidentalis (Iodine bush) (Halostachys occidentalis) 224139 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q67HV8 psbN Allium textile (Textile onion) (Allium reticulatum) 207935 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9G2I2 psbN Amborella trichopoda 13333 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q67I70 psbN Ananas comosus (Pineapple) (Ananas ananas) 4615 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A2T361 psbN Angiopteris evecta (Mule's foot fern) (Polypodium evectum) 13825 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7PRH1 Anopheles gambiae (African malaria mosquito) 7165 Protein crossbronx homolog Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain A0A1S4H5M5 CLIPA28 Anopheles gambiae (African malaria mosquito) 7165 Inactive CLIP domain-containing serine protease A28 [Cleaved into: Inactive CLIP domain-containing serine protease A28 light chain; Inactive CLIP domain-containing serine protease A28 heavy chain] Although it belongs to peptidase S1 family, lacks the conserved Ser residue within the catalytic triad (Asp-His-Ser) which is replaced by a Gly residue, probably resulting in a loss of proteolytic activity. {ECO:0000305}. degenerate-domain A0A1S4H5S2 CLIPA8 Anopheles gambiae (African malaria mosquito) 7165 Inactive CLIP domain-containing serine protease A8 [Cleaved into: Inactive CLIP domain-containing serine protease A8 light chain; Inactive CLIP domain-containing serine protease A8 heavy chain] Although it belongs to peptidase S1 family, lacks the conserved Ser residue within the catalytic triad (Asp-His-Ser) which is replaced by a Gly residue, probably resulting in a loss of proteolytic activity. {ECO:0000305}. degenerate-domain A0A1S4HE51 SPCLIP1 Anopheles gambiae (African malaria mosquito) 7165 Inactive CLIP domain-containing serine protease A30 (Inactive CLIP domain-containing serine protease SPCLIP1) Although it belongs to peptidase S1 family, the residues corresponding to the serine protease catalytic triad (Asp-His-Ser) are not conserved suggesting that SPCLIP1 lacks catalytic activity. {ECO:0000305|PubMed:24039584}. degenerate-domain Q85BG2 psbN Anthoceros angustus (Hornwort) (Anthoceros formosae) 48387 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain O24654 Arabidopsis thaliana (Mouse-ear cress) 3702 Inactive endochitinase At2g43600 Lacks the conserved Glu residue that is essential for catalytic activity, suggesting it lacks enzyme activity. {ECO:0000305}. degenerate-domain Q94JR6 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 206 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain F4JGB7 Arabidopsis thaliana (Mouse-ear cress) 3702 Chromatin remodeling protein At4g04260 Lacks two Cys residues in the RING-type zinc finger domain 2 that are conserved features of the family. {ECO:0000305}. degenerate-domain Q8RWH8 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable magnesium transporter NIPA9 Lacks one of the 9 transmembrane regions, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q9SUF4 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative protein phosphatase 2C 53 (AtPP2C53) (EC 3.1.3.16) (Protein phosphatase AP2C5) Although related to the protein phosphatase 2C family, lacks some of the conserved residues that bind manganese, suggesting it has no phosphatase activity. {ECO:0000305}.; degenerate-domain P0CAY2 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 53 Could be the product of a pseudogene. Lacks the signal peptide, which is a conserved features of the family. {ECO:0000305}. degenerate-domain Q2L6T1 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 283 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V311 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 303 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V370 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 218 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3K2 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 209 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3K7 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 211 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3Q8 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 255 Could be the product of a pseudogene. Lacks 2 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3W5 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 302 Could be the product of a pseudogene. Lacks the signal peptide and 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4D5 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 36 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4F3 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 35 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4N5 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 288 Could be the product of a pseudogene. Lacks the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q3E8B0 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 41 Could be the product of a pseudogene. Lacks the signal peptide, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain Q3E8R5 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 207 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q680C0 Arabidopsis thaliana (Mouse-ear cress) 3702 GDSL esterase/lipase At4g10955 (EC 3.1.1.-) Lacks the conserved active site 'GDSL' motif. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q84WD3 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable disease resistance protein At4g19060 Although strongly related to the NB-LRR family, it is shorter and lacks the LRR repeats that are present in other proteins of the family. {ECO:0000305}. degenerate-domain Q8LPI0 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative cysteine-rich receptor-like protein kinase At4g11521 (Cysteine-rich RLK At4g11521) Lacks the transmembrane and the protein kinase domains, which are conserved features of the CRK subfamily. {ECO:0000305}.; degenerate-domain Q9LW09 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative disease resistance protein At3g15700 Although strongly related to the NB-LRR family, it is shorter and lacks the LRR repeats that are present in other proteins of the family. {ECO:0000305}. degenerate-domain Q9SSR8 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable disease resistance protein At1g52660 Although strongly related to the NB-LRR family, it is shorter and lacks the LRR repeats that are present in other proteins of the family. {ECO:0000305}. degenerate-domain P0CAY1 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 42 Could be the product of a pseudogene. Lacks the signal peptide, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain Q2V2W3 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 264 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V2W6 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 224 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V304 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 220 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V305 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 219 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V369 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 223 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3J6 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 202 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3R9 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 29 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V472 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 291 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4A3 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 293 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4A7 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 64 Could be the product of a pseudogene. Lacks 2 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4D7 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 34 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4J8 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 316 Could be the product of a pseudogene. Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q56XB0 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 204 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain O80443 Arabidopsis thaliana (Mouse-ear cress) 3702 GDSL esterase/lipase At2g38180 (EC 3.1.1.-) (Extracellular lipase At2g38180) Lacks the conserved active site 'GDSL' motif. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q2V306 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 221 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3K4 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 210 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3R5 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 315 Could be the product of a pseudogene. Lacks the signal peptide and 2 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3X3 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 311 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V493 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 305 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4A4 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 294 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4F0 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 266 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4I8 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 32 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4J2 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 26 Could be the product of a pseudogene. Lacks 2 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q9LV55 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 259 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q9SH25 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative flavin-containing monooxygenase FMO GS-OX-like 11 (EC 1.8.-.-) (Putative flavin-monooxygenase glucosinolate S-oxygenase-like 11) Could be the product of a pseudogene. Lacks the C-terminal part of the protein containing the NADP-binding domain, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain P0CAY0 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 28 Could be the product of a pseudogene. Lacks the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain P0CAY3 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 105 Could be the product of a pseudogene. Lacks the signal peptide and 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q0WN71 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 123 Could be the product of a pseudogene. Lacks the signal peptide, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain Q2L6T6 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 286 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V2S9 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 72 Could be the product of a pseudogene. Lacks the signal peptide, which is a conserved features of the family. {ECO:0000305}. degenerate-domain Q2V2W2 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 265 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V300 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 222 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V318 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 254 Could be the product of a pseudogene. Lacks 2 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V342 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 113 Could be the product of a pseudogene. Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3D7 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 31 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3H5 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 307 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3K9 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 312 Could be the product of a pseudogene. Lacks 3 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3S0 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 30 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4D6 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 33 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4F6 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 279 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4N4 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 287 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q7XA64 Arabidopsis thaliana (Mouse-ear cress) 3702 Sugar transporter ERD6-like 9 This ERD6-like sugar transporter is shorter than other family members and contains only 8 transmembrane domains. It may not be functional. {ECO:0000305}. degenerate-domain Q9FHI7 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable disease resistance protein At5g45490 Although strongly related to the NB-LRR family, it is shorter and lacks the LRR repeats that are present in other proteins of the family. {ECO:0000305}. degenerate-domain Q9FKC1 Arabidopsis thaliana (Mouse-ear cress) 3702 Cytochrome b561 and DOMON domain-containing protein At5g48750 (Protein b561A.tha17) Lacks the C-terminal part of the cytochrome b561 domain, which contains the residues coordinating the two heme molecules and 4 of the 6 conserved transmembrane regions. {ECO:0000305}. degenerate-domain Q9FKZ2 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable disease resistance protein At5g66890 Lacks the typical ATP binding site, suggesting that it may not be functional. {ECO:0000305}. degenerate-domain P0CAY8 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 292 Could be the product of a pseudogene. Lacks the signal peptide and 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V2Q8 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 208 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V2Y0 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 282 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V309 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 304 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V310 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 309 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V354 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 267 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3J1 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 88 Could be the product of a pseudogene. Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3S7 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 258 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3S8 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 257 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V3Y5 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 317 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V433 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 52 Could be the product of a pseudogene. Lacks 2 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V477 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 12 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V483 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 256 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4C3 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 281 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4C4 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 280 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q2V4F7 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 278 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q3E7S1 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 87 Could be the product of a pseudogene. Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q3E8K0 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 313 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q3EAZ3 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative protein phosphatase 2C-like protein 45 (AtPP2C45) (Protein phosphatase AP2C6) Although related to the protein phosphatase 2C family, lacks some of the conserved residues that bind manganese, suggesting it has no phosphatase activity. {ECO:0000305}.; degenerate-domain Q3EDD7 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable protein cornichon homolog 2 Lacks one of the three transmembrane regions, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q4VP04 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 308 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q9C9F4 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative zinc finger protein At1g68190 Lacks the conserved CCT domain, which is one of the features of the CONSTANS family. {ECO:0000305}. degenerate-domain Q9FHJ2 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable disease resistance protein At5g45440 Although strongly related to the NB-LRR family, it is shorter and lacks the LRR repeats that are present in other proteins of the family. {ECO:0000305}. degenerate-domain Q9LW60 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative protein phosphatase 2C-like protein 44 (AtPP2C44) Although related to the protein phosphatase 2C family, lacks the conserved residues that bind manganese, suggesting it has no phosphatase activity. {ECO:0000305}.; degenerate-domain Q9M9M3 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 205 Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q9FX01 3BETAHSD/D1 Arabidopsis thaliana (Mouse-ear cress) 3702 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1 (At3BETAHSD/D1) (EC 1.1.1.418) (4alpha-carboxysterol-C3-dehydrogenase/C4-decarboxylase isoform 1-1) (Reticulon-like protein B24) (AtRTNLB24) (Sterol-4-alpha-carboxylate 3-dehydrogenase 1, decarboxylating) Lacks one transmembrane, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain Q7FB56 ABCC15 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative ABC transporter C family member 15 (ABC transporter ABCC.15) (AtABCC15) (EC 7.6.2.2) (ATP-energized glutathione S-conjugate pump 15) (Glutathione S-conjugate-transporting ATPase 15) (Putative multidrug resistance-associated protein 15) Lacks some conserved transmembrane domains, which are one of the features of the ABC conjugate transporter subfamily. {ECO:0000305}.; degenerate-domain Q944H2 ABCI12 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein ABCI12, chloroplastic (ABC transporter I family member 12) (ABC transporter ABCI.12) (AtABCI12) Was originally thought to belong to the ABC transporter family (PubMed:18299247). Lacks the conserved ABC domain, which is one of the features of the ABC transporter family. {ECO:0000305|PubMed:18299247}. degenerate-domain Q9LQK7 ABCI7 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein ABCI7, chloroplastic (ABC transporter I family member 7) (ABC transporter ABCI.7) (AtABCI7) (Non-intrinsic ABC protein 6) (Plastid SufD-like protein) Was originally (PubMed:11346655) thought to belong to the ABC transporter family. Lacks the conserved ABC domain, which is one of the features of the ABC transporter family. {ECO:0000305|PubMed:11346655}. degenerate-domain Q9ZS97 ABCI8 Arabidopsis thaliana (Mouse-ear cress) 3702 Iron-sulfur cluster assembly SufBD family protein ABCI8, chloroplastic (ABC transporter I family member 8) (ABC transporter ABCI.8) (AtABCI8) (Non-intrinsic ABC protein 1) (Protein ABC1) (Plastid sufB-like protein) (Protein LONG AFTER FAR-RED 6) Was originally (PubMed:11346655) thought to belong to the ABC transporter family. Lacks the conserved ABC domain, which is one of the features of the ABC transporter family. {ECO:0000305|PubMed:11346655}. degenerate-domain Q3E8H7 ABCI9 Arabidopsis thaliana (Mouse-ear cress) 3702 Iron-sulfur cluster assembly SufBD family protein ABCI9 (ABC transporter I family member 9) (ABC transporter ABCI.9) (AtABCI9) Was originally (PubMed:18299247) thought to belong to the ABC transporter family. Lacks the conserved ABC domain, which is one of the features of the ABC transporter family. {ECO:0000305|PubMed:18299247}. degenerate-domain Q06429 ACS1 Arabidopsis thaliana (Mouse-ear cress) 3702 1-aminocyclopropane-1-carboxylate synthase-like protein 1 Lacks the conserved tripeptide Ser/Thr-Asn-Pro in position 205 necessary for the ACS activity. {ECO:0000305}. degenerate-domain Q9SSC9 AHP6 Arabidopsis thaliana (Mouse-ear cress) 3702 Pseudo histidine-containing phosphotransfer protein 6 (Histidine-containing phosphotransfer protein 6) Lacks the conserved active histidine at position 83 that mediates the phosphotransfer. Shows a conserved HPt domain that may have some alternative degenerated phosphorelay role in cell signaling. {ECO:0000305}. degenerate-domain Q9M2B4 AL3 Arabidopsis thaliana (Mouse-ear cress) 3702 PHD finger protein ALFIN-LIKE 3 (Protein AL3) Lacks the Tyr (here Asp-204), a conserved feature of the aromatic cage required for the interaction with histone H3K4me3/2. {ECO:0000305}. degenerate-domain Q9ZUT3 ALS3 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein ALUMINUM SENSITIVE 3 (ABC transporter I family member 16) (ABC transporter ABCI.16) (AtABCI16) (ybbM homolog protein) Was originally (PubMed:18299247) thought to belong to the ABC transporter family. Lacks the conserved ABC domain, which is one of the features of the ABC transporter family. {ECO:0000305|PubMed:18299247}. degenerate-domain Q6LA43 APRR2 Arabidopsis thaliana (Mouse-ear cress) 3702 Two-component response regulator-like APRR2 (Pseudo-response regulator 2) (TOC2 protein) Lacks the phospho-accepting Asp (here Glu-76), present in the receiver domain, which is one of the conserved features of the two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q9LVG4 APRR3 Arabidopsis thaliana (Mouse-ear cress) 3702 Two-component response regulator-like APRR3 (Pseudo-response regulator 3) Lacks the phospho-accepting Asp (here Glu-116), present in the receiver domain, which is one of the conserved features of two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q9FJ16 APRR4 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative two-component response regulator-like APRR4 (Pseudo-response regulator 4) Lacks the phospho-accepting Asp (here Gln-94), present in the receiver domain, which is one of the conserved features of the two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q6LA42 APRR5 Arabidopsis thaliana (Mouse-ear cress) 3702 Two-component response regulator-like APRR5 (Pseudo-response regulator 5) Lacks the phospho-accepting Asp (here Glu-102), present in the receiver domain, which is one of the conserved features of two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q9C9F6 APRR6 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative two-component response regulator-like APRR6 (Pseudo-response regulator 6) Lacks the phospho-accepting Asp (here Asn-65), present in the receiver domain, which is one of the conserved features of the two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q93WK5 APRR7 Arabidopsis thaliana (Mouse-ear cress) 3702 Two-component response regulator-like APRR7 (Pseudo-response regulator 7) Lacks the phospho-accepting Asp (here Glu-130), present in the receiver domain, which is one of the conserved features of two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain O23100 APRR8 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative two-component response regulator-like APRR8 (Pseudo-response regulator 8) Lacks the phospho-accepting Asp (here Glu-66), present in the receiver domain, which is one of the conserved features of two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q8L500 APRR9 Arabidopsis thaliana (Mouse-ear cress) 3702 Two-component response regulator-like APRR9 (Pseudo-response regulator 9) Lacks the phospho-accepting Asp (here Glu-89), present in the receiver domain, which is one of the conserved features of two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q949V6 ARI1 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable E3 ubiquitin-protein ligase ARI1 (EC 2.3.2.31) (ARIADNE-like protein ARI1) (Protein ariadne homolog 1) (RING-type E3 ubiquitin transferase ARI1) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q84RQ9 ARI12 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable E3 ubiquitin-protein ligase ARI12 (EC 2.3.2.31) (ARIADNE-like protein ARI12) (Protein ariadne homolog 12) (RING-type E3 ubiquitin transferase ARI12) Lacks two Cys residues in the IBR-type zinc finger domain and two Cys residues in the RING-type zinc finger domain 2 that are conserved features of the family. {ECO:0000305}. degenerate-domain Q9FFN9 ARI13 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable E3 ubiquitin-protein ligase ARI13 (EC 2.3.2.31) (ARIADNE-like protein ARI13) (Protein ariadne homolog 13) (RING-type E3 ubiquitin transferase ARI13) Lacks two Cys residues in the RING-type zinc finger domain 2 that are conserved features of the family. {ECO:0000305}. degenerate-domain Q9FFP1 ARI14 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable E3 ubiquitin-protein ligase ARI14 (EC 2.3.2.31) (ARIADNE-like protein ARI14) (Protein ariadne homolog 14) (RING-type E3 ubiquitin transferase ARI14) Lacks four Cys residues in the RING-type zinc finger domain 1 and two Cys residues in the RING-type zinc finger domain 2 that are conserved features of the family. {ECO:0000305}. degenerate-domain Q84RQ8 ARI15 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable E3 ubiquitin-protein ligase ARI15 (EC 2.3.2.31) (ARIADNE-like protein ARI15) (Protein ariadne homolog 15) (RING-type E3 ubiquitin transferase ARI15) Lacks two Cys residues in the RING-type zinc finger domain 2 that are conserved features of the family. {ECO:0000305}. degenerate-domain Q9C5A4 ARI16 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable E3 ubiquitin-protein ligase ARI16 (EC 2.3.2.31) (ARIADNE-like protein ARI16) (Protein ariadne homolog 16) (RING-type E3 ubiquitin transferase ARI16) Lacks three Cys residues in the RING-type zinc finger domain 1 and two Cys residues in the RING-type zinc finger domain 2 that are conserved features of the family. {ECO:0000305}. degenerate-domain Q84RR2 ARI2 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable E3 ubiquitin-protein ligase ARI2 (EC 2.3.2.31) (ARIADNE-like protein ARI2) (Protein ariadne homolog 2) (RING-type E3 ubiquitin transferase ARI2) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q9LVX0 ARI3 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable E3 ubiquitin-protein ligase ARI3 (EC 2.3.2.31) (ARIADNE-like protein ARI3) (Protein ariadne homolog 3) (RING-type E3 ubiquitin transferase ARI3) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q9LJL6 ATL62 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative RING-H2 finger protein ATL62 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase ATL62) Lacks one cysteine (here Phe-106), present in the RING domain, which is one of the conserved features of the RING-type zinc finger family. {ECO:0000305}.; degenerate-domain Q9FM68 BAM4 Arabidopsis thaliana (Mouse-ear cress) 3702 Inactive beta-amylase 4, chloroplastic (Inactive beta-amylase 6) In contrast to other members of the family, lacks the conserved Glu active site in position 473, which is replaced by an Arg residue, explaining why it is inactive. {ECO:0000305}. degenerate-domain Q8VYW2 BAM9 Arabidopsis thaliana (Mouse-ear cress) 3702 Inactive beta-amylase 9 (1,4-alpha-D-glucan maltohydrolase) (Inactive beta-amylase 3) In contrast to other members of the family, lacks the conserved Glu active site in position 449, which is replaced by a Gln residue, suggesting it is inactive. {ECO:0000305}. degenerate-domain O82772 BGLU25 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive beta-glucosidase 25 (AtBGLU25) Lacks the conserved Glu residue involved in nucleophilic attack and essential for hydrolase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain P93280 CCMB Arabidopsis thaliana (Mouse-ear cress) 3702 Putative cytochrome c biogenesis ccmB-like mitochondrial protein (ABC transporter I family member 2) (ABC transporter ABCI.2) (AtABCI2) Was originally (PubMed:18299247) thought to belong to the ABC transporter family. Lacks the conserved ABC domain, which is one of the features of the ABC transporter family. {ECO:0000305|PubMed:18299247}. degenerate-domain P92527 CCMC Arabidopsis thaliana (Mouse-ear cress) 3702 Putative cytochrome c biosynthesis ccmC-like mitochondrial protein (ABC transporter I family member 3) (ABC transporter ABCI.3) (AtABCI3) Was originally (PubMed:18299247) thought to belong to the ABC transporter family. Lacks the conserved ABC domain, which is one of the features of the ABC transporter family. {ECO:0000305|PubMed:18299247}. degenerate-domain Q9S7S2 CDA4 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive cytidine deaminase 4 Lacks part of the deaminase domain and the catalytically essential zinc-binding residues. It is therefore most likely inactive. {ECO:0000305}. degenerate-domain Q9S789 CDA9 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive cytidine deaminase 9 Lacks the conserved Glu active site which is replaced by Gly. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain F4JVJ1 CLPB2 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative chaperone protein ClpB2, chloroplastic (ATP-dependent Clp protease ATP-binding subunit ClpB homolog 2) (Casein lytic proteinase B2) Lacks the C-terminal domain, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain Q9SJ61 CPK25 Arabidopsis thaliana (Mouse-ear cress) 3702 Calcium-dependent protein kinase 25 (EC 2.7.11.1) Lacks two EF-hand domains in the calmodulin-like domain, which are conserved features of the CDPK ubfamily. {ECO:0000305}. degenerate-domain O65469 CRK9 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative cysteine-rich receptor-like protein kinase 9 (Cysteine-rich RLK9) Lacks the transmembrane and the protein kinase domains, which are conserved features of the CRK subfamily. {ECO:0000305}.; degenerate-domain Q9LRL0 CRRSP27 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative cysteine-rich repeat secretory protein 27 Lacks the Cys (here Ser-215), present in the DUF26 domain, which is one of the conserved features of the cysteine-rich repeat secretory protein family. {ECO:0000305}.; degenerate-domain Q8LDI5 CXXS1 Arabidopsis thaliana (Mouse-ear cress) 3702 Thioredoxin-like protein CXXS1 (AtCXXS1) (Mono-cysteine thioredoxin 1) Lacks the conserved cysteine (here Ser-39), present in the redox-active center, which is one of the conserved features of the thioredoxin family. {ECO:0000305}. degenerate-domain Q8GXV2 CXXS2 Arabidopsis thaliana (Mouse-ear cress) 3702 Thioredoxin-like protein CXXS2 (AtCXXS2) (Mono-cysteine thioredoxin 2) Lacks the conserved cysteine (here Ser-77), present in the redox-active center, which is one of the conserved features of the thioredoxin family. {ECO:0000305}. degenerate-domain Q3E8B4 DEGP15 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative Do-like 15 protein Lacks the conserved Asp residue in position 117 essential for protease activity. {ECO:0000305}. degenerate-domain Q8RY22 DEGP7 Arabidopsis thaliana (Mouse-ear cress) 3702 Protease Do-like 7 (EC 3.4.21.-) Lacks the conserved Asp residue in position 654 essential for protease activity. {ECO:0000305}. degenerate-domain Q8H1E8 DRM3 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive DNA (cytosine-5)-methyltransferase DRM3 (Protein DOMAINS REARRANGED METHYLTRANSFERASE 3) Lacks the conserved tripeptide Ser-Pro-Cys in position 672 necessary for the methyltransferase activity in DRM protein (AC Q9M548). degenerate-domain Q9ZP56 DRP4A Arabidopsis thaliana (Mouse-ear cress) 3702 Putative dynamin-related protein 4A Could be the product of a pseudogene. Lacks the GED domain, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain Q56XC2 EDA21 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 37 (Protein EMBRYO SAC DEVELOPMENT ARREST 21) Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain O22993 FTSHI1 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive ATP-dependent zinc metalloprotease FTSHI 1, chloroplastic (AtFTSHI1) (Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 1) (Protein ARC1) (Protein FTSH INACTIVE PROTEASE 1) Lacks the conserved zinc-binding motif HEXXH, which presumably renders it inactive for proteolysis. {ECO:0000303|PubMed:14996218}. degenerate-domain A8MPR5 FTSHI2 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic (AtFTSHI2) (Protein EMBRYO DEFECTIVE 2083) (Protein FTSH INACTIVE PROTEASE 2) Lacks the conserved zinc-binding motif HEXXH, which presumably renders it inactive for proteolysis. {ECO:0000303|PubMed:14996218}. degenerate-domain Q9M895 FTSHI3 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive ATP-dependent zinc metalloprotease FTSHI 3, chloroplastic (AtFTSHI3) (Protein FTSH INACTIVE PROTEASE 3) Lacks the conserved zinc-binding motif HEXXH, which presumably renders it inactive for proteolysis. {ECO:0000303|PubMed:14996218}. degenerate-domain F4KF14 FTSHI4 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive ATP-dependent zinc metalloprotease FTSHI 4, chloroplastic (AtFTSHI4) (Protein EMBRYO DEFECTIVE 3144) (Protein FTSH INACTIVE PROTEASE 4) Lacks the conserved zinc-binding motif HEXXH, which presumably renders it inactive for proteolysis. {ECO:0000303|PubMed:14996218}. degenerate-domain F4J3N2 FTSHI5 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive ATP-dependent zinc metalloprotease FTSHI 5, chloroplastic (AtFTSHI5) (Protein EMBRYO DEFECTIVE 2458) (Protein FTSH INACTIVE PROTEASE 5) Lacks the conserved zinc-binding motif HEXXH, which presumably renders it inactive for proteolysis. {ECO:0000305}. degenerate-domain Q8W4H8 GLL23 Arabidopsis thaliana (Mouse-ear cress) 3702 Inactive GDSL esterase/lipase-like protein 23 (GDSL-like lipase 23) (Probable myrosinase-associated protein GLL23) Lacks the conserved active site 'GDSL' motif. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain F4KHL6 HIPP10 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 10 (AtHIP10) Contains an apparent HMA-like domain but lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain Q9LTE4 HIPP11 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 11 (AtHIP11) Contains an apparent HMA-like domain but lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain Q9LTE3 HIPP12 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 12 (AtHIP12) Contains an apparent HMA-like domain but lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain Q9LTE2 HIPP13 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 13 (AtHIP13) Contains an apparent HMA-like domain but lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain Q9LTE1 HIPP14 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 14 (AtHIP14) Contains an apparent HMA-like domain but lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain Q9CAK6 HIPP15 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 15 (AtHIP15) The HMA domain lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain Q9SSF0 HIPP16 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 16 (AtHIP16) (Farnesylated protein 4) (AtFP4) Contains an apparent HMA-like domain but lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain Q9FVS0 HIPP17 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 17 (AtHIP17) The HMA domain lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain Q9T0K9 HIPP18 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 18 (AtHIP18) (Protein maternal effect embryo arrest 56) The HMA domain lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain O03982 HIPP39 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 39 (AtHIP39) The HMA domain lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain Q9CAV5 HIPP42 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 42 (AtHIP42) The HMA domain lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain Q5PNZ7 HIPP46 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 46 (AtHIP46) (Farnesylated protein 5) (AtFP5) Contains an apparent HMA-like domain but lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain F4JDJ0 HIPP47 Arabidopsis thaliana (Mouse-ear cress) 3702 Heavy metal-associated isoprenylated plant protein 47 (AtHIP47) Contains an apparent HMA-like domain but lacks the core conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}. degenerate-domain O48722 HO2 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive heme oxygenase 2, chloroplastic (AtHO2) Lacks the conserved His residue involved in heme iron binding and essential for heme oxygenase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9LQK9 IDH4 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative isocitrate dehydrogenase [NAD] subunit-like 4 (IDH-IV) (Isocitric dehydrogenase-like protein 4) (NAD(+)-specific ICDH 4) Lacks the isocitrate binding site which is one of the conserved features of the isocitrate dehydrogenase family. {ECO:0000305}.; degenerate-domain Q8L7T6 JMJ19 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive lysine-specific demethylase JMJ19 (Jumonji domain-containing protein 19) (AtJMJ19) (Protein JUMONJI 19) Lacks the 2 conserved His residues involved in iron binding and essential for dioxygenase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9XFR0 KCO3 Arabidopsis thaliana (Mouse-ear cress) 3702 Potassium inward rectifier (Kir)-like channel 3 (AtKCO3) KCO3 shares similarity to the TPK family (2P/4TM) but lacks the conserved internal part including one pore-forming region and two transmembrane segments. As a result and according to its structure, KCO3 could also be classified as a member of the IRK family (1P/2TM). {ECO:0000305}. degenerate-domain P82757 LCR42 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 187 (Putative low-molecular-weight cysteine-rich protein 42) (Protein LCR42) Could be the product of a pseudogene. Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q4VP09 LURE1.1 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein LURE 1.1 (AtLURE1.1) (Cysteine-Rich Peptide 810_1.1) (CRP810_1.1) (Defensin-like protein 217) Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q4VP08 LURE1.2 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein LURE 1.2 (AtLURE1.2) (Cysteine-Rich Peptide 810_1.2) (CRP810_1.2) (Defensin-like protein 213) Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q4VP10 LURE1.3 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein LURE 1.3 (AtLURE1.3) (Cysteine-Rich Peptide 810_1.3) (CRP810_1.3) (Defensin-like protein 214) Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain P0CAY6 LURE1.4 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein LURE 1.4 (AtLURE1.4) (Cysteine-Rich Peptide 810_1.4) (CRP810_1.4) (Defensin-like protein 216) Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain A8MRC6 LURE1.5 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein LURE 1.5 (AtLURE1.5) (Cysteine-Rich Peptide 810_1.5) (CRP810_1.5) (Defensin-like protein 212) Lacks 2 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q4VP07 LURE1.6 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein LURE 1.6 (AtLURE1.6) (Cysteine-Rich Peptide 810_1.6) (CRP810_1.6) (Defensin-like protein 215) Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain F4JRA6 MES20 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative inactive methylesterase 20 (AtMES20) (Protein MATERNAL EFFECT EMBRYO ARREST 69) Could be the product of a pseudogene. The protein is truncated and lacks two of the residues of the predicted catalytic triad, suggesting that it does not have this enzymatic activity. {ECO:0000305}. degenerate-domain F4K494 MOB2B Arabidopsis thaliana (Mouse-ear cress) 3702 Putative MOB kinase activator-like 2B (Mob1 homolog 2B) (Mps one binder kinase activator-like 2B) Could be the product of a pseudogene. Lacks two of the four zinc-binding sites, which are conserved features of the MOB1/phocein family. {ECO:0000305}. degenerate-domain Q9ZU25 MPPalpha1 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable mitochondrial-processing peptidase subunit alpha-1, mitochondrial (Alpha-MPP 1) (Complex III subunit II) (Core protein II) (Cytochrome b-c1 complex subunit 2-1, mitochondrial) (Inactive zinc metalloprotease alpha-1) (Ubiquinol-cytochrome c oxidoreductase core protein 2-1) Does not seem to have a protease activity as it lacks one of the conserved zinc-binding sites. {ECO:0000305}. degenerate-domain O04308 MPPalpha2 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable mitochondrial-processing peptidase subunit alpha-2, chloroplastic/mitochondrial (Alpha-MPP 2) (Complex III subunit II) (Core protein II) (Cytochrome b-c1 complex subunit 2-2, mitochondrial) (Inactive zinc metalloprotease alpha-2) (Ubiquinol-cytochrome c oxidoreductase core protein 2-2) Does not seem to have a protease activity as it lacks one of the conserved zinc-binding sites. {ECO:0000305}. degenerate-domain Q9LXD4 MRS2-9 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative magnesium transporter MRS2-9 Could be the product of a pseudogene. Lacks the GMN motif, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain Q7XA74 MVP1 Arabidopsis thaliana (Mouse-ear cress) 3702 Inactive GDSL esterase/lipase-like protein 25 (GDSL-like lipase 25) (Myrosinase-associated protein GLL25) (Protein ENDOPLASMIC RETICULUM MORPHOLOGY 3) (Protein GOLGI DEFECTS 36) (Protein MODIFIED VACUOLE PHENOTYPE 1) (Protein NUCLEAR CAGE) Lacks the conserved active site 'GDSL' motif and has no lipase activity. {ECO:0000305}. degenerate-domain Q8LNP3 OFUT10 Arabidopsis thaliana (Mouse-ear cress) 3702 O-fucosyltransferase 10 (O-FucT-10) (EC 2.4.1.-) (O-fucosyltransferase family protein) Lacks the transmembrane domain, which is one of the conserved feature of the family. {ECO:0000305}. degenerate-domain F4HT49 PAB1 Arabidopsis thaliana (Mouse-ear cress) 3702 Polyadenylate-binding protein 1 (PABP-1) (Poly(A)-binding protein 1) Lacks the PABC domain, which is one of the conserved features of the PAPB family. {ECO:0000305}. degenerate-domain O04319 PAB6 Arabidopsis thaliana (Mouse-ear cress) 3702 Polyadenylate-binding protein 6 (PABP-6) (Poly(A)-binding protein 6) Lacks the PABC domain, which is one of the conserved features of the PAPB family. {ECO:0000305}. degenerate-domain Q9LMX4 PAP1 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive purple acid phosphatase 1 Lacks the conserved His residue essential for phosphatase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q84LR6 PAP14 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive purple acid phosphatase 14 Lacks the conserved His residue essential for phosphatase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9SR79 PAP16 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive purple acid phosphatase 16 Lacks the conserved His residue essential for phosphatase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9LMG7 PAP2 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive purple acid phosphatase 2 Lacks the conserved His residue essential for phosphatase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q8H1R2 PAP24 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive purple acid phosphatase 24 Lacks the conserved His residue essential for phosphatase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q5MAU8 PAP27 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive purple acid phosphatase 27 Lacks the conserved His residue essential for phosphatase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9LU72 PAP28 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive purple acid phosphatase 28 Lacks the conserved His residue essential for phosphatase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9FMK9 PAP29 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive purple acid phosphatase 29 Lacks the conserved His residue essential for phosphatase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9ZQ81 PAP9 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive purple acid phosphatase 9 Lacks the conserved His residue essential for phosphatase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain O80446 PDX1L4 Arabidopsis thaliana (Mouse-ear cress) 3702 Pyridoxal 5'-phosphate synthase PDX1-like 4 Although its N-terminus is strongly related to pyridoxal 5'-phosphate synthase PDX1 subunits (PDX1), it is much shorter and probably not functional. {ECO:0000305}. degenerate-domain O22862 PER26 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable peroxidase 26 (Atperox P26) (EC 1.11.1.7) (ATP50) Lacks the distal histidine (here Ser-77), present in the active site, which is one of the conserved features of the classical plant (class III) peroxidase family. {ECO:0000305}. degenerate-domain Q9FLV5 PER61 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable peroxidase 61 (Atperox P61) (EC 1.11.1.7) Lacks the distal histidine (here Ser-77), present in the active site, which is one of the conserved features of the classical plant (class III) peroxidase family. {ECO:0000305}. degenerate-domain Q9LT91 PER66 Arabidopsis thaliana (Mouse-ear cress) 3702 Peroxidase 66 (Atperox P66) (EC 1.11.1.7) (ATP27a) Lacks one of the disulfide bridges highly conserved in the class III peroxidase family. {ECO:0000305}. degenerate-domain Q9SV43 PLP7 Arabidopsis thaliana (Mouse-ear cress) 3702 Patatin-like protein 7 (AtPLP7) (EC 3.1.1.-) (Patatin-related phospholipase A IIIbeta) (pPLAIIIb) (Phospholipase A IIIA) (AtPLAIIIA) Lacks the conserved Asp residue expected to act as the active site proton acceptor. {ECO:0000305}. degenerate-domain Q8H133 PLP8 Arabidopsis thaliana (Mouse-ear cress) 3702 Patatin-like protein 8 (AtPLP8) (EC 3.1.1.-) (Patatin-related phospholipase A IIIgamma) (pPLAIIIg) (Phospholipase A IVD) (AtPLAIVD) Lacks the conserved Asp residue expected to act as the active site proton acceptor. {ECO:0000305}. degenerate-domain Q93ZQ3 PLP9 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive patatin-like protein 9 (AtPLP9) (Patatin-related phospholipase A IIIdelta) (pPLAIIId) (Phospholipase A IIIB) (AtPLAIIIB) Lacks the conserved Ser residue involved in nucleophilic attack and essential for hydrolase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain O81320 PME38 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative pectinesterase/pectinesterase inhibitor 38 [Includes: Pectinesterase inhibitor 38 (Pectin methylesterase inhibitor 38); Pectinesterase 38 (PE 38) (EC 3.1.1.11) (Pectin methylesterase 38) (AtPME38)] Lacks the conserved signal peptide, which is one of the features of the pectinesterase family. {ECO:0000305}. degenerate-domain F4J264 PRFB3 Arabidopsis thaliana (Mouse-ear cress) 3702 Peptide chain release factor PrfB3, chloroplastic (AtPrfB3) Lacks the stop codon recognition motif 'SPF' and the catalytic center 'GGQ' for peptidyl-tRNA hydrolysis, which are two conserved features of the family. {ECO:0000305|PubMed:21771930}. degenerate-domain Q3ED99 PUP9 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative purine permease 9 Could be the product of a pseudogene. Truncated purine permease that is probably not expressed. {ECO:0000269|PubMed:27701112}. degenerate-domain Q8RY59 RCD1 Arabidopsis thaliana (Mouse-ear cress) 3702 Inactive poly [ADP-ribose] polymerase RCD1 (Protein RADICAL-INDUCED CELL DEATH 1) Lacks the conserved catalytic triad His-Tyr-Glu of the active site. {ECO:0000305}. degenerate-domain Q9FZ92 RH44 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative DEAD-box ATP-dependent RNA helicase 44 (EC 3.6.4.13) Lacks the conserved Q motif, which is one of the features of the DEAD box helicase family. {ECO:0000305}.; degenerate-domain F4HTV6 RLP16 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative receptor-like protein 16 (AtRLP16) Could be the product of a pseudogene. Lacks the signal peptide and the transmembrane domain, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q9ZUK7 RLP18 Arabidopsis thaliana (Mouse-ear cress) 3702 Receptor-like protein 18 (AtRLP18) Lacks the signal peptide, which is a conserved feature of the gene family. {ECO:0000305}. degenerate-domain O48763 RLP25 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative receptor like protein 25 (AtRLP25) Could be the product of a pseudogene. Lacks the signal peptide and part of the extracellular leucine-rich repeats that are required for the specificity of the elicitor protein recognition, which are conserved features of the family. {ECO:0000305}. degenerate-domain Q9SLI6 RLP8 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative receptor-like protein 8 (AtRLP8) Could be the product of a pseudogene. In strain cv. Columbia, a naturally occurring variation results in the deletion of 35 amino acids in the middle part of the protein. Lacks part of the extracellular leucine-rich repeats that are required for the specificity of the elicitor protein recognition. {ECO:0000305}. degenerate-domain P0DKH3 RNR2B Arabidopsis thaliana (Mouse-ear cress) 3702 Ribonucleoside-diphosphate reductase small chain B (EC 1.17.4.1) (Ribonucleoside-diphosphate reductase R2B subunit) (Ribonucleotide reductase small subunit B) In cv. Columbia, could be the product of a pseudogene (AC P0DKH2) due to a frameshift in position 140. The resulting shorter protein lacks the conserved features of the family. {ECO:0000305}. degenerate-domain P0DKH2 RNR2B Arabidopsis thaliana (Mouse-ear cress) 3702 Putative ribonucleoside-diphosphate reductase small chain B (Ribonucleoside-diphosphate reductase R2B subunit) (Ribonucleotide reductase small subunit B) Could be the product of a pseudogene. In strain cv. Columbia, a frameshift at position 140 results in a truncated RNR2B protein. The resulting sequence lacks the conserved features of the family. A second start codon could potentially direct the translational initiation of a second peptide homologous with TSO2 (AC Q9LSD0) at residues 141 to 332. A complete sequence for a functional RNR2B can be found in strain cv. Landsberg erecta (AC P0DKH3). {ECO:0000305}. degenerate-domain Q2V2T9 SCL16 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative scarecrow-like protein 16 (AtSCL16) Lacks the VHIID motif which is one of the conserved features of the GRAS family. {ECO:0000305}.; degenerate-domain Q8S8P0 SCPL52 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative serine carboxypeptidase-like 52 Lacks the first part of the protein and the active site Ser residue which is a conserved feature of peptidase S10 family. {ECO:0000305}.; degenerate-domain Q9LXY6 SCPL53 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative serine carboxypeptidase-like 53 Lacks the second part of the protein and the active site Asp and His residues which is a conserved feature of peptidase S10 family. {ECO:0000305}.; degenerate-domain Q9FFB2 SCPL54 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative serine carboxypeptidase-like 54 Lacks the second part of the protein and the active site Asp and His residues which is a conserved feature of peptidase S10 family. {ECO:0000305}.; degenerate-domain P82620 SCRL1 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 225 (Putative S locus cysteine-rich-like protein 1) (Protein SCRL1) (SCR-like protein 1) Could be the product of a pseudogene. Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain P82645 SCRL26 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative defensin-like protein 235 (Putative S locus cysteine-rich-like protein 26) (Protein SCRL26) (SCR-like protein 26) Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. {ECO:0000305}. degenerate-domain F4I313 SCYL2A Arabidopsis thaliana (Mouse-ear cress) 3702 SCY1-like protein 2 A (Inactive protein kinase SCYL2A) Although it belongs to the kinase superfamily, lacks the residues involved in ATP binding, suggesting that it has no protein kinase activity. {ECO:0000305}. degenerate-domain Q9C9H8 SCYL2B Arabidopsis thaliana (Mouse-ear cress) 3702 SCY1-like protein 2 B (Inactive protein kinase SCYL2B) Although it belongs to the kinase superfamily, lacks the residues involved in ATP binding, suggesting that it has no protein kinase activity. {ECO:0000305}. degenerate-domain Q93WE4 SINAT6 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive E3 ubiquitin-protein ligase SINAT6 (Protein SEVEN IN ABSENTIA 2) (Seven in absentia homolog 6) Lacks the RING-type zinc finger domain that is essential for ubiquitin ligase activity. May not possess E3 ubiquitin-protein ligase activity by itself. {ECO:0000305|PubMed:24350984}. degenerate-domain Q9LW20 SKL1 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive shikimate kinase like 1, chloroplastic (AtSKL1) SKL1 does not possess shikimate kinase activity in vitro probably because it lacks the conserved active sites and substrate binding sites of the shikimate kinase family. {ECO:0000305|PubMed:19057671}. degenerate-domain O82290 SKL2 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive shikimate kinase like 2, chloroplastic (AtSKL2) SKL2 does not possess shikimate kinase activity in vitro probably because it lacks the conserved active sites and substrate binding sites of the shikimate kinase family. {ECO:0000305|PubMed:19057671}. degenerate-domain Q9S850 SOX Arabidopsis thaliana (Mouse-ear cress) 3702 Sulfite oxidase (EC 1.8.3.1) (Moco-containing protein AtMCP) (At-SO) (AtSOX) Lacks the conserved cytochrome b5 heme-binding domain present in other sulfite oxidases. {ECO:0000305}. degenerate-domain O82491 SPT16 Arabidopsis thaliana (Mouse-ear cress) 3702 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain O82289 SRO1 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive poly [ADP-ribose] polymerase SRO1 (Protein SIMILAR TO RCD ONE 1) Lacks the conserved catalytic triad His-Tyr-Glu of the active site. {ECO:0000305}. degenerate-domain Q9ZUD9 SRO2 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive poly [ADP-ribose] polymerase SRO2 (Protein SIMILAR TO RCD ONE 2) Lacks the conserved catalytic triad His-Tyr-Glu of the active site. {ECO:0000305}. degenerate-domain O64592 SRO3 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive poly [ADP-ribose] polymerase SRO3 (Protein SIMILAR TO RCD ONE 3) Lacks the conserved catalytic triad His-Tyr-Glu of the active site. {ECO:0000305}. degenerate-domain Q9STU1 SRO4 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive poly [ADP-ribose] polymerase SRO4 (Protein SIMILAR TO RCD ONE 4) Lacks the conserved catalytic triad His-Tyr-Glu of the active site. {ECO:0000305}. degenerate-domain Q9FJJ3 SRO5 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable inactive poly [ADP-ribose] polymerase SRO5 (Protein SIMILAR TO RCD ONE 5) Lacks the conserved catalytic triad His-Tyr-Glu of the active site. {ECO:0000305}. degenerate-domain Q3EC60 SUVH10 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative inactive histone-lysine N-methyltransferase family member SUVH10 (Histone H3-K9 methyltransferase 10) (H3-K9-HMTase 10) (Protein SET DOMAIN GROUP 11) (Suppressor of variegation 3-9 homolog protein 10) (Su(var)3-9 homolog protein 10) The S-adenosyl-L-methionine binding sites are not conserved, suggesting that this protein lacks methyltransferase activity. Likewise, the zinc-binding Cys residues in the pre-SET domain are only partially conserved. {ECO:0000305}. degenerate-domain Q8L4R0 TGD1 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein TRIGALACTOSYLDIACYLGLYCEROL 1, chloroplastic (ABC transporter I family member 14) (ABC transporter ABCI.14) (AtABCI14) Was originally (PubMed:18299247) thought to belong to the ABC transporter family. Lacks the conserved ABC domain, which is one of the features of the ABC transporter family. {ECO:0000305|PubMed:18299247}. degenerate-domain Q9LTR2 TGD2 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein TRIGALACTOSYLDIACYLGLYCEROL 2, chloroplastic (ABC transporter I family member 15) (ABC transporter ABCI.15) (AtABCI15) Was originally (PubMed:18299247) thought to belong to the ABC transporter family. Lacks the conserved ABC domain, which is one of the features of the ABC transporter family. {ECO:0000305|PubMed:18299247}. degenerate-domain Q9SSN3 TIR Arabidopsis thaliana (Mouse-ear cress) 3702 Toll/interleukin-1 receptor-like protein (AtTIR) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain P82281 TL29 Arabidopsis thaliana (Mouse-ear cress) 3702 Thylakoid lumenal 29 kDa protein, chloroplastic (TL29) (EC 1.-.-.-) (AtAPx07) (P29) (Probable L-ascorbate peroxidase 4) Was originally thought to be an ascorbate peroxidase (PubMed:12068123, PubMed:16034597). PubMed:19828564 fails to show any peroxidase activity associated with TL29 and demonstrates that TL29 could bind neither heme nor ascorbate. TL29 lacks the heme-binding site, the proton acceptor and the transition state stabilizer, which are conserved features of the ascorbate peroxidase. {ECO:0000305|PubMed:12068123, ECO:0000305|PubMed:16034597}. degenerate-domain P0CJ42 TPS02 Arabidopsis thaliana (Mouse-ear cress) 3702 Putative inactive (E)-beta-ocimene synthase, chloroplastic (Inactive (E,E)-alpha-farnesene synthase) (Inactive terpenoid synthase 2) (AtTPS02) Could be the product of a pseudogene. In strain cv. Columbia, a naturally frameshift at position 65 results in a truncated TPS02 protein. Lacks the conserved active sites, suggesting that it has no terpenoid synthase activity. A complete sequence for TPS02 can be found in strain cv. Wassilewskija (AC P0CJ43). {ECO:0000305}. degenerate-domain Q8RY67 WAKL14 Arabidopsis thaliana (Mouse-ear cress) 3702 Wall-associated receptor kinase-like 14 (EC 2.7.11.-) Lacks the calcium-binding EGF-like domain which is a conserved feature of the wall-associated receptor kinase family. {ECO:0000305}. degenerate-domain Q9M342 WAKL15 Arabidopsis thaliana (Mouse-ear cress) 3702 Wall-associated receptor kinase-like 15 (EC 2.7.11.-) Lacks the calcium-binding EGF-like domain which is a conserved feature of the wall-associated receptor kinase family. {ECO:0000305}. degenerate-domain Q9LZM4 WAKL20 Arabidopsis thaliana (Mouse-ear cress) 3702 Wall-associated receptor kinase-like 20 (EC 2.7.11.-) Lacks the calcium-binding EGF-like domain which is a conserved feature of the wall-associated receptor kinase family. {ECO:0000305}. degenerate-domain Q8GYF5 WAKL21 Arabidopsis thaliana (Mouse-ear cress) 3702 Wall-associated receptor kinase-like 21 (EC 2.7.11.-) Lacks the calcium-binding EGF-like domain which is a conserved feature of the wall-associated receptor kinase family. {ECO:0000305}. degenerate-domain Q9SMP1 XTH11 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable xyloglucan endotransglucosylase/hydrolase protein 11 (At-XTH11) (XTH-11) (EC 2.4.1.207) In contrast to other xyloglucan endotransglucosylase proteins, the catalytic motif is atypical and lacks the proton donor site. It therefore may not be functional in vivo. {ECO:0000305}. degenerate-domain P62113 psbN Arabidopsis thaliana (Mouse-ear cress) 3702 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A4QK46 psbN Arabis hirsuta (Hairy rock-cress) (Turritis hirsuta) 78191 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain O29165 cdhA1 Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16) 224325 Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 (ACDS complex subunit alpha 1) (EC 1.2.7.4) (ACDS complex carbon monoxide dehydrogenase subunit alpha 1) (ACDS CODH subunit alpha 1) This protein lacks the conserved Cys in positions 65 and 69; they are replaced by a Gln and an Asn, respectively. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form heterotetramers. {ECO:0000305}. degenerate-domain O28429 cooS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16) 224325 Carbon monoxide dehydrogenase (CODH) (EC 1.2.7.4) This protein lacks the conserved Cys in positions 48 and 292; they are replaced by a Ser and a Glu, respectively. It is therefore possible that the C- and D-clusters are either altered or missing in this protein, which may not form homodimers. {ECO:0000305}. degenerate-domain Q6EYL4 psbN Aristolochia macrophylla (Dutchman's pipe vine) (Isotrema macrophyllum) 12949 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain D4B5D4 Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) 663331 Cell surface Cu-only superoxide dismutase ARB_03674 (EC 1.15.1.1) Although the beta-barrel of Cu/Zn SODs is largely preserved, SOD5 is a monomeric copper protein that lacks a zinc-binding site and is missing the electrostatic loop element proposed to promote catalysis through superoxide guidance. Without an electrostatic loop, the copper site of SOD5 is not recessed and is readily accessible to bulk solvent. {ECO:0000250|UniProtKB:Q5AD07}. degenerate-domain D4AKU7 ECM14 Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) 663331 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 512 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain E4UPZ6 ECM14 Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum gypseum) 535722 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 512 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain C5FPR9 ECM14 Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) 554155 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 503 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q67HV0 psbN Asparagus officinalis (Garden asparagus) 4686 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9C4B1 abfB Aspergillus awamori (Black koji mold) 105351 Probable alpha-L-arabinofuranosidase B (ABF B) (Arabinosidase B) (EC 3.2.1.55) Lacks the conserved Asp residue in position 297 essential for alpha-L-arabinofuranosidase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain A1CSU3 ecm14 Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) 344612 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 488 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain A1DGH9 ecm14 Aspergillus fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Neosartorya fischeri) 331117 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 491 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain B8NBP9 ecm14 Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) 332952 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 482 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q4X1U0 ecm14 Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) 330879 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 490 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q4WHW1 png1 Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) 330879 Protein png1 Although strongly related to the peptide:N-glycanase enzyme, it lacks the conserved active site Cys in position 261, which is replaced by a Val residue suggesting that it has no activity. {ECO:0000305}. degenerate-domain Q4WJ02 spt16 Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) 330879 FACT complex subunit spt16 (Facilitates chromatin transcription complex subunit spt16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain B0XRS8 ecm14 Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) 451804 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 490 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain A2QN74 btgC Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) 425011 Putative glucan endo-1,3-beta-glucosidase btgC (EC 3.2.1.39) (Endo-1,3-beta-glucanase btgC) (Laminarinase btgC) Lacks the conserved Glu residue in position 619 essential for glucanase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain A2QZA2 ecm14 Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) 425011 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 487 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain A2QWT2 rhgD Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) 425011 Putative rhamnogalacturonase D (RGase D) (RHG D) (EC 3.2.1.-) Lacks the conserved His residue in position 290 essential for rhamnogalacturonase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q2TZK2 ecm14 Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) 510516 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 482 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q2UPS5 png1 Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) 510516 Protein png1 Although strongly related to the peptide:N-glycanase enzyme, it lacks the conserved active site Cys in position 259, which is replaced by a Val residue suggesting that it has no activity. {ECO:0000305}. degenerate-domain Q2UBF1 spt16 Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) 510516 FACT complex subunit spt16 (Facilitates chromatin transcription complex subunit spt16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q0C9B4 ecm14 Aspergillus terreus (strain NIH 2624 / FGSC A1156) 341663 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 485 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain P9WEK7 avaF Aspergillus versicolor 46472 Cytochrome P450 monooxygenase-like protein avaF (Ava biosynthesis cluster protein F) Lacks the heme-binding cysteine residue and therefore might not act as a functional cytochrome P450 monooxygenase. {ECO:0000305}. degenerate-domain P9WEL3 avaL Aspergillus versicolor 46472 Cytochrome P450 monooxygenase avaL (EC 1.-.-.-) (Ava biosynthesis cluster protein L) Lacks the heme-binding cysteine residue and therefore might not act as a functional cytochrome P450 monooxygenase. {ECO:0000305}. degenerate-domain P9WEL5 avaN Aspergillus versicolor 46472 Cytochrome P450 monooxygenase-like protein avaN (Ava biosynthesis cluster protein N) Lacks the heme-binding cysteine residue and therefore might not act as a functional cytochrome P450 monooxygenase. {ECO:0000305}. degenerate-domain Q2NJZ2 pheT Aster yellows witches'-broom phytoplasma (strain AYWB) 322098 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved glutamate residue in position 506 that binds magnesium; it is replaced by a serine residue. {ECO:0000305}. degenerate-domain P62115 psbN Atropa belladonna (Belladonna) (Deadly nightshade) 33113 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A0RZC6 Austrelaps superbus (Lowland copperhead snake) (Hoplocephalus superbus) 29156 A.superbus venom factor 2 (AVF-2) (CVF-like) (Complement C3 homolog) [Cleaved into: AVF-2 alpha chain; AVF-2 gamma chain; AVF-2 beta chain] Lacks the typical Cys at position 1000 required for the thioester bond formation. {ECO:0000305}. degenerate-domain P18785 hisH Azospirillum brasilense 192 Imidazole glycerol phosphate synthase subunit HisH (EC 4.3.2.10) (IGP synthase glutaminase subunit) (EC 3.5.1.2) (IGP synthase subunit HisH) (ImGP synthase subunit HisH) (IGPS subunit HisH) Compared to other HisH it lacks an internal segment that normally contains the Cys active site residue. {ECO:0000305}. degenerate-domain Q37896 15 Bacillus phage B103 (Bacteriophage B103) 2994042 Endolysin (EC 3.2.1.17) (Lysis protein) (Lysozyme) (Muramidase) (Protein p15) Lacks the conserved Asp active site. {ECO:0000255|HAMAP-Rule:MF_04110}. degenerate-domain P07540 15 Bacillus phage PZA (Bacteriophage PZA) 10757 Endolysin (EC 3.2.1.17) (Lysis protein) (Lysozyme) (Muramidase) (Protein p15) Lacks the conserved Asp active site. {ECO:0000255|HAMAP-Rule:MF_04110}. degenerate-domain P11187 15 Bacillus phage phi29 (Bacteriophage phi-29) 2884424 Endolysin (EC 3.2.1.17) (Lysis protein) (Lysozyme) (Muramidase) (Protein p15) Lacks the conserved Asp active site. {ECO:0000255|HAMAP-Rule:MF_04110}. degenerate-domain C0SPB6 ssbB Bacillus subtilis (strain 168) 224308 Single-stranded DNA-binding protein B (SSB B) Lacks the C-terminal region present in SsbA and thus is probably not able to participate in DNA replication and/or DNA repair. {ECO:0000305|PubMed:14762004}. degenerate-domain C0H404 ykzR Bacillus subtilis (strain 168) 224308 Probably inactive glycosylase YkzR Although related to the glycosyl hydrolase 18 family, lacks the conserved Glu active site at position 30, which is relaced by a Lys residue, suggesting it has no glycosidase activity. {ECO:0000305}. degenerate-domain O31764 ymfF Bacillus subtilis (strain 168) 224308 Probable inactive metalloprotease YmfF In contrast to other members of the family, it lacks one conserved zinc-binding site and the active site. {ECO:0000305}. degenerate-domain C0SPA8 yobH Bacillus subtilis (strain 168) 224308 DNA repair protein homolog YobH Could be the product of a pseudogene. This sequence is shorter than orthologs and lacks the conserved active site Glu and metal-binding site Asp residues. {ECO:0000305}. degenerate-domain O31971 yomM Bacillus subtilis (strain 168) 224308 SPbeta prophage-derived recombinase-like protein YomM Although strongly related to the 'phage' integrase family this protein lacks the conserved Tyr at position 318 suggesting it has no recombinase activity. {ECO:0000305}. degenerate-domain O31841 yozK Bacillus subtilis (strain 168) 224308 DNA repair protein homolog YozK Could be the product of a pseudogene. This sequence is shorter than orthologs and lacks the conserved active site Glu. {ECO:0000305}. degenerate-domain O32185 yusS Bacillus subtilis (strain 168) 224308 Short-chain dehydrogenase/reductase homolog YusS Could be the product of a pseudogene. This sequence is shorter than orthologs and lacks the conserved active site Tyr residue. {ECO:0000305}. degenerate-domain P71037 ywnB Bacillus subtilis (strain 168) 224308 Uncharacterized protein YwnB The N-terminus share sequence similarity with the dihydrodipicolinate reductase family. It however lacks the conserved C-terminal part, suggesting it has no dihydrodipicolinate reductase activity. {ECO:0000305}. degenerate-domain Q8AB53 Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) 226186 Putative glucosamine-6-phosphate deaminase-like protein BT_0258 Lacks the two conserved aspartate and the histidine residues in position 106, 177 and 179 respectively, that are involved in the active site of the protein in orthologs; they are replaced by a tyrosine, a valine and an asparagine residue respectively. {ECO:0000305}. degenerate-domain A4QKD3 psbN Barbarea verna (Land cress) (Erysimum vernum) 50458 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7GZ99 psbN Bassia hyssopifolia (Fivehorn smotherweed) (Salsola hyssopifolia) 224140 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6Y8A2 psbN Bertholletia excelsa (Brazil nut tree) 3645 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain C5C233 Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / CCUG 43141 / JCM 11478 / NBRC 16432 / NCIMB 13614 / HKI 0122) 471853 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q06J22 psbN Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain CCMP621)) 227086 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B2LT61 TLR2 Bison bison (American bison) (Bos bison) 9901 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q6T6S7 Bitis gabonica (Gaboon adder) (Gaboon viper) 8694 Snake venom serine protease homolog 1 (Venom serine proteinase-like protein 1) Lacks the conserved His residue in position 67 and the conserved Ser residue in position 206 essential for protease activity. {ECO:0000305}. degenerate-domain D8MIA1 Bitis rhinoceros (West African gaboon viper) (Vipera rhinoceros) 715877 Snake venom serine protease homolog rhinocerase 3 (BG-RHIN3) (Venom serine proteinase-like protein 3) Lacks the conserved His residue in position 66 and the conserved Ser residue in position 205 essential for protease activity. {ECO:0000305}. degenerate-domain D8MIA0 Bitis rhinoceros (West African gaboon viper) (Vipera rhinoceros) 715877 Snake venom serine protease homolog rhinocerase 2 (BG-RHIN2) (Venom serine proteinase-like protein 2) Lacks the conserved His residue in position 66 and the conserved Ser residue in position 205 essential for protease activity. {ECO:0000305}. degenerate-domain C5JZS0 ECM14 Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis) 559298 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 487 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q7VR66 pheT Blochmanniella floridana 203907 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks 2 conserved residues that bind magnesium; the aspartate residue in position 464 is replaced by an asparagine and the glutamate residue in position 467 is replaced by a serine residue. {ECO:0000305}. degenerate-domain Q492V0 pheT Blochmanniella pennsylvanica (strain BPEN) 291272 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks 2 conserved residues that bind magnesium; the aspartate residue in position 461 is replaced by an asparagine and the glutamate residue in position 464 is replaced by an alanine residue. {ECO:0000305}. degenerate-domain B5T267 TLR2 Bos indicus (Zebu) 9915 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q2KJA2 ABCF2 Bos taurus (Bovine) 9913 ATP-binding cassette sub-family F member 2 Lacks transmembrane domains and is probably not involved in transport. {ECO:0000305}. degenerate-domain A6QLR3 ABRAXAS2 Bos taurus (Bovine) 9913 BRISC complex subunit Abraxas 2 (Abraxas brother protein 1) (Protein FAM175B) Although strongly related to the ABRAXAS1 protein, lacks the C-terminal pSXXF that constitutes a specific recognition motif for the BRCT domain of BRCA1. {ECO:0000305}. degenerate-domain Q3ZBM1 ADPRHL1 Bos taurus (Bovine) 9913 Inactive ADP-ribosyltransferase ARH2 (ADP-ribosylhydrolase-like protein 1) ([Protein ADP-ribosylarginine] hydrolase-like protein 1) Although it belongs to the ADP-ribosylglycohydrolase family, lacks the metal-binding and substrate-binding residues, suggesting that it has no hydrolase activity. {ECO:0000250|UniProtKB:Q6AZR2}. degenerate-domain P30922 CHI3L1 Bos taurus (Bovine) 9913 Chitinase-3-like protein 1 (39 kDa whey protein) (Cartilage glycoprotein 39) (CGP-39) (GP-39) (Chitinase-like protein 1) (CLP-1) (SPC-40) (Signal-processing protein) Although it belongs to the glycosyl hydrolase 18 family, Leu-140 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity. {ECO:0000305}. degenerate-domain A6QQ21 COPS6 Bos taurus (Bovine) 9913 COP9 signalosome complex subunit 6 (SGN6) (Signalosome subunit 6) Although related to the peptidase M67A family, it lacks the JAMM motif that probably constitutes the catalytic center and therefore it probably does not have a protease activity. {ECO:0000305}. degenerate-domain O02675 DPYSL2 Bos taurus (Bovine) 9913 Dihydropyrimidinase-related protein 2 (DRP-2) (Neural-specific protein NSP60) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain A5PJF6 HSDL1 Bos taurus (Bovine) 9913 Inactive hydroxysteroid dehydrogenase-like protein 1 Although related to the SDR family, lacks the conserved active Tyr residue in position 218 which is replaced by a Phe, suggesting that it may lack oxidoreductase activity. {ECO:0000305}. degenerate-domain Q3T095 ING4 Bos taurus (Bovine) 9913 Inhibitor of growth protein 4 (p29ING4) Lacks the Trp (here Arg-220), a conserved feature of the aromatic cage required for the interaction with histone H3K4me3/2. {ECO:0000305}. degenerate-domain Q2T9N7 LYZL4 Bos taurus (Bovine) 9913 Lysozyme-like protein 4 (Lysozyme-4) Although it belongs to the glycosyl hydrolase 22 family, Gly-72 is present instead of the conserved Asp which is an active site residue. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain A7MB43 MTMR9 Bos taurus (Bovine) 9913 Myotubularin-related protein 9 (Inactive phosphatidylinositol 3-phosphatase 9) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 333 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q2KJ24 MTMR9L Bos taurus (Bovine) 9913 Myotubularin-related protein 9-like (Inactive phosphatidylinositol 3-phosphatase 9-like) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 337 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q0VCN1 NMRAL1 Bos taurus (Bovine) 9913 NmrA-like family domain-containing protein 1 Lacks the conserved Tyr residue in the active site triad of Ser-Tyr-Lys necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity. {ECO:0000305}. degenerate-domain Q3ZCA2 NUDT21 Bos taurus (Bovine) 9913 Cleavage and polyadenylation specificity factor subunit 5 (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) Lacks the conserved metal-binding residues in the NUDIX motif and is not expected to have hydrolase activity. {ECO:0000305}. degenerate-domain Q5E9P5 PAMR1 Bos taurus (Bovine) 9913 Inactive serine protease PAMR1 (Peptidase domain-containing protein associated with muscle regeneration 1) (Regeneration-associated muscle protease homolog) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 665 which is replaced by a Thr, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain Q5E9X7 PRSS35 Bos taurus (Bovine) 9913 Inactive serine protease 35 Although related to peptidase S1 family, lacks the conserved active Ser residue in position 345 which is replaced by a Thr, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain Q32KU2 PRSS37 Bos taurus (Bovine) 9913 Probable inactive serine protease 37 (Probable inactive trypsin-X2) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 192 which is replaced by an Ala, suggesting that it has no protease activity. Also lacks metal binding sites Glu in position 67 which is replaced by Asn, and Asn in position 69 which is replaced by Arg. {ECO:0000305}. degenerate-domain A5PK27 RNF144B Bos taurus (Bovine) 9913 E3 ubiquitin-protein ligase RNF144B (EC 2.3.2.31) (RING finger protein 144B) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain A6QQ77 SPACA3 Bos taurus (Bovine) 9913 Sperm acrosome membrane-associated protein 3 Although it belongs to the glycosyl hydrolase 22 family, Ala-70 and Asn-87 are present instead of the conserved Glu and Asp which are active site residues. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain Q0P5L5 SUMF1 Bos taurus (Bovine) 9913 Formylglycine-generating enzyme (FGE) (EC 1.8.3.7) (C-alpha-formylglycine-generating enzyme 1) (Sulfatase-modifying factor 1) The enzyme reaction was initially thought to act via a redox-active disulfide bond mechanism; however the disulfide bond only takes place with inactive enzyme that lacks the copper cofactor. The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation. {ECO:0000250|UniProtKB:Q8NBK3}. degenerate-domain Q58CP2 SUMF2 Bos taurus (Bovine) 9913 Inactive C-alpha-formylglycine-generating enzyme 2 (Sulfatase-modifying factor 2) Although strongly similar to formylglycine-generating enzyme, lacks the catalytic Cys residues that bind the catalytic copper. The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation. {ECO:0000305}. degenerate-domain P01267 TG Bos taurus (Bovine) 9913 Thyroglobulin (Tg) The cholinesterase-like (ChEL) region lacks the Ser residue of the catalytic triad suggesting that it has no esterase activity. {ECO:0000305}. degenerate-domain Q6GV17 TLR10 Bos taurus (Bovine) 9913 Toll-like receptor 10 (CD antigen CD290) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q95LA9 TLR2 Bos taurus (Bovine) 9913 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9GL65 TLR4 Bos taurus (Bovine) 9913 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q704V6 TLR6 Bos taurus (Bovine) 9913 Toll-like receptor 6 (CD antigen CD286) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q2V897 TLR2 Boselaphus tragocamelus (Nilgai) 9917 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q2V898 TLR4 Boselaphus tragocamelus (Nilgai) 9917 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain P0CG03 Bothrops alternatus (Urutu) (Rhinocerophis alternatus) 64174 Thrombin-like enzyme bhalternin (SVTLE) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) Lacks the typical His and Asp active sites in position 65 and 112, which are replaced by an Asn and Thr residues, preventing the protease activity. The sequence corresponding to the activity described in PubMed:20184912 may be slightly different from the sequence shown. {ECO:0000305}. degenerate-domain Q5W958 Bothrops jararaca (Jararaca) (Bothrops jajaraca) 8724 Snake venom serine protease homolog HS120 (Venom serine proteinase-like HS120) Lacks the conserved His residue in position 64 essential for protease activity. {ECO:0000305}. degenerate-domain Q7T229 Bothrops jararacussu (Jararacussu) 8726 Snake venom serine protease homolog (Serine proteinase-like protein) Lacks the conserved His residue in position 67 essential for protease activity. {ECO:0000305}. degenerate-domain A0A9W3HR52 L1 Bovine adenovirus B serotype 3 (BAdV-3) (Mastadenovirus bos3) 10510 Pre-hexon-linking protein IIIa (Capsid vertex-specific component IIIa) (CVSC) (Protein IIIa) (pIIIa) [Cleaved into: Hexon-linking protein IIIa] Lacks conserved residue(s) required for the propagation of feature annotation. {ECO:0000255|HAMAP-Rule:MF_04047}. degenerate-domain A0A9W3HR39 L2 Bovine adenovirus B serotype 3 (BAdV-3) (Mastadenovirus bos3) 10510 Pre-histone-like nucleoprotein (Pre-core protein VII) (pVII) [Cleaved into: pVIIn2; Histone-like nucleoprotein (NP) (Core protein VII)] Lacks conserved residue(s) required for the propagation of feature annotation. {ECO:0000255|HAMAP-Rule:MF_04056}. degenerate-domain Q71LB9 psbN Bowenia serrulata (Byfield fern) (Bowenia spectabilis var. serrulata) 13365 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B3TN77 psbN Brachypodium distachyon (Purple false brome) (Trachynia distachya) 15368 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q2YKI6 Brucella abortus (strain 2308) 359391 Purine-binding protein BAB2_0673 Lacks the conserved Cys that is essential for lipidation. {ECO:0000305}. degenerate-domain Q2YJF8 ftcR Brucella abortus (strain 2308) 359391 Flagellar transcriptional regulator FtcR Lacks the conserved Asp residue in position 50 usually required for phosphorylation. {ECO:0000305}. degenerate-domain Q576I4 ftcR Brucella abortus biovar 1 (strain 9-941) 262698 Flagellar transcriptional regulator FtcR Lacks the conserved Asp residue in position 50 usually required for phosphorylation. {ECO:0000305}. degenerate-domain Q8YDL7 ftcR Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M) 224914 Flagellar transcriptional regulator FtcR Lacks the conserved Asp residue in position 50 usually required for phosphorylation. The Glu residue in position 50 may mimic constitutive phosphorylation and allow FtcR to bypass the requirement for phosphorylation. {ECO:0000305}. degenerate-domain A5VW00 ftcR Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) 444178 Flagellar transcriptional regulator FtcR Lacks the conserved Asp residue in position 50 usually required for phosphorylation. {ECO:0000305}. degenerate-domain A9WYA0 nanM Brucella suis (strain ATCC 23445 / NCTC 10510) 470137 N-acetylneuraminate epimerase (EC 5.1.3.24) (N-acetylneuraminate mutarotase) (Neu5Ac mutarotase) (Sialic acid epimerase) Lacks the conserved Glu residue in position 242, which is expected to be an active site residue. {ECO:0000305}. degenerate-domain Q8FUS8 ftcR Brucella suis biovar 1 (strain 1330) 204722 Flagellar transcriptional regulator FtcR Lacks the conserved Asp residue in position 50 usually required for phosphorylation. {ECO:0000305}. degenerate-domain A8QFF6 Brugia malayi (Filarial nematode worm) 6279 Probable spastin homolog Bm1_53365 (EC 5.6.1.1) Lacks the conserved MIT domain, which is one of the features of the spastin family. {ECO:0000305}. degenerate-domain Q7YS85 CHI3L1 Bubalus bubalis (Domestic water buffalo) 89462 Chitinase-3-like protein 1 (Mammary gland protein 40) (SPB-40) Although it belongs to the glycosyl hydrolase 18 family, Leu-140 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity. {ECO:0000305}. degenerate-domain Q2PZH4 TLR2 Bubalus bubalis (Domestic water buffalo) 89462 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain P57229 pheS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) 107806 Phenylalanine--tRNA ligase alpha subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS) Lacks the conserved glutamate residue that binds magnesium. {ECO:0000305}. degenerate-domain P57230 pheT Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) 107806 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved glutamate residue in position 462 that binds magnesium; it is replaced by a glycine residue. {ECO:0000305}. degenerate-domain P59504 pheS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) 224915 Phenylalanine--tRNA ligase alpha subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS) Lacks the conserved glutamate residue that binds magnesium. {ECO:0000305}. degenerate-domain P59505 pheT Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) 224915 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved glutamate residue in position 465 that binds magnesium; it is replaced by a serine residue. {ECO:0000305}. degenerate-domain P59056 pheS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) 198804 Phenylalanine--tRNA ligase alpha subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS) Lacks the conserved glutamate residue that binds magnesium. {ECO:0000305}. degenerate-domain P59057 pheT Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) 198804 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved glutamate residue in position 464 that binds magnesium; it is replaced by a glycine residue. {ECO:0000305}. degenerate-domain Q8AY47 Bungarus candidus (Malayan krait) 92438 Basic phospholipase A2 beta-bungarotoxin A2 chain (Beta-BuTX A2 chain) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) In contrast to other phospholipases, it lacks the typical Asp active site (Asp->Gln in position 114). {ECO:0000305}. degenerate-domain Q3JNA0 nuoB2 Burkholderia pseudomallei (strain 1710b) 320372 Putative NADH-quinone oxidoreductase subunit B 2 (EC 7.1.1.-) (NADH dehydrogenase I subunit B 2) (NDH-1 subunit B 2) This protein lacks the conserved Cys in position 39; it is replaced by Arg. Thus this protein is probably unable to bind the 4Fe-4S cluster and may be non-functional. {ECO:0000305}. degenerate-domain Q67IA0 psbN Butomus umbellatus (Flowering rush) 50236 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A6MM64 psbN Buxus microphylla (Littleleaf boxwood) (Japanese boxwood) 153571 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7J198 psbN Cabomba caroliniana (Carolina fanwort) 4426 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A8XHQ1 Caenorhabditis briggsae 6238 Acireductone dioxygenase 3 (Acireductone dioxygenase (Fe(2+)-requiring) 3) (ARD' 3) (Fe-ARD 3) (EC 1.13.11.54) (Acireductone dioxygenase (Ni(2+)-requiring) 3) (ARD 3) (Ni-ARD 3) (EC 1.13.11.53) This enzyme lacks one or more conserved metal-binding sites. It may be non-functional. {ECO:0000305}. degenerate-domain A8X409 Caenorhabditis briggsae 6238 Probable inactive acireductone dioxygenase 2 This enzyme lacks one or more conserved metal-binding sites. It may be non-functional. {ECO:0000305}. degenerate-domain A8XYX3 Caenorhabditis briggsae 6238 Inactive cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1B (Inactive cap1 2'O-ribose methyltransferase 1B) (MTr1B) Although related to the cap-specific mRNA (nucleoside-2'-O-)-methyltransferase, lacks the conserved Lys active site in position 367, which is replaced by an Asn residue, suggesting it has no methyltransferase activity. {ECO:0000305}. degenerate-domain A8XV40 spas-1 Caenorhabditis briggsae 6238 Probable spastin homolog spas-1 (EC 5.6.1.1) Lacks the conserved MIT domain, which is one of the features of the spastin family. {ECO:0000305}. degenerate-domain Q61E63 spt-16 Caenorhabditis briggsae 6238 FACT complex subunit spt-16 (Facilitates chromatin transcription complex subunit spt-16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain A8XXC0 ttll-12 Caenorhabditis briggsae 6238 Tubulin--tyrosine ligase-like protein 12 (Inactive tubulin--tyrosine ligase-like protein 12) Although it belongs to the tubulin--tyrosine ligase family, the TTL domain lacks some of the ATP binding sites predicted to be essential for TTL activity (By similarity). Lacks tyrosine ligase activity in vitro (By similarity). Lacks glutamylation activity in vitro (By similarity). {ECO:0000250|UniProtKB:Q14166, ECO:0000250|UniProtKB:Q3UDE2}. degenerate-domain P91309 Caenorhabditis elegans 6239 Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) (InsP6 and PP-IP5 kinase) Although related to histidine acid phosphatases, it lacks the conserved active sites, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain P90850 Caenorhabditis elegans 6239 Uncharacterized peptidase C1-like protein F26E4.3 Although strongly related to peptidase C1 family, it lacks the conserved active Cys in position 210, which is replaced by a Ser residue, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain Q17405 Caenorhabditis elegans 6239 Aminopeptidase-like protein AC3.5 Although strongly related to the peptidase M1 family, it lacks the conserved active metal binding Glu and His in positions 496 and 499, which are replaced by a Arg and Ala residues respectively, suggesting that it has no activity. {ECO:0000305}. degenerate-domain P91416 Caenorhabditis elegans 6239 Probable inactive acireductone dioxygenase 1 This enzyme lacks one or more conserved metal-binding sites. It may be non-functional. {ECO:0000305}. degenerate-domain Q09407 Caenorhabditis elegans 6239 Probable inactive acireductone dioxygenase 2 This enzyme lacks one or more conserved metal-binding sites. It may be non-functional. {ECO:0000305}. degenerate-domain Q9U256 Caenorhabditis elegans 6239 Phospholipase A2-like protein Y52B11A.8 Although strongly related to the phospholipase A2 family, it lacks the conserved active Asp in position 129, which is replaced by a Val residue, suggesting that it has no activity. {ECO:0000305}. degenerate-domain O62247 bli-5 Caenorhabditis elegans 6239 Kunitz-type protein bli-5 (Blistered cuticle protein 5) (Kunitz-type protease inhibitor bli-5) Appears to have serine protease activity in vitro (PubMed:19716386). However, it is uncertain if this activity is genuine as bli-5 lacks all the catalytic features of serine proteases. {ECO:0000269|PubMed:19716386, ECO:0000305}. degenerate-domain G5ECE8 chhy-1 Caenorhabditis elegans 6239 Chondroitin hydrolase (EC 3.2.1.-) Lacks conserved residue(s) required for the propagation of feature annotation. {ECO:0000255|PROSITE-ProRule:PRU00076}. degenerate-domain G5ECQ8 cin-4 Caenorhabditis elegans 6239 DNA topoisomerase-like protein cin-4 Lacks the conserved ATP binding sites, the conserved active site tyrosine at position 404, the conserved isoleucine at position 455 important for DNA bending, and the conserved magnesium binding site at position 143, and therefore probably lacks topoisomerase activity. {ECO:0000305}. degenerate-domain Q20595 ctbp-1 Caenorhabditis elegans 6239 C-terminal-binding protein 1 In contrast to other members of the family, lacks the conserved Arg and Glu active sites at positions 417 and 446 respectively, suggesting that it lacks dehydrogenase activity. {ECO:0000305}. degenerate-domain G5EGU2 eak-6 Caenorhabditis elegans 6239 Tyrosine-protein phosphatase non-receptor type eak-6 (EC 3.1.3.48) (Enhancer of akt-1 null 6) Its phosphatase activity is uncertain. Lacks in vitro phosphatase activity with p-nitrophenylphosphate, even if the catalytic Cys is conserved. {ECO:0000269|PubMed:16839187}. degenerate-domain Q20826 glit-1 Caenorhabditis elegans 6239 Neuroligin-like protein glit-1 (Gliotactin homolog) (Inactive esterase glit-1) Although glit-1 contains an extracellular carboxylesterase-like domain, the characteristic Ser-Glu-His catalytic triad present in acetylcholinesterase is replaced by two Asp residues and an Arg, suggesting that glit-1 lacks catalytic activity. {ECO:0000305|PubMed:29346364}. degenerate-domain G5EGJ5 ida-1 Caenorhabditis elegans 6239 Receptor-type tyrosine-protein phosphatase-like ida-1 (Dense-core vesicle membrane protein ida-1) (Related to islet cell diabetic autoantigen protein) Lacks the typical Cys active site in position 696 that is replaced by a Ser residue, preventing the tyrosine-protein phosphatase activity. {ECO:0000305}. degenerate-domain G5EF51 ltd-1 Caenorhabditis elegans 6239 Lim and transglutaminase domain protein ltd-1 (Kyphoscoliosis inactive peptidase homolog ltd-1) Unlike the mammalian homolog KY, the residues forming the catalytic triad in the putative transglutaminase-like domain of ltd-1 are not conserved, therefore it is likely that the protein lacks protease activity. {ECO:0000305}. degenerate-domain O62415 lys-1 Caenorhabditis elegans 6239 Lysozyme-like protein 1 Lacks conserved active site residues, suggesting it has no catalytic activity. {ECO:0000305}. degenerate-domain O62416 lys-2 Caenorhabditis elegans 6239 Lysozyme-like protein 2 Lacks conserved active site residues, suggesting it has no catalytic activity. {ECO:0000305}. degenerate-domain Q9XXS1 lys-3 Caenorhabditis elegans 6239 Lysozyme-like protein 3 Weak similarity to other lysozymes and lacks the conserved active site. {ECO:0000305}. degenerate-domain Q20967 lys-5 Caenorhabditis elegans 6239 Lysozyme-like protein 5 Lacks conserved active site residues, suggesting it has no catalytic activity. {ECO:0000305}. degenerate-domain Q95XN2 mppa-1 Caenorhabditis elegans 6239 Mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (Inactive zinc metalloprotease mppa-1) Although it belongs to the peptidase M16 family, lacks the zinc-binding sites and appears to lack catalytic activity in vitro. {ECO:0000269|PubMed:16788047}. degenerate-domain Q9TXP3 mtm-5 Caenorhabditis elegans 6239 Myotubularin-related protein 5 (Inactive phosphatidylinositol 3-phosphatase 5) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 1284 in the dsPTPase catalytic loop and does not have phosphatase activity (By similarity). The pocket is however sufficiently preserved to bind phosphorylated substrates, and maybe protect them from phosphatases. {ECO:0000250|UniProtKB:O95248, ECO:0000305}. degenerate-domain Q965W9 mtm-9 Caenorhabditis elegans 6239 Myotubularin-related protein 9 (Inactive phosphatidylinositol 3-phosphatase 9) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 346 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain A5JYX8 nra-2 Caenorhabditis elegans 6239 Nicalin (Inactive aminopeptidase nra-2) (Nicotinic receptor-associated protein 2) Although it contains a putative aminopeptidase domain, the critical residues for Zn(2+) binding and thus for catalytic activity are not conserved suggesting that nra-2 lacks peptidase activity. {ECO:0000305|PubMed:19609303}. degenerate-domain Q8MNV0 spas-1 Caenorhabditis elegans 6239 Spastin homolog (EC 5.6.1.1) Lacks the conserved MIT domain, which is one of the features of the spastin family. {ECO:0000303|PubMed:17531954}. degenerate-domain Q9N5R9 spt-16 Caenorhabditis elegans 6239 FACT complex subunit spt-16 (Facilitates chromatin transcription complex subunit spt-16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain G5EEM6 tap-1 Caenorhabditis elegans 6239 TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (TAB1-like protein 1) (TAK1 kinase/MOM-4 binding Protein) Lacks several key residues involved in metal-binding and catalytic activity, therefore has lost phosphatase activity. {ECO:0000250|UniProtKB:Q15750}. degenerate-domain Q09503 ttbk-6 Caenorhabditis elegans 6239 Inactive tau-tubulin kinase ttbk-6 Although it belongs to the protein kinase family, lacks the active site Asp residue which has been changed to Asn so is unlikely to be catalytically active. {ECO:0000305}. degenerate-domain Q09512 ttll-12 Caenorhabditis elegans 6239 Tubulin--tyrosine ligase-like protein 12 (Inactive tubulin--tyrosine ligase-like protein 12) Although it belongs to the tubulin--tyrosine ligase family, the TTL domain lacks some of the ATP binding sites predicted to be essential for TTL activity (By similarity). Lacks tyrosine ligase activity in vitro (By similarity). Lacks glutamylation activity in vitro (By similarity). {ECO:0000250|UniProtKB:Q14166, ECO:0000250|UniProtKB:Q3UDE2}. degenerate-domain P91853 uev-3 Caenorhabditis elegans 6239 Ubiquitin-conjugating enzyme E2 variant 3 Lacks the active site cysteine required for interaction with ubiquitin. {ECO:0000305}. degenerate-domain Q01630 unc-33 Caenorhabditis elegans 6239 Protein unc-33 (Inactive dihydropyrimidinase unc-33) (Uncoordinated protein 33) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q23229 xol-1 Caenorhabditis elegans 6239 XO lethal protein 1 Although clearly related the GHMP kinase family as demonstrated by the 3D-structure, it lacks many conserved feature of GHMP kinases and probably does not bind ATP, suggesting that it probably does not have kinase activity. {ECO:0000305}. degenerate-domain Q9GFA1 psbN Calycanthus floridus (Eastern sweetshrub) 3429 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7HKX5 psbN Calycanthus floridus var. glaucus (Eastern sweetshrub) (Calycanthus fertilis var. ferax) 212734 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9PMZ6 Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) 192222 Putative 3-oxoacyl-[acyl-carrier-protein] synthase 3 (EC 2.3.1.180) (3-oxoacyl-[acyl-carrier-protein] synthase III) (Beta-ketoacyl-ACP synthase III) (KAS III) Lacks the Asn-Xaa-Arg residues, which are typical of the ACP-binding site and are essential for the association between AcpP and FabH. {ECO:0000305}. degenerate-domain Q5A1D5 CDC68 Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) 237561 FACT complex subunit SPT16 (CaCDC68) (Cell division control protein 68) (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q5AD07 SOD5 Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) 237561 Cell surface Cu-only superoxide dismutase 5 (EC 1.15.1.1) (Predicted GPI-anchored protein 3) Although the beta-barrel of Cu/Zn SODs is largely preserved, SOD5 is a monomeric copper protein that lacks a zinc-binding site and is missing the electrostatic loop element proposed to promote catalysis through superoxide guidance. Without an electrostatic loop, the copper site of SOD5 is not recessed and is readily accessible to bulk solvent (PubMed:24711423). {ECO:0000305|PubMed:24711423}. degenerate-domain Q6FWT4 SPT16 Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus) 284593 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q6EYK6 psbN Canella winterana (Wild cinnamon) (Laurus winterana) 3426 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain E2RFJ3 SLC40A1 Canis lupus familiaris (Dog) (Canis familiaris) 9615 Ferroportin (Solute carrier family 40 protein member 1) Manganese (Mn) transport by SLC40A1 remains controversial. Some in vitro studies have suggested that SLC40A1 transports minimal amounts of Mn(2+) (By similarity). Other groups have suggested that it does not. The affinity of SLC40A1 for manganese is extremely low compared with iron, implying that any SLC40A1-mediated Mn transport in vivo would likely be trivial (By similarity). A recent study examined the role of SLC40A1 in Mn homeostasis by using Tmprss6-O mice, which express high levels of hepcidin/HAMP and therefore have very low SLC40A1 levels in their tissues. These mice show frank iron deficiency and reduced iron levels in most tissues, but manganese levels are largely unaffected (By similarity). These studies suggest that manganese is probably not the physiological substrate of SLC40A1. {ECO:0000250|UniProtKB:Q9JHI9, ECO:0000250|UniProtKB:Q9NP59, ECO:0000305}. degenerate-domain B6VH75 SPACA3 Canis lupus familiaris (Dog) (Canis familiaris) 9615 Sperm acrosome membrane-associated protein 3 (Sperm protein reactive with antisperm antibodies) (Sperm protein reactive with ASA) Although it belongs to the glycosyl hydrolase 22 family, Thr-70 and Asn-87 are present instead of the conserved Glu and Asp which are active site residues. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain Q689D1 TLR2 Canis lupus familiaris (Dog) (Canis familiaris) 9615 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q8SPQ0 CHI3L1 Capra hircus (Goat) 9925 Chitinase-3-like protein 1 (BP40) (Mammary gland protein 40) (MGP-40) Although it belongs to the glycosyl hydrolase 18 family, Leu-140 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity. {ECO:0000305}. degenerate-domain Q0GC71 TLR2 Capra hircus (Goat) 9925 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain B2LT62 TLR2 Capra ibex (Ibex) 72542 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain A4QKM0 psbN Capsella bursa-pastoris (Shepherd's purse) (Thlaspi bursa-pastoris) 3719 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A9XVA1 psbN Carica papaya (Papaya) 3649 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q71LB5 psbN Cedrus deodara (Deodar cedar) (Pinus deodara) 3322 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7SYF1 Cerastes cerastes (Horned desert viper) 8697 Thrombin-like enzyme cerastocytin (SVTLE) (EC 3.4.21.-) (C.cerastes platelet proaggregant protein) (CC-PPP) (Factor VIII activator) (Fibrinogen-clotting enzyme) (Proaggregant serine proteinase) (Snake venom serine protease) (SVSP) Lacks the conserved Cys-50-Cys-66 disulfide bridge due to the replacement of Cys-50 by a Gly. {ECO:0000305}. degenerate-domain Q7J196 psbN Ceratophyllum demersum (Rigid hornwort) (Coontail) 4428 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7J194 psbN Cercidiphyllum japonicum (Katsura tree) 13413 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q2GXG8 Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus) 306901 Vacuolar membrane protease (EC 3.4.-.-) (FXNA-related family protease 1) Although related to the peptidase M28 family, it lacks some conserved zinc-binding sites involved in catalysis and therefore has probably lost hydrolase activity. {ECO:0000305}. degenerate-domain Q8M9Z2 psbN Chaetosphaeridium globosum (Charophycean green alga) (Herposteiron globosum) 96477 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q1ACH3 psbN Chara vulgaris (Common stonewort) 55564 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain C0HKH6 Chassalia chartacea (Chassalia curviflora) 510798 Chassatide C11 (Cyclotide chaC11) This peptide is linear as it lacks the C-terminal Asp/Asn residue required for cyclization. {ECO:0000269|PubMed:22467870}. degenerate-domain I0B6F5 Chassalia chartacea (Chassalia curviflora) 510798 Chassatide C8 (Cyclotide chaC8) The mature peptide is linear as it lacks the C-terminal Asp/Asn residue required for cyclization. {ECO:0000269|PubMed:22467870}. degenerate-domain I0B6F4 Chassalia chartacea (Chassalia curviflora) 510798 Chassatide C7 (Cyclotide chaC7) The mature peptide is linear as it lacks the C-terminal Asp/Asn residue required for cyclization. {ECO:0000269|PubMed:22467870}. degenerate-domain Q3YAU5 Chersonesometrus fulvipes (Indian black scorpion) (Heterometrus fulvipes) 141248 Phospholipase A2 large subunit (HfPLA2) (EC 3.1.1.4) In contrast to other phospholipases, it lacks the typical Asp active site (Asp->Glu in position 62). {ECO:0000305}. degenerate-domain A8HME3 FAP9 Chlamydomonas reinhardtii (Chlamydomonas smithii) 3055 Intraflagellar transport protein 22 (Flagellar-associated protein 9) Although similar to the small GTPase superfamily, lacks the conserved catalytic Gln in position 67 which is replaced by a Ser residue, possibly explaining the weak GTPase activity. In contrast to other members of the family, it is not prenylated (PubMed:22076686) and unlikely to associate directly with membranes. {ECO:0000305|PubMed:22076686}. degenerate-domain A8HN58 IFT27 Chlamydomonas reinhardtii (Chlamydomonas smithii) 3055 Intraflagellar transport protein 27 (Flagellar-associated protein 156) Although similar to the small GTPase superfamily, lacks the conserved catalytic Gln in position 79 which is replaced by a Ser residue, possibly explaining the weak GTPase activity. In contrast to other members of the family, it is not prenylated (PubMed:21505417). {ECO:0000305|PubMed:21505417}. degenerate-domain Q06480 psbN Chlamydomonas reinhardtii (Chlamydomonas smithii) 3055 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A6MMF0 psbN Chloranthus spicatus (Chulantree) (Nigrina spicata) 13006 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P56326 psbN Chlorella vulgaris (Green alga) 3077 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8KBL4 Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum) 194439 Ribulose bisphosphate carboxylase-like protein (RuBisCO-like protein) Although strongly related to RuBisCO family, it lacks the conserved Lys active site in position 327, which is replaced by an Arg residue, suggesting that it may catalyze enolization but not carboxylation. {ECO:0000305}. degenerate-domain Q8KDE2 argF Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum) 194439 Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3) Lacks the conserved threonine and leucine residues in positions 66 and 276, respectively, which are part of the carbamoylphosphate and ornithine binding sites; they are replaced by a leucine and a methionine residue, respectively. {ECO:0000305}. degenerate-domain Q9AMC5 Chlorobaculum thiosulfatiphilum (Chlorobium limicola f.sp. thiosulfatophilum) 115852 Ribulose bisphosphate carboxylase-like protein (RuBisCO-like protein) Although strongly related to RuBisCO family, it lacks the conserved Lys active site in position 327, which is replaced by an Arg residue, suggesting that it may catalyze enolization but not carboxylation. {ECO:0000305}. degenerate-domain Q71KP0 psbN Chlorokybus atmophyticus (Soil alga) 3144 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B5LMQ1 psbN Cicer arietinum (Chickpea) (Garbanzo) 3827 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain D2TN58 ytfP Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280) 637910 Gamma-glutamylcyclotransferase family protein ytfP Lacks the conserved Glu residue at position 70 that serves as proton acceptor in enzymes with gamma-glutamylcyclotransferase activity. {ECO:0000305}. degenerate-domain Q09ME9 psbN Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) 2711 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A8C7R3 easA Claviceps fusiformis (Ergot fungus) 40602 Probable inactive dehydrogenase easA (Ergot alkaloid biosynthesis protein A) In contrast to other members of the family, lacks the conserved Tyr active site at position 176 which is replaced by a Phe residue. {ECO:0000305}. degenerate-domain Q6ZXC1 easA Claviceps purpurea (Ergot fungus) (Sphacelia segetum) 5111 Probable inactive dehydrogenase easA (Ergot alkaloid biosynthesis protein A) In contrast to other members of the family, lacks the conserved Tyr active site at position 176 which is replaced by a Phe residue. {ECO:0000305}. degenerate-domain M1W0Y0 easA Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum) 1111077 Probable inactive dehydrogenase easA (Ergot alkaloid biosynthesis protein A) In contrast to other members of the family, lacks the conserved Tyr active site at position 176 which is replaced by a Phe residue. {ECO:0000305}. degenerate-domain Q97H19 Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) 272562 Putative polysaccharide biosynthesis protein with aminopeptidase-like domain Has distant sequence similarity to aminopeptidases that belong to the MEROPS peptidase family M28, but binds only one zinc ion, contrary to the metallopeptidases of the MEROPS family M28 that bind two catalytic zinc ions. Lacks the active site Asp and Glu residues that are conserved in family members with aminopeptidase activity. {ECO:0000305}. degenerate-domain C5PHW9 ECM14 Coccidioides posadasii (strain C735) (Valley fever fungus) 222929 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 488 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain E9DD69 ECM14 Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus) 443226 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 488 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q67I10 psbN Coelogyne cristata (Orchid) (Cymbidium speciosissimum) 38221 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A0A363 psbN Coffea arabica (Arabian coffee) 13443 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q71KQ8 psbN Coleochaete orbicularis (Charophycean green alga) 3124 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6J1Z5 cnbCa Comamonas testosteroni (Pseudomonas testosteroni) 285 2-aminophenol 1,6-dioxygenase subunit alpha (2-amino-5-chlorophenol 1,6-dioxygenase subunit alpha) In contrast to other members of the family, lacks the conserved iron-binding sites, suggesting that the alpha subunit has no oxidoreductase activity. {ECO:0000305}. degenerate-domain Q9AHG2 tsaB2 Comamonas testosteroni (Pseudomonas testosteroni) 285 Putative toluene-4-sulfonate monooxygenase system reductase subunit TsaB2 (EC 1.5.1.-) (Toluenesulfonate methyl-monooxygenase reductase component TsaB2) Could be the product of a pseudogene. Probably not expressed, due to the absence of promoter-like sequences upstream of the operon tsaMBCD2 (PubMed:11282598). {ECO:0000305|PubMed:11282598}. degenerate-domain Q9AHG1 tsaD2 Comamonas testosteroni (Pseudomonas testosteroni) 285 Putative 4-(hydroxymethyl)benzenesulfonate dehydrogenase TsaD2 (EC 1.1.1.257) (Toluenesulfonate aldehyde dehydrogenase TsaD) Could be the product of a pseudogene. Probably not expressed, due to the absence of promoter-like sequences upstream of the operon tsaMBCD2 (PubMed:11282598). {ECO:0000305|PubMed:11282598}. degenerate-domain Q9AHG3 tsaM2 Comamonas testosteroni (Pseudomonas testosteroni) 285 Putative toluene-4-sulfonate monooxygenase system iron-sulfur subunit TsaM2 (EC 1.14.14.-) (Toluenesulfonate methyl-monooxygenase oxygenase component TsaM2) Could be the product of a pseudogene. Probably not expressed, due to the absence of promoter-like sequences upstream of the operon tsaMBCD2 (PubMed:11282598). {ECO:0000305|PubMed:11282598}. degenerate-domain Q6EYJ8 psbN Cornus mas (Cornelian cherry dogwood) 4285 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6NFH6 Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) 257309 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q8FT61 Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) 196164 Nucleotide-binding protein CE1710 Lacks the conserved ATP-binding site due to Leu-43 (instead of a conserved basic residue). {ECO:0000305}. degenerate-domain Q8FMN2 Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) 196164 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q8NQ56 Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) 196627 Nucleotide-binding protein Cgl1591/cg1794 Lacks the conserved ATP-binding site due to Leu-38 (instead of a conserved basic residue). {ECO:0000305}. degenerate-domain Q8NMJ4 Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) 196627 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain A4QGX7 Corynebacterium glutamicum (strain R) 340322 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q4JXD1 Corynebacterium jeikeium (strain K411) 306537 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain B1VII7 Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109) 504474 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q9R1F8 TLR2 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) 10029 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9WV82 TLR4 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) 10029 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain B1WUD5 psbN Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain ATCC 51142)) 43989 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A7MGE5 glpG Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) 290339 Rhomboid protease GlpG homolog Although strongly related to the peptidase S54 family, it lacks the conserved active sites, suggesting that it has no peptidase activity. {ECO:0000305}. degenerate-domain A4QKV9 psbN Crucihimalaya wallichii (Rock-cress) (Arabidopsis campestris) 78192 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P0CQ23 SPT16 Cryptococcus deneoformans (strain B-3501A) (Cryptococcus neoformans var. neoformans serotype D) 283643 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain P0CQ22 SPT16 Cryptococcus deneoformans (strain JEC21 / ATCC MYA-565) (Cryptococcus neoformans var. neoformans serotype D) 214684 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q5IHC2 psbN Cryptomeria japonica (Japanese cedar) (Cupressus japonica) 3369 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q4VZJ0 psbN Cucumis sativus (Cucumber) 3659 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B0X6E8 Culex quinquefasciatus (Southern house mosquito) (Culex pungens) 7176 Protein crossbronx homolog Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q6EYJ4 psbN Cunninghamia lanceolata (China fir) (Pinus lanceolata) 28977 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6AAW4 Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium acnes) 267747 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q85FZ3 psbN Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga) 280699 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain O19926 psbN Cyanidium caldarium (Red alga) 2771 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P48108 psbN Cyanophora paradoxa 2762 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q71LA6 psbN Cycas revoluta (Sago palm) 3396 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A6H5K9 psbN Cycas taitungensis (Prince sago) (Cycas taiwaniana) 54799 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain D2Y2C6 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 Hainantoxin-XVII-2 (HNTX-XVII-2) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 95. {ECO:0000305}. degenerate-domain D2Y203 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 Mu-theraphotoxin-Hhn2g (Mu-TRTX-Hhn2g) (Hainantoxin-III-14) (HNTX-III-14) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 64. {ECO:0000305}. degenerate-domain D2Y284 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U11-theraphotoxin-Hhn1n (U11-TRTX-Hhn1n) (Hainantoxin-XVI-14) (HNTX-XVI-14) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 95. {ECO:0000305}. degenerate-domain D2Y274 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U11-theraphotoxin-Hhn1e (U11-TRTX-Hhn1e) (Hainantoxin-XVI-5) (HNTX-XVI-5) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 82. {ECO:0000305}. degenerate-domain D2Y2Q6 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 Kunitz-type U15-theraphotoxin-Hhn1o (U15-TRTX-Hhn1o) (Kunitz-type serine protease inhibitor hainantoxin-XI-15) (HNTX-XI-15) Lacks the conserved Cys residue in position 81. {ECO:0000305}. degenerate-domain D2Y245 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U3-theraphotoxin-Hhn1k (U3-TRTX-Hhn1k) (Hainantoxin-VIII-3) (HNTX-VIII-3) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 62. {ECO:0000305}. degenerate-domain D2Y2R4 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 Hainantoxin-X-3 (HNTX-X-3) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 39. {ECO:0000305}. degenerate-domain D2Y282 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U11-theraphotoxin-Hhn1l (U11-TRTX-Hhn1l) (Hainantoxin-XVI-12) (HNTX-XVI-12) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 90. {ECO:0000305}. degenerate-domain D2Y2F2 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 Hainantoxin-X-2 (HNTX-X-2) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 45. {ECO:0000305}. degenerate-domain D2Y2L8 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 Omega-theraphotoxin-Hhn1e (Omega-TRTX-Hhn1e) (Hainantoxin-IX-6) (HNTX-IX-6) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 71. {ECO:0000305}. degenerate-domain D2Y2M2 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U3-theraphotoxin-Hhn1b (U3-TRTX-Hhn1b) (Hainantoxin-VIII-10) (HNTX-VIII-10) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 79. {ECO:0000305}. degenerate-domain D2Y278 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U11-theraphotoxin-Hhn1h (U11-TRTX-Hhn1h) (Hainantoxin-XVI-8) (HNTX-XVI-8) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 75. {ECO:0000305}. degenerate-domain D2Y285 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U11-theraphotoxin-Hhn1o (U11-TRTX-Hhn1o) (Hainantoxin-XVI-15) (HNTX-XVI-15) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 110. {ECO:0000305}. degenerate-domain D2Y2I0 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U11-theraphotoxin-Hhn1w (U11-TRTX-Hhn1w) (Hainantoxin-XVI-24) (HNTX-XVI-24) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 110. {ECO:0000305}. degenerate-domain D2Y279 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U11-theraphotoxin-Hhn1i (U11-TRTX-Hhn1i) (Hainantoxin-XVI-9) (HNTX-XVI-9) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 89. {ECO:0000305}. degenerate-domain D2Y2G8 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U3-theraphotoxin-Hhn1o (U3-TRTX-Hhn1o) (Hainantoxin-VIII-7) (HNTX-VIII-7) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 66. {ECO:0000305}. degenerate-domain D2Y2H3 Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) 2781057 U7-theraphotoxin-Hhn1k (U7-TRTX-Hhn1k) (Hainantoxin-XIII-13) (HNTX-XIII-13) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 81. {ECO:0000305}. degenerate-domain P68426 Cyriopagopus schmidti (Chinese bird spider) (Haplopelma schmidti) 29017 U6-theraphotoxin-Hs1a (U6-TRTX-Hs1a) (SHT-I) (Toxin 1) (Toxin-I) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 77. {ECO:0000305}. degenerate-domain A1DZY4 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Ras-like protein family member 11A-like (EC 3.6.5.2) Although highly related to the Ras family, lacks the conserved prenylation motif at the C-terminus, which serves to target Ras proteins to membrane compartments. {ECO:0000305}. degenerate-domain Q5XJB9 adprhl1 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Inactive ADP-ribosyltransferase arh2 (ADP-ribosylhydrolase-like protein 1) ([Protein ADP-ribosylarginine] hydrolase-like protein 1) Although it belongs to the ADP-ribosylglycohydrolase family, lacks the metal-binding and substrate-binding residues, suggesting that it has no hydrolase activity. {ECO:0000250|UniProtKB:Q6AZR2}. degenerate-domain Q7ZYX1 aktip Danio rerio (Zebrafish) (Brachydanio rerio) 7955 AKT-interacting protein (Fused toes protein homolog) Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q1L8G6 ankib1 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Ankyrin repeat and IBR domain-containing protein 1 (EC 2.3.2.31) Lacks one Cys residue in the IBR-type zinc finger domain that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q52PJ5 dpysl3 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Dihydropyrimidinase-related protein 3 (DRP-3) (Collapsin response mediator protein 4) (CRMP-4) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q08BC6 eno4 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Enolase 4 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) Although it is highly related to enolase enzyme family, lacks the conserved Glu active site. {ECO:0000305}. degenerate-domain A4QP81 frrs1 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Ferric reductase 1 (EC 1.-.-.-) The cytochrome b561 domain lacks the conserved His residue that binds iron in the heme. {ECO:0000305}. degenerate-domain A5WWC6 hsdl1 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Inactive hydroxysteroid dehydrogenase-like protein 1 Although it belongs to the SDR family, Phe-218 is present instead of the conserved Tyr which is an active site residue. It is therefore expected that this protein lacks oxidoreductase activity. {ECO:0000305}. degenerate-domain A0JMF6 mtmr10 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Myotubularin-related protein 10 (Inactive phosphatidylinositol 3-phosphatase 10) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 388 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain A2BGG1 mtmr12 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Myotubularin-related protein 12 (Inactive phosphatidylinositol 3-phosphatase 12) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 378 in the dsPTPase catalytic loop and does not have phosphatase activity. {ECO:0000250|UniProtKB:Q80TA6}. degenerate-domain Q6DFZ6 notum1b Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Inactive palmitoleoyl-protein carboxylesterase notum1b In contrast to other members of the family, lacks the active sites for palmitoleoyl-protein carboxylesterase activity, suggesting it has no activity. degenerate-domain Q7T3C6 nudt21 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Cleavage and polyadenylation specificity factor subunit 5 (Nudix hydrolase 21) Lacks the conserved metal-binding residues in the NUDIX motif and is not expected to have hydrolase activity. {ECO:0000305}. degenerate-domain Q5RFV4 rnf144aa Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Probable E3 ubiquitin-protein ligase RNF144A-A (EC 2.3.2.31) (RING finger protein 144A-A) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q6DH94 rnf144ab Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Probable E3 ubiquitin-protein ligase RNF144A-B (EC 2.3.2.31) (RING finger protein 144A-B) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain A0A0R4IQZ2 zdhhc13 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Putative palmitoyltransferase ZDHHC13 (DHHC domain-containing protein 13) (DHHC-13) (Zinc finger DHHC domain-containing protein 13) Although it belongs to the DHHC palmitoyltransferase family, lacks the conserved active site cysteine residue at position 479 and may lack catalytic activity. {ECO:0000305}. degenerate-domain Q0ZUL9 TLR6 Dasypus novemcinctus (Nine-banded armadillo) 9361 Toll-like receptor 6 (CD antigen CD286) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q0G9T4 psbN Daucus carota (Wild carrot) 4039 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6BXE5 SPT16 Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) 284592 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q9RYL9 Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) 243230 Alpha-2-macroglobulin homolog Lacks the conserved thioester bond that is characteristic of the alpha-2-macroglobulins. {ECO:0000305}. degenerate-domain Q9RY70 argF Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) 243230 Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3) Lacks the conserved threonine residue in position 53, which is part of the carbamoylphosphate binding site; it is replaced by a leucine residue. {ECO:0000305}. degenerate-domain Q9RU48 sodC Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) 243230 Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) Lacks the last conserved histidine that binds copper. {ECO:0000305}. degenerate-domain Q54KL0 Dictyostelium discoideum (Social amoeba) 44689 Citrate synthase-related protein DDB_G0287281 Although highly related to the citrate synthase family, lacks the conserved active His at position 264 which is replaced by an Asn residue. {ECO:0000305}. degenerate-domain Q54JC9 Dictyostelium discoideum (Social amoeba) 44689 Lysozyme C-like protein DDB_G0288143 Although related to the glycosyl hydrolase 22 family, lacks the conserved Asp active site, suggesting it may not have lysozyme activity. {ECO:0000305}. degenerate-domain Q54LJ8 Dictyostelium discoideum (Social amoeba) 44689 NmrA-like family domain-containing protein DDB_G0286605 Lacks the conserved Tyr residue in the active site triad of Ser-Tyr-Lys necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity. {ECO:0000305}. degenerate-domain Q558W0 Dictyostelium discoideum (Social amoeba) 44689 HIT domain-containing protein DDB_G0272839 In contrast to other HIT domain proteins, lacks the conserved histidine triad motif (HXHXH), suggesting it has no hydrolase activity. {ECO:0000305}. degenerate-domain Q8T6B7 abcF2 Dictyostelium discoideum (Social amoeba) 44689 ABC transporter F family member 2 Lacks transmembrane domains and is probably not involved in transport. {ECO:0000305}. degenerate-domain Q54TR1 cfaD Dictyostelium discoideum (Social amoeba) 44689 Counting factor associated protein D Lacks catalytic activity, even though the active site residues are conserved. {ECO:0000305}. degenerate-domain Q54F36 lyC2 Dictyostelium discoideum (Social amoeba) 44689 Lysozyme C-like protein DDB_G0291137 Although related to the glycosyl hydrolase 22 family, lacks the conserved Asp active site, suggesting it may not have lysozyme activity. {ECO:0000305}. degenerate-domain Q55E68 nudt21 Dictyostelium discoideum (Social amoeba) 44689 Cleavage and polyadenylation specificity factor subunit 5 Lacks the conserved metal-binding residues in the NUDIX motif and is not expected to have hydrolase activity. {ECO:0000305}. degenerate-domain Q54S43 spt16 Dictyostelium discoideum (Social amoeba) 44689 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain A0A5C1RF03 Didymella fabae (Leaf and pod spot disease fungus) (Ascochyta fabae) 372025 Ascochitine biosynthesis cluster transcriptional regulator (Ascochitine biosynthesis cluster protein 11) The deduced amino acid sequence of the orf11 gene lacks a DNA-binding domain and contains only the conserved domain (termed 'middle homology region') that is commonly found in Zn(II)2Cys6-type transcription factors. {ECO:0000269|PubMed:31554725}. degenerate-domain Q9GF93 psbN Dioscorea bulbifera (Air potato) (Dioscorea latifolia) 35874 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A6MMN5 psbN Dioscorea elephantipes (Elephant's foot yam) (Testudinaria elephantipes) 145284 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A7MAQ2 dioA3 Dioscorea japonica (Japanese yam) 4673 Dioscorin dioA3 (EC 1.6.5.4) (EC 4.2.1.1) (Dj-dio5) (Dj-dioA3) (Tuber storage protein dioA3) Despite overall sequence similarity to the typical alpha class carbonic anhydrases, lacks one of the three conserved catalytic zinc-ligand histidines. The carbonate dehydratase activity of this protein is zinc-independent. {ECO:0000305|PubMed:25747844}. degenerate-domain Q75N35 DB3L Dioscorea polystachya (Chinese yam) 55575 Dioscorin DB3L (Tuber storage protein DB3L) Despite overall sequence similarity to the typical alpha class carbonic anhydrases, lacks one of the three conserved catalytic zinc-ligand histidines. {ECO:0000305}. degenerate-domain Q75N34 DB3S Dioscorea polystachya (Chinese yam) 55575 Dioscorin DB3S (EC 1.6.5.4) (EC 4.2.1.1) (Tuber storage protein DB3S) (allergen Dio p TSP) Despite overall sequence similarity to the typical alpha class carbonic anhydrases, lacks one of the three conserved catalytic zinc-ligand histidines. The carbonate dehydratase activity of this protein is zinc-independent. {ECO:0000250|UniProtKB:A7MAQ2}.; degenerate-domain A4QL47 psbN Draba nemorosa (Woodland whitlowgrass) 171822 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q06GW9 psbN Drimys granadensis 224735 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7J192 psbN Drimys winteri (Winter's bark) (Drimys chilensis) 3419 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B3MGT3 Drosophila ananassae (Fruit fly) 7217 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B3MEZ6 cbx Drosophila ananassae (Fruit fly) 7217 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B3NK72 Drosophila erecta (Fruit fly) 7220 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B3N6U7 cbx Drosophila erecta (Fruit fly) 7220 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4JWF5 Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi) 7222 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4J613 cbx Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi) 7222 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q9VSH0 Drosophila melanogaster (Fruit fly) 7227 Cyclic GMP-AMP synthase-like protein (EC 2.7.7.-) Homolog of vertebrate CGAS/Cyclic GMP-AMP synthase but lacks any detectable ability to activate STING in response to dsDNA (PubMed:34261128). Lacks the zinc-ribbon domain and positively charged N-terminus essential for DNA binding. {ECO:0000269|PubMed:34261128, ECO:0000305|PubMed:29924997}. degenerate-domain A1ZBR5 Drosophila melanogaster (Fruit fly) 7227 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain A0A0B4JD40 Drosophila melanogaster (Fruit fly) 7227 Topors-like protein Although the protein has similarity to Topors, it lacks the region enabling E3 ubiquitin-protein ligase activity. {ECO:0000305}. degenerate-domain Q9VQK9 GABPI Drosophila melanogaster (Fruit fly) 7227 Protein beta4GalNAcTB pilot (GalNAcTB pilot) (Palmitoyltransferase) (EC 2.3.1.225) Shares similarity with vertebrate DHHC palmitoyltransferase proteins but lacks the active site Cys within the DHHC motif and instead has a Ser. It is unclear if this can form a S-palmitoyl serine intermediate required for acyltransferase activity. {ECO:0000305}. degenerate-domain Q95RA9 GILT1 Drosophila melanogaster (Fruit fly) 7227 GILT-like protein 1 Lacks the conserved active site CXXC motif that is essential for thiol reductase activity. Its enzyme activity is therefore unsure. {ECO:0000305|PubMed:24491521}. degenerate-domain Q9VCK2 GILT3 Drosophila melanogaster (Fruit fly) 7227 GILT-like protein 3 Lacks the conserved active site CXXC motif that is essential for thiol reductase activity. Its enzyme activity is therefore unsure. {ECO:0000305|PubMed:24491521}. degenerate-domain Q9NFT9 Hexl Drosophila melanogaster (Fruit fly) 7227 Hexokinase-like protein (Inactive hexokinase-1) Although it belongs to the hexokinase family it lacks the residues for ATP substrate binding, suggesting it has no kinase activity. {ECO:0000305|Ref.2}. degenerate-domain Q23997 Idgf6 Drosophila melanogaster (Fruit fly) 7227 Imaginal disk growth factor 6 (Inactive chitinase-like protein) Lacks the typical Glu active site in position 165 that is replaced by a Gln residue, exhibits no chitinolytic activity towards either polymeric and oligomeric substrates (PubMed:18342251). Its precise function remains unclear. Strongly binds chitin even though it lacks a chitin binding domain (PubMed:18342251). {ECO:0000269|PubMed:18342251, ECO:0000305|PubMed:18342251}. degenerate-domain P08761 MsrA Drosophila melanogaster (Fruit fly) 7227 Peptide methionine sulfoxide reductase (EC 1.8.4.11) (Ecdysone-induced protein 28/29 kDa) (Methionine-S-sulfoxide reductase) (Peptide-methionine (S)-S-oxide reductase) Unlike mammalian MSRA, lacks methionine oxidase activity because Cys-232 cannot function as a resolving cysteine to perform the disulfide exchange and instead remains as a free thiol (PubMed:30529269). As a result, the active site cysteine is trapped in disulfide linkage with Cys-246 and is therefore unable to react with a second molecule of methionine sulfoxide to complete methionine oxidation (PubMed:30529269). {ECO:0000269|PubMed:30529269}. degenerate-domain A8DYP0 Obsc Drosophila melanogaster (Fruit fly) 7227 Protein Obscurin (Inactive serine/threonine-protein kinase obscurin) (Muscle M-line assembly protein Unc-89) In contrast to obscurins in other species, lacks serine/threonine kinase activity as protein kinase domain 1 is catalytically inactive and protein kinase domain 2 is predicted to be inactive (PubMed:37121260). The lack of activity of protein kinase domain 1 is probably due to the presence of a glycine residue instead of an aspartate residue at position 3306 in the catalytic site pocket (PubMed:37121260). {ECO:0000269|PubMed:37121260}. degenerate-domain Q9VXP4 Paf-AHalpha Drosophila melanogaster (Fruit fly) 7227 Platelet-activating factor acetylhydrolase IB subunit beta homolog Although strongly related to acetylglycerophosphocholine esterase enzymes, it lacks the active site and has no lipase activity. {ECO:0000305}. degenerate-domain Q9VSM6 S-Lap1 Drosophila melanogaster (Fruit fly) 7227 Crystallomitin S-Lap1 (Inactive sperm-leucylaminopeptidase 1) Although it belongs to the peptidase M17 family, lacks the active site Arg residue and has no aminopeptidase activity. {ECO:0000269|PubMed:30802236}. degenerate-domain Q9VSM7 S-Lap2 Drosophila melanogaster (Fruit fly) 7227 Crystallomitin S-Lap2 (Inactive sperm-leucylaminopeptidase 2) Although it belongs to the peptidase M17 family, lacks the active site Arg residue, suggesting it has no aminopeptidase activity. {ECO:0000305}. degenerate-domain Q961W5 S-Lap3 Drosophila melanogaster (Fruit fly) 7227 Crystallomitin S-Lap3 (Inactive sperm-leucylaminopeptidase 3) Although it belongs to the peptidase M17 family, lacks the active site Lys and Arg residues and zinc binding sites, suggesting it has no aminopeptidase activity. {ECO:0000305}. degenerate-domain Q95R35 S-Lap4 Drosophila melanogaster (Fruit fly) 7227 Crystallomitin S-Lap4 (Inactive sperm-leucylaminopeptidase 4) Although it belongs to the peptidase M17 family, lacks the active site Lys and Arg residues and zinc binding sites, suggesting it has no aminopeptidase activity. {ECO:0000305}. degenerate-domain A1Z9G3 S-Lap5 Drosophila melanogaster (Fruit fly) 7227 Crystallomitin S-Lap5 (Inactive sperm-leucylaminopeptidase 5) Although it belongs to the peptidase M17 family, lacks the active site Lys and Arg residues and zinc binding sites, suggesting it has no aminopeptidase activity. {ECO:0000305}. degenerate-domain Q500X4 S-Lap7 Drosophila melanogaster (Fruit fly) 7227 Crystallomitin S-Lap7 (Inactive sperm-leucylaminopeptidase 7) Although it belongs to the peptidase M17 family, lacks the active site Lys and Arg residues and zinc binding sites, suggesting it has no aminopeptidase activity. {ECO:0000305}. degenerate-domain Q7K5K9 S-Lap8 Drosophila melanogaster (Fruit fly) 7227 Crystallomitin S-Lap8 (Inactive sperm-leucylaminopeptidase 8) Although it belongs to the peptidase M17 family, lacks the active site Lys and Arg residues and zinc binding sites, suggesting it has no aminopeptidase activity. {ECO:0000305}. degenerate-domain P18168 Ser Drosophila melanogaster (Fruit fly) 7227 Protein serrate (Delta-like protein) (Protein beaded) Lacks conserved residue(s) required for the propagation of feature annotation. {ECO:0000255|PROSITE-ProRule:PRU00076}. degenerate-domain O18373 Sps1 Drosophila melanogaster (Fruit fly) 7227 Inactive selenide, water dikinase-like protein (Protein patufet) (Selenophosphate synthetase 1) The conserved active site Cys (or selenocysteine) residue in position 49 is replaced by an Arg and therefore the protein lacks selenide-dependent monoselenophosphate synthetase activity. {ECO:0000269|PubMed:9398525}. degenerate-domain P08953 Tl Drosophila melanogaster (Fruit fly) 7227 Protein toll In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9VUN0 Toll-6 Drosophila melanogaster (Fruit fly) 7227 Toll-like receptor 6 In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q7KIN0 Toll-7 Drosophila melanogaster (Fruit fly) 7227 Toll-like receptor 7 In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9V477 Tollo Drosophila melanogaster (Fruit fly) 7227 Toll-like receptor Tollo (Toll-like receptor 8) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9VIP7 bwa Drosophila melanogaster (Fruit fly) 7227 Inactive alkaline ceramidase (AlkCDase) (Dacer) (Alkaline N-acylsphingosine amidohydrolase) (Alkaline acylsphingosine deacylase) (Protein brain washing) Ortholog of mammalian alkaline ceramidases that lacks ceramidase (EC:3.5.1.23) activity (PubMed:21148295). There is evidence of increased ceramidase activity in cells overexpressing this protein, though this could be due to regulation of expression or activity of other proteins involved in this pathway (PubMed:20112046, PubMed:21148295). The CREST motif amino acids that form the Zn(2+) binding active site in mammalian alkaline ceramidases are conserved. {ECO:0000269|PubMed:20112046, ECO:0000269|PubMed:21148295, ECO:0000305}. degenerate-domain Q9V629 cuff Drosophila melanogaster (Fruit fly) 7227 Protein cutoff In contrast to other members of the family, does not possess detectable exonuclease activity toward 5'-monophosphate RNA or pyrophosphohydrolase activity (PubMed:27292797). Lacks the conserved catalytic sites that bind the divalent metal cations required for ribonuclease activity. {ECO:0000269|PubMed:27292797, ECO:0000305}. degenerate-domain Q9V422 dnt Drosophila melanogaster (Fruit fly) 7227 Inactive tyrosine-protein kinase Dnt (Protein doughnut) Although this protein belongs to the kinase superfamily, it lacks key residues required for catalytic activity, suggesting that it does not have kinase activity. {ECO:0000305|PubMed:11135307}. degenerate-domain Q8IRG6 dre4 Drosophila melanogaster (Fruit fly) 7227 FACT complex subunit spt16 (Facilitates chromatin transcription complex subunit SPT16) (dSPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q9VR59 l(1)G0196 Drosophila melanogaster (Fruit fly) 7227 Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) (InsP6 and PP-IP5 kinase) Although related to histidine acid phosphatases, it lacks the conserved active sites, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q7K2S9 loopin-1 Drosophila melanogaster (Fruit fly) 7227 Crystallomitin loopin-1 (Inactive sperm-leucylaminopeptidase 6) Although it belongs to the peptidase M17 family, lacks the active site Arg residue and zinc binding sites, and has no aminopeptidase activity. {ECO:0000269|PubMed:30802236}. degenerate-domain Q9VZH2 mas Drosophila melanogaster (Fruit fly) 7227 Protein masquerade Lacks the conserved Ser residue within the catalytic triad which is replaced by a Gly residue, probably resulting in a loss of proteolytic activity. {ECO:0000305}. degenerate-domain Q9VVX5 nes Drosophila melanogaster (Fruit fly) 7227 Lysophospholipid acyltransferase 5 (LPLAT 5) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 5) (O-acyltransferase domain-containing protein 5) (Protein nessy) (Nes) Although strongly related to the membrane-bound acyltransferase family, it lacks the conserved His active site which is replaced by an Asn-415 residue. {ECO:0000305}. degenerate-domain Q7K4V4 peo Drosophila melanogaster (Fruit fly) 7227 Protein pendolino Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000269|PubMed:26110638}. degenerate-domain Q8IA41 pgant11 Drosophila melanogaster (Fruit fly) 7227 Putative inactive polypeptide N-acetylgalactosaminyltransferase 11 (pp-GaNTase 11) (Inactive UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) (Inactive protein-UDP acetylgalactosaminyltransferase 11) Although strongly related to polypeptide N-acetylgalactosaminyltransferase proteins, it lacks the conserved Asp-Xaa-His motif in positions 199-201 and the conserved His residue in position 330 which are involved in the binding to the cofactor Mn(2+). This suggests that it may have lost its activity. {ECO:0000305}. degenerate-domain Q8IA44 pgant12 Drosophila melanogaster (Fruit fly) 7227 Putative inactive polypeptide N-acetylgalactosaminyltransferase 12 (pp-GaNTase 12) (Inactive UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12) (Inactive protein-UDP acetylgalactosaminyltransferase 12) Although strongly related to polypeptide N-acetylgalactosaminyltransferase proteins, it lacks the conserved His at position 211 which is part of the Asp-Xaa-His motif which binds the cofactor Mn(2+). This suggests that it may have lost its activity. {ECO:0000305}. degenerate-domain Q76NQ1 rho-5 Drosophila melanogaster (Fruit fly) 7227 Inactive rhomboid protein 1 (iRhom1) (Rhomboid family protein rhomboid-5) An inactive member of the rhomboid-like family of serine proteases (PubMed:21439629). Lacks the catalytic His residue and has a Pro residue just upstream of the catalytic Ser-1160. {ECO:0000269|PubMed:21439629, ECO:0000305|PubMed:21439629}. degenerate-domain Q7K5M0 scaf Drosophila melanogaster (Fruit fly) 7227 Inactive serine protease scarface Lacks the conserved residues within the catalytic triad, probably resulting in a loss of proteolytic activity. {ECO:0000303|PubMed:20379222}. degenerate-domain Q8MSU3 sdr2 Drosophila melanogaster (Fruit fly) 7227 Ferric reductase 1 (EC 1.-.-.-) (stromal cell-derived receptor 2) The cytochrome b561 domain lacks the conserved His residue that binds iron in the heme. {ECO:0000305}. degenerate-domain Q9W0H3 sturkopf Drosophila melanogaster (Fruit fly) 7227 Lipid droplet-associated hydrolase (EC 3.1.1.13) (Lipid droplet-associated serine hydrolase) The catalytic activity is unsure despite catalytic sites being conserved (PubMed:23525007, PubMed:27836991). Lacks cholesterol esterase activity when overexpressed in S2 cells (PubMed:27836991). The murine ortholog does have cholesterol esterase activity, although the activity is so low that it may be undetectable under certain experimental conditions or masked by other cellular cholesterol esterases (By similarity). Lacks lipolytic activity towards trioleoylglycerol, dioleoylglycerol or monooleoylglycerol when overexpressed in COS-7 cells or S2 cells (PubMed:23525007, PubMed:27836991). {ECO:0000250|UniProtKB:Q8BVA5, ECO:0000269|PubMed:23525007, ECO:0000269|PubMed:27836991}. degenerate-domain B4KS18 Drosophila mojavensis (Fruit fly) 7230 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4KMF8 cbx Drosophila mojavensis (Fruit fly) 7230 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4GD81 Drosophila persimilis (Fruit fly) 7234 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4H581 cbx Drosophila persimilis (Fruit fly) 7234 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q28YD9 Drosophila pseudoobscura pseudoobscura (Fruit fly) 46245 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q28XA5 cbx Drosophila pseudoobscura pseudoobscura (Fruit fly) 46245 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4HPU1 Drosophila sechellia (Fruit fly) 7238 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4HT57 cbx Drosophila sechellia (Fruit fly) 7238 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4QEJ9 Drosophila simulans (Fruit fly) 7240 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4QHS6 cbx Drosophila simulans (Fruit fly) 7240 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4LPP8 Drosophila virilis (Fruit fly) 7244 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4LNV5 cbx Drosophila virilis (Fruit fly) 7244 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4MRW2 Drosophila willistoni (Fruit fly) 7260 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4MQY1 cbx Drosophila willistoni (Fruit fly) 7260 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4PAP8 Drosophila yakuba (Fruit fly) 7245 Protein crossbronx-like Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain B4NWM2 cbx Drosophila yakuba (Fruit fly) 7245 Protein crossbronx Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q5B011 ecm14 Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) 227321 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 477 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q5AU62 nmrA Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) 227321 Nitrogen metabolite repression protein nmrA (Negative-acting nitrogen regulatory protein nmrA) (Nitrogen metabolite regulation protein) Lacks the conserved Tyr residue in position 127 in the active site triad of Ser-Tyr-Lys that is necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity. {ECO:0000305}. degenerate-domain Q5B6P3 png1 Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) 227321 Protein PNG1 Although strongly related to the peptide:N-glycanase enzyme, it lacks the conserved active site Cys in position 246, which is replaced by a Val residue suggesting that it has no activity. {ECO:0000305}. degenerate-domain Q5B2X8 spt16 Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) 227321 FACT complex subunit spt16 (Facilitates chromatin transcription complex subunit spt16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q4G3C3 psbN Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi) 2903 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8SRV5 Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) 284813 Probable ATP-binding cassette sub-family F member 3 homolog Lacks transmembrane domains and is probably not involved in transport. {ECO:0000305}. degenerate-domain Q8HS39 psbN Ephedra sinica (Chinese ephedra) (Ma huang) 33152 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A2TBU0 easA Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii) 73839 Probable inactive reductase easA (Ergot alkaloid synthesis protein A) In contrast to other members of the family, lacks the conserved Tyr active site at position 176 which is replaced by a Phe residue. {ECO:0000305}. degenerate-domain Q4G3R0 lolP2 Epichloe uncinata (Endophyte fungus) (Neotyphodium uncinatum) 5050 Inactive cytochrome P450 monooxygenase lolP2 (Loline biosynthesis cluster 2 protein P) Lacks the heme-binding site and is thus probably inactive (PubMed:15654104). {ECO:0000305|PubMed:15654104}. degenerate-domain Q6T752 TLR2 Equus caballus (Horse) 9796 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9MYW3 TLR4 Equus caballus (Horse) 9796 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q759K3 RIM13 Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Ashbya gossypii) 284811 Calpain-like protease palB/RIM13 (EC 3.4.22.-) (Cysteine protease RIM13) Lacks the conserved Asn residue of the catalytic triad in position 292, which is replaced by an Asp residue. {ECO:0000305}. degenerate-domain Q756A7 SPT16 Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Ashbya gossypii) 284811 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain P31450 glvG Escherichia coli (strain K12) 83333 Putative inactive 6-phospho-alpha-glucosidase Could be the product of a pseudogene. Lacks the C-terminal half of the catalytic domain found in other members of this family. This truncated polypeptide does not display phospho-alpha- or phospho-beta-glucosidase activity (PubMed:9209025). {ECO:0000305|PubMed:9209025}. degenerate-domain P0CF60 insD8 Escherichia coli (strain K12) 83333 Putative transposase InsD for insertion element IS2E Could be the product of a pseudogene. IS2E is a partial IS2 sequence which lacks the N-terminal 83 residues of InsD. Locus b1578 is not annotated in the MG1655 genome and b1578/JW1570 is probably not expressed. {ECO:0000305}. degenerate-domain P76168 intQ Escherichia coli (strain K12) 83333 Putative defective protein IntQ (Putative lambdoid prophage Qin defective integrase) May not be functional, the original sequence is interrupted by an IS2 element. {ECO:0000305}. degenerate-domain P37613 panZ Escherichia coli (strain K12) 83333 PanD regulatory factor Lacks the conserved catalytic glutamate found in many enzymatically active members of the Gcn5-like N-acetyltransferase (GNAT) family. {ECO:0000250|UniProtKB:Q7CPJ9}. degenerate-domain P46130 ybhC Escherichia coli (strain K12) 83333 Putative acyl-CoA thioester hydrolase YbhC (EC 3.1.2.-) Lacks the conserved Asp residue in position 252 essential for pectinase activity. Likewise, most of the residues involved in substrate binding are not conserved. Was originally (PubMed:15808744) thought to have palmitoyl-CoA thioesterase activity, but PubMed:19452549 were unable to detect any pectinase or palmitoyl-CoA thioesterase activity. Its enzyme activity is therefore unsure. {ECO:0000305|PubMed:15808744}. degenerate-domain P42624 yhaK Escherichia coli (strain K12) 83333 Pirin-like protein YhaK Lacks the conserved His residues required for metal binding. Its function must therefore be different from the metal-dependent roles proposed for other family members. {ECO:0000305}. degenerate-domain P0AE48 ytfP Escherichia coli (strain K12) 83333 Gamma-glutamylcyclotransferase family protein YtfP Lacks the conserved Glu residue at position 70 that serves as proton acceptor in enzymes with gamma-glutamylcyclotransferase activity. {ECO:0000305}. degenerate-domain A7ZLX1 lsrA Escherichia coli O139:H28 (strain E24377A / ETEC) 331111 Putative autoinducer 2 import ATP-binding protein LsrA homolog Could be the product of a pseudogene. The C-terminus is shorter than in related proteins. In addition, LsrC and LsrD permeases are missing, this ABC transporter is therefore probably not functional in strain E24377A. {ECO:0000305}. degenerate-domain Q8XE35 yfaS Escherichia coli O157:H7 83334 Alpha-2-macroglobulin homolog Lacks the conserved thioester bond that is characteristic of the alpha-2-macroglobulins. {ECO:0000305}. degenerate-domain P58115 yhaK Escherichia coli O157:H7 83334 Pirin-like protein YhaK Lacks the conserved His residues required for metal binding. Its function must therefore be different from the metal-dependent roles proposed for other family members. {ECO:0000305}. degenerate-domain P0AE50 ytfP Escherichia coli O157:H7 83334 Gamma-glutamylcyclotransferase family protein YtfP Lacks the conserved Glu residue at position 70 that serves as proton acceptor in enzymes with gamma-glutamylcyclotransferase activity. {ECO:0000305}. degenerate-domain Q8FI27 Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) 199310 Putative hemolysin E-like protein Could be the product of a pseudogene. Although it is strongly related to the hemolysin E toxin from E.coli K12 strain, it lacks all the N-terminal part of the protein, and it is therefore probably not functional. {ECO:0000305}. degenerate-domain P0AE49 ytfP Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) 199310 Gamma-glutamylcyclotransferase family protein YtfP Lacks the conserved Glu residue at position 70 that serves as proton acceptor in enzymes with gamma-glutamylcyclotransferase activity. {ECO:0000305}. degenerate-domain Q49KX0 psbN Eucalyptus globulus subsp. globulus (Tasmanian blue gum) 71271 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6EYJ0 psbN Euonymus alatus (Burning bush) (Celastrus alatus) 4307 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7YMA2 psbN Exsertotheca crispa (Moss) (Neckera crispa) 103981 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B2XWQ1 psbN Fagopyrum esculentum subsp. ancestrale (Wild buckwheat) 180217 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P58727 TLR4 Felis catus (Cat) (Felis silvestris catus) 9685 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q02452 nifD Frankia alni 1859 Nitrogenase molybdenum-iron protein alpha chain (EC 1.18.6.1) (Dinitrogenase) (Nitrogenase component I) This sequence lacks the conserved His that serves as a ligand for the 7Fe-Mo-9S-C-homocitryl cluster. {ECO:0000305}. degenerate-domain Q8R687 hemA Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355) 190304 Glutamyl-tRNA reductase (GluTR) (EC 1.2.1.70) Lacks the conserved histidine residue in position 89 which is potentially part of the active site; it is replaced by a tyrosine residue. {ECO:0000305}. degenerate-domain A0A6J1W8N1 LOC113510063 Galleria mellonella (Greater wax moth) 7137 Phenoloxidase-activating factor 2 (PFAF2) (Prophenoloxidase-activating factor II) Lacks the conserved Ser residue within the catalytic triad which is replaced by a Gly residue, probably resulting in a loss of proteolytic activity. {ECO:0000305}. degenerate-domain Q5ZJJ5 AKTIP Gallus gallus (Chicken) 9031 AKT-interacting protein (Fused toes protein homolog) Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q90635 DPYSL2 Gallus gallus (Chicken) 9031 Dihydropyrimidinase-related protein 2 (DRP-2) (Collapsin response mediator protein CRMP-62) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q5ZID0 NMRAL1 Gallus gallus (Chicken) 9031 NmrA-like family domain-containing protein 1 Lacks the conserved Tyr residue in the active site triad of Ser-Tyr-Lys necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity. {ECO:0000305}. degenerate-domain Q9IAY5 NUDT16L1 Gallus gallus (Chicken) 9031 Tudor-interacting repair regulator protein (NUDT16-like protein 1) (Protein syndesmos) Although strongly related to the nudix NUDT16 protein, lacks the Nudix box and is therefore not related to the rest of the family. Lacks a number of residues which are necessary for hydrolase activity and does not play a role in U8 snoRNA decapping activity. {ECO:0000305}. degenerate-domain Q9DD78 TLR2-1 Gallus gallus (Chicken) 9031 Toll-like receptor 2 type-1 In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9DGB6 TLR2-2 Gallus gallus (Chicken) 9031 Toll-like receptor 2 type-2 In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9ZB62 argF Geobacillus stearothermophilus (Bacillus stearothermophilus) 1422 Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3) Lacks the conserved threonine and arginine residues in positions 60 and 61, which are part of the carbamoylphosphate binding site; the threonine residue is replaced by a glycine residue. {ECO:0000305}. degenerate-domain S0ENM8 STC5 Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae and foot rot disease fungus) (Fusarium fujikuroi) 1279085 Inactive (1R,4R,5S)-(-)-guaia-6,10(14)-diene synthase Although similar to (1R,4R,5S)-(-)-guaia-6,10(14)-diene synthase, lacks the metal binding site Asn at position 288 and does not show (1R,4R,5S)-(-)-guaia-6,10(14)-diene synthase activity. Converting Lys-288 to a asparagine restores activity. {ECO:0000269|PubMed:27294564}. degenerate-domain Q8J2R3 PNG1 Gibberella moniliformis (Maize ear and stalk rot fungus) (Fusarium verticillioides) 117187 Protein PNG1 Although strongly related to the peptide:N-glycanase enzyme, it lacks the conserved active site Cys in position 243, which is replaced by a Val residue suggesting that it has no activity. {ECO:0000305}. degenerate-domain Q4IR87 PNG1 Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) 229533 Protein PNG1 Although strongly related to the peptide:N-glycanase enzyme, it lacks the conserved active site Cys in position 243, which is replaced by a Val residue suggesting that it has no activity. {ECO:0000305}. degenerate-domain Q4HYB8 SPT16 Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) 229533 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q9GF86 psbN Ginkgo biloba (Ginkgo) (Maidenhair tree) 3311 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B2LT64 TLR2 Giraffa camelopardalis (Giraffe) 9894 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q7NCE0 petA Gloeobacter violaceus (strain ATCC 29082 / PCC 7421) 251221 Cytochrome f Lacks the conserved Tyr/Phe in position 29 necessary for binding heme. {ECO:0000305}. degenerate-domain Q7NCH8 psbN Gloeobacter violaceus (strain ATCC 29082 / PCC 7421) 251221 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8AWX7 Gloydius halys (Chinese water mocassin) (Agkistrodon halys) 8714 Zinc metalloproteinase-disintegrin agkistin (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP) This protein does probably not undergo proteolytic processing to release the disintegrin domain. {ECO:0000305}. degenerate-domain Q5FUA2 pheT Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) 290633 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved aspartate residue in position 480 that binds magnesium; it is replaced by a serine residue. {ECO:0000305}. degenerate-domain P93164 Glycine max (Soybean) (Glycine hispida) 3847 Gamma-glutamyl hydrolase (EC 3.4.19.9) (Conjugase) (GH) (Gamma-Glu-X carboxypeptidase) Lacks the conserved Cys residue in position 155 and the conserved His residue in position 268 essential for carbopeptidase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q2PMQ7 psbN Glycine max (Soybean) (Glycine hispida) 3847 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9GF82 psbN Gnetum gnemon (Spanish joint-fir) (Gnetum acutatum) 3382 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B3Y615 TLR2 Gorilla gorilla gorilla (Western lowland gorilla) 9595 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q8SPE8 TLR4 Gorilla gorilla gorilla (Western lowland gorilla) 9595 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain A0ZZ63 psbN Gossypium barbadense (Sea Island cotton) (Hibiscus barbadensis) 3634 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q2L935 psbN Gossypium hirsutum (Upland cotton) (Gossypium mexicanum) 3635 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6B8Y6 psbN Gracilaria tenuistipitata var. liui (Red alga) 285951 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain O78513 psbN Guillardia theta (Cryptophyte) (Cryptomonas phi) 55529 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B2LMM1 psbN Guizotia abyssinica (Niger) (Ramtilla) 4230 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7HIW6 psbN Gunnera chilensis (Chilean rhubarb) 130722 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain D3GGZ8 bli-5 Haemonchus contortus (Barber pole worm) 6289 Kunitz-type protein bli-5 (Blistered cuticle protein 5) (Kunitz-type protease inhibitor bli-5) Appears to have serine protease activity in vitro (PubMed:19716386). However, it is uncertain if this activity is genuine as bli-5 lacks all the catalytic features of serine proteases. {ECO:0000269|PubMed:19716386, ECO:0000305}. degenerate-domain P71375 Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) 71421 Putative uncharacterized symporter HI_1315 Could be the product of a pseudogene. Similar to the N-terminal section of E.coli YidK, but does not seem to be complete and thus may not be functional as a transporter. {ECO:0000305}. degenerate-domain Q1KXT1 psbN Helianthus annuus (Common sunflower) 4232 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain O25371 ymxG Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) 85962 Non-peptidase homolog YmxG Does not seem to have protease activity as it lacks the conserved zinc-binding sites and the active site. {ECO:0000305|PubMed:33970782}. degenerate-domain P0DMI6 Heterometrus laoticus (Thai giant scorpion) 217256 Phospholipase A2 heteromtoxin (HmTx) [Cleaved into: Heteromtoxin large subunit (EC 3.1.1.4); Heteromtoxin small subunit] In contrast to other phospholipases, it lacks the typical Asp active site (Asp->Glu in position 93). {ECO:0000305}. degenerate-domain Q949H3 CHI-L1 Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) 3981 Inactive chitinase-like protein 1 (HbCLP1) (allergen Hev b 11) Lacks the conserved Glu active site in position 136, which is replaced by an Ala residue, explaining why it is inactive. {ECO:0000269|PubMed:25104038}. degenerate-domain W0IWL0 CHI-L2 Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) 3981 Inactive chitinase-like protein 2 (HbCLP2) (allergen Hev b 11) Lacks the conserved Glu active site in position 166, which is replaced by an Ala residue, explaining why it is inactive. {ECO:0000269|PubMed:25104038}. degenerate-domain Q8GUD7 LACIC Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) 3981 Probable inactive chitinase-like protein LaCIC (Leaf class I chitinase) (LaCIC) (allergen Hev b 11) Lacks the conserved Glu active site in position 117, which is replaced by an Ala residue, explaining why it is inactive. {ECO:0000305}. degenerate-domain A6QS12 Histoplasma mississippiense (Darling's disease fungus) 2059318 Vacuolar membrane protease (EC 3.4.-.-) (FXNA-related family protease 1) Although related to the peptidase M28 family, it lacks some conserved zinc-binding and active site residues and therefore has probably lost hydrolase activity. {ECO:0000305}. degenerate-domain A6RCF5 ECM14 Histoplasma mississippiense (Darling's disease fungus) 2059318 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 488 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q9GRW0 PPAF2 Holotrichia diomphalia (Korean black chafer) 33394 Phenoloxidase-activating factor 2 (45 KDa PPAF) (Hd-45) (Prophenoloxidase-activating factor II) (Serine protease-like PPAF-2) [Cleaved into: Phenoloxidase-activating factor 2 light chain; Phenoloxidase-activating factor 2 heavy chain] Lacks the conserved Ser residue within the catalytic triad which is replaced by a Gly residue, probably resulting in a loss of proteolytic activity. {ECO:0000305}.; degenerate-domain Q9NUQ8 ABCF3 Homo sapiens (Human) 9606 ATP-binding cassette sub-family F member 3 Lacks transmembrane domains and is probably not involved in transport. {ECO:0000305}. degenerate-domain Q8N6G6 ADAMTSL1 Homo sapiens (Human) 9606 ADAMTS-like protein 1 (ADAMTSL-1) (Punctin-1) Although strongly similar to members of the ADAMTS family it lacks the metalloprotease and disintegrin-like domains which are typical of that family. {ECO:0000305}. degenerate-domain Q86TH1 ADAMTSL2 Homo sapiens (Human) 9606 ADAMTS-like protein 2 (ADAMTSL-2) Although strongly similar to members of the ADAMTS family it lacks the metalloprotease and disintegrin-like domains which are typical of that family. {ECO:0000305}. degenerate-domain P82987 ADAMTSL3 Homo sapiens (Human) 9606 ADAMTS-like protein 3 (ADAMTSL-3) (Punctin-2) Although strongly similar to members of the ADAMTS family it lacks the metalloprotease and disintegrin-like domains which are typical of that family. {ECO:0000305}. degenerate-domain Q6ZMM2 ADAMTSL5 Homo sapiens (Human) 9606 ADAMTS-like protein 5 (ADAMTSL-5) (Thrombospondin type-1 domain-containing protein 6) Although strongly similar to members of the ADAMTS family it lacks the metalloprotease and disintegrin-like domains which are typical of that family. {ECO:0000305}. degenerate-domain Q9NS39 ADARB2 Homo sapiens (Human) 9606 Inactive double-stranded RNA-specific editase B2 (RNA-dependent adenosine deaminase 3) (RNA-editing deaminase 2) (RNA-editing enzyme 2) (dsRNA adenosine deaminase B2) Although it is similar to the double-stranded RNA adenosine deaminases ADAR/ADAR1 and ADARB1/ADAR2 and capable of binding RNA, it lacks double-stranded RNA adenosine deaminase activity in vitro. Instead, it inhibits adenosine-to-inosine editing in vivo. {ECO:0000269|PubMed:10836796, ECO:0000269|PubMed:31552420}. degenerate-domain Q8N7X0 ADGB Homo sapiens (Human) 9606 Androglobin The calpain domain lacks the conserved active site residues. Probably catalytically inactive as a calcium-dependent cysteine-type endopeptidase. {ECO:0000305|PubMed:22115833}. degenerate-domain Q8NDY3 ADPRHL1 Homo sapiens (Human) 9606 Inactive ADP-ribosyltransferase ARH2 (ADP-ribosylhydrolase-like protein 1) ([Protein ADP-ribosylarginine] hydrolase-like protein 1) Although it belongs to the ADP-ribosylglycohydrolase family, lacks the metal-binding and substrate-binding residues, suggesting that it has no hydrolase activity. {ECO:0000250|UniProtKB:Q6AZR2}. degenerate-domain Q8IUX7 AEBP1 Homo sapiens (Human) 9606 Adipocyte enhancer-binding protein 1 (AE-binding protein 1) (Aortic carboxypeptidase-like protein) Although related to peptidase M14 family, lacks the active site residues and zinc-binding sites, suggesting that it has no carboxypeptidase activity. {ECO:0000305}. degenerate-domain Q9P2G1 ANKIB1 Homo sapiens (Human) 9606 Ankyrin repeat and IBR domain-containing protein 1 (EC 2.3.2.31) Lacks one Cys residue in the IBR-type zinc finger domain that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q3SXY8 ARL13B Homo sapiens (Human) 9606 ADP-ribosylation factor-like protein 13B (ADP-ribosylation factor-like protein 2-like 1) (ARL2-like protein 1) Was initially thought to form a homodimer (PubMed:18554500). However, 3D structure of C.reinhardtii ortholog showed that it is probably not the case. {ECO:0000305|PubMed:18554500}. degenerate-domain P0C7U1 ASAH2B Homo sapiens (Human) 9606 Putative inactive neutral ceramidase B (ASAH2-like protein) (Putative inactive N-acylsphingosine amidohydrolase 2B) (Putative inactive non-lysosomal ceramidase B) In contrast to other members of the family, ASAH2B has no predicted transmembrane domain, and lacks the active site, suggesting that it may be catalytically inactive. {ECO:0000305}. degenerate-domain P35219 CA8 Homo sapiens (Human) 9606 Carbonic anhydrase-related protein (CARP) (Carbonic anhydrase VIII) (CA-VIII) Although it belongs to the alpha-carbonic anhydrase family, Arg-116 is present instead of the conserved His which is a zinc-binding residue. It is therefore expected that this protein lacks carbonic anhydrase activity. {ECO:0000305}. degenerate-domain Q9UKY3 CES1P1 Homo sapiens (Human) 9606 Putative inactive carboxylesterase 4 (Inactive carboxylesterase 1 pseudogene 1) (Placental carboxylesterase 3) (PCE-3) In contrast to other members of the family, it is shorter and lacks the C-terminal part that contains the conserved Glu and His active sites. {ECO:0000305}.; degenerate-domain P36222 CHI3L1 Homo sapiens (Human) 9606 Chitinase-3-like protein 1 (39 kDa synovial protein) (Cartilage glycoprotein 39) (CGP-39) (GP-39) (hCGP-39) (YKL-40) Although it belongs to the glycosyl hydrolase 18 family, Leu-140 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity. {ECO:0000305}. degenerate-domain Q15782 CHI3L2 Homo sapiens (Human) 9606 Chitinase-3-like protein 2 (Chondrocyte protein 39) (YKL-39) Lacks the conserved sequence motif DxxDxDxE that is essential for the catalytic activity of chitinases of the glycosyl hydrolase 18 family, and therefore has no chitinase activity. {ECO:0000305}. degenerate-domain Q9Y471 CMAHP Homo sapiens (Human) 9606 Inactive cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMP-NeuAc hydroxylase-like protein) (Cytidine monophosphate-N-acetylneuraminic acid hydroxylase pseudogene) An Alu-mediated mutation of this gene occured in a common ancestor of Homo sapiens and Homo sapiens neanderthalis, approximately 2.1-2.2 million years ago, before brain expansion. It is generally accepted that the product of this gene, if any, is catalytically inactive as suggested by the absence of CMP-Neu5Gc sialic acid in human, while it is abundantly expressed at the surface of many cells in other vertebrates. The gene is however, significantly transcribed and the product described here might be expressed in vivo (PubMed:19890979). The putative protein is N-terminally truncated compared to orthologs and lacks a region probably essential to the CMP-N-acetylneuraminate monooxygenase activity. {ECO:0000269|PubMed:19890979, ECO:0000305|PubMed:11562455, ECO:0000305|PubMed:12192086, ECO:0000305|PubMed:9624188, ECO:0000305|PubMed:9751737}. degenerate-domain Q7L5N1 COPS6 Homo sapiens (Human) 9606 COP9 signalosome complex subunit 6 (SGN6) (Signalosome subunit 6) (JAB1-containing signalosome subunit 6) (MOV34 homolog) (Vpr-interacting protein) (hVIP) Although related to the peptidase M67A family, it lacks the JAMM motif that probably constitutes the catalytic center and therefore it probably does not have a protease activity. {ECO:0000305}. degenerate-domain Q8N436 CPXM2 Homo sapiens (Human) 9606 Inactive carboxypeptidase-like protein X2 Although related to peptidase M14 family, lacks the active site residues and zinc-binding sites, suggesting that it has no carboxypeptidase activity. {ECO:0000305}. degenerate-domain Q14194 CRMP1 Homo sapiens (Human) 9606 Dihydropyrimidinase-related protein 1 (DRP-1) (Collapsin response mediator protein 1) (CRMP-1) (Inactive dihydropyrimidinase) (Unc-33-like phosphoprotein 3) (ULIP-3) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q5NE16 CTSL3P Homo sapiens (Human) 9606 Putative inactive cathepsin L-like protein CTSL3P (Cathepsin L3 pseudogene) (HCTSL-s) Could be the product of a pseudogene. Lacks the region corresponding to the signal sequence and the propeptide. Has mutations in all 3 active site positions. {ECO:0000305}. degenerate-domain Q6ZSU1 CYP2G1P Homo sapiens (Human) 9606 Putative inactive cytochrome P450 2G1 (Cytochrome P450 2G1 pseudogene) Could be the product of a pseudogene. Probable pseudogene which is probably not functional. However, according to PubMed:11186129, some individuals may have an allele allowing the expression of a functional protein with an extended N-terminus. {ECO:0000305}. degenerate-domain Q8N1L4 CYP4Z2P Homo sapiens (Human) 9606 Putative inactive cytochrome P450 family member 4Z2 Could be the product of a pseudogene. In contrast to other members of the family, it is shorter at the C-terminus and lacks the heme-binding sites. {ECO:0000305}. degenerate-domain P27707 DCK Homo sapiens (Human) 9606 Deoxycytidine kinase (dCK) (EC 2.7.1.74) (Deoxyadenosine kinase) (EC 2.7.1.76) (Deoxyguanosine kinase) (EC 2.7.1.113) Was shown to be phosphorylated and activated by CSNK1D/CK1 in vitro but probably not in vivo. {ECO:0000305|PubMed:20637175}. degenerate-domain Q16555 DPYSL2 Homo sapiens (Human) 9606 Dihydropyrimidinase-related protein 2 (DRP-2) (Collapsin response mediator protein 2) (CRMP-2) (N2A3) (Unc-33-like phosphoprotein 2) (ULIP-2) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q14195 DPYSL3 Homo sapiens (Human) 9606 Dihydropyrimidinase-related protein 3 (DRP-3) (Collapsin response mediator protein 4) (CRMP-4) (Unc-33-like phosphoprotein 1) (ULIP-1) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain O14531 DPYSL4 Homo sapiens (Human) 9606 Dihydropyrimidinase-related protein 4 (DRP-4) (Collapsin response mediator protein 3) (CRMP-3) (UNC33-like phosphoprotein 4) (ULIP-4) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9BPU6 DPYSL5 Homo sapiens (Human) 9606 Dihydropyrimidinase-related protein 5 (DRP-5) (CRMP3-associated molecule) (CRAM) (Collapsin response mediator protein 5) (CRMP-5) (UNC33-like phosphoprotein 6) (ULIP-6) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q0D2K5 EGFEM1P Homo sapiens (Human) 9606 Putative EGF-like and EMI domain-containing protein 1 Could be the product of a pseudogene. The N-terminus is shorter and lacks the signal sequence compared to the mouse sequence, suggesting it may not be functional. {ECO:0000305}. degenerate-domain Q5JZY3 EPHA10 Homo sapiens (Human) 9606 Ephrin type-A receptor 10 (Inactive tyrosine-protein kinase EPHA10) Although this protein belongs to the kinase superfamily, it lacks key residues required for catalytic activity, suggesting that it does not have kinase activity. Despite the predicted lack of kinase activity, can bind ATP (PubMed:34431498). {ECO:0000269|PubMed:34431498, ECO:0000305|PubMed:34431498}. degenerate-domain O15197 EPHB6 Homo sapiens (Human) 9606 Ephrin type-B receptor 6 (HEP) (Tyrosine-protein kinase-defective receptor EPH-6) Although this protein belongs to the kinase superfamily, it lacks key residues required for catalytic activity, suggesting that it does not have kinase activity. In addition, lacks kinase activity in vitro (PubMed:34431498, PubMed:9207182). Despite the lack of kinase activity, can bind ATP (PubMed:34431498). {ECO:0000269|PubMed:34431498, ECO:0000269|PubMed:9207182, ECO:0000305|PubMed:34431498}. degenerate-domain Q96MK3 FAM20A Homo sapiens (Human) 9606 Pseudokinase FAM20A Although strongly related to other members of the family, lacks the kinase activity. A conserved Asp/Glu residue present in other members of the family, which coordinates the Mn(2+) ion and the ion-pair Lys and is indispensable for kinase activity, is replaced by a Gln in position 258. {ECO:0000269|PubMed:25789606}. degenerate-domain Q9UK05 GDF2 Homo sapiens (Human) 9606 Growth/differentiation factor 2 (GDF-2) (Bone morphogenetic protein 9) (BMP-9) Can promote osteogenic differentiation in vitro (PubMed:25237187, PubMed:25751889). This is probably not physiologically relevant. {ECO:0000269|PubMed:25237187, ECO:0000269|PubMed:25751889, ECO:0000305}. degenerate-domain Q3SXM5 HSDL1 Homo sapiens (Human) 9606 Inactive hydroxysteroid dehydrogenase-like protein 1 (Short chain dehydrogenase/reductase family 12C member 3) Although it belongs to the SDR family, Phe-218 is present instead of the conserved Tyr which is an active site residue. It is therefore expected that this protein lacks oxidoreductase activity. {ECO:0000305}. degenerate-domain Q8IVT5 KSR1 Homo sapiens (Human) 9606 Kinase suppressor of Ras 1 (EC 2.7.11.1) Although it belongs to the protein kinase superfamily, the ATP-binding motif VAIK has an arginine instead of a lysine residue suggesting that KSR1 cannot bind ATP and therefore lacks protein kinase activity. However, KSR1 is capable of binding ATP (PubMed:29433126). Has protein kinase activity towards MAP2K1 in the presence of RAF1/c-RAF in vitro (By similarity). {ECO:0000250|UniProtKB:Q61097, ECO:0000269|PubMed:29433126, ECO:0000305}. degenerate-domain Q6UWM7 LCTL Homo sapiens (Human) 9606 Lactase-like protein (Klotho/lactase-phlorizin hydrolase-related protein) Although it belongs to the glycosyl hydrolase 1 family, Asp-201 is present instead of the conserved Glu which is an active site residue. It is therefore expected that this protein lacks glycosidase activity. {ECO:0000305}. degenerate-domain Q96KX0 LYZL4 Homo sapiens (Human) 9606 Lysozyme-like protein 4 (Lysozyme-4) Although it belongs to the glycosyl hydrolase 22 family, Gly-72 is present instead of the conserved Asp which is an active site residue. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain Q2M2H8 MGAM2 Homo sapiens (Human) 9606 Probable maltase-glucoamylase 2 (Maltase-glucoamylase (alpha-glucosidase) pseudogene) [Includes: Glucoamylase (EC 3.2.1.3) (Glucan 1,4-alpha-glucosidase)] Although it belongs to the glycosyl hydrolase 31 family, it lacks one active site residue, thus suggesting it may lack some enzyme activity. {ECO:0000305}. degenerate-domain A8MYZ0 MINDY4B Homo sapiens (Human) 9606 Inactive ubiquitin carboxyl-terminal hydrolase MINDY-4B (Protein FAM188B2) In contrast to other members of the MINDY family, lacks the conserved active sites required for deubiquitination. {ECO:0000305}. degenerate-domain Q9H9J2 MRPL44 Homo sapiens (Human) 9606 Large ribosomal subunit protein mL44 (39S ribosomal protein L44, mitochondrial) (L44mt) (MRP-L44) Lacks RNase activity due to the absence of RNase-specific catalytic domain. {ECO:0000305|PubMed:11551941}. degenerate-domain Q2TV78 MST1L Homo sapiens (Human) 9606 Putative macrophage stimulating 1-like protein (Brain rescue factor 1) (BRF-1) (Hepatocyte growth factor-like protein homolog) Although it belongs to the peptidase S1 family, it lacks essential His, Asp, and Ser residues of the catalytic triad and is therefore predicted to lack peptidase activity. {ECO:0000305}. degenerate-domain Q9NXD2 MTMR10 Homo sapiens (Human) 9606 Myotubularin-related protein 10 (Inactive phosphatidylinositol 3-phosphatase 10) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 403 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain A4FU01 MTMR11 Homo sapiens (Human) 9606 Myotubularin-related protein 11 (Cisplatin resistance-associated protein) (hCRA) (Inactive phosphatidylinositol 3-phosphatase 11) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 375 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q9C0I1 MTMR12 Homo sapiens (Human) 9606 Myotubularin-related protein 12 (Inactive phosphatidylinositol 3-phosphatase 12) (Phosphatidylinositol 3 phosphate 3-phosphatase adapter subunit) (3-PAP) (3-phosphatase adapter protein) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 391 in the dsPTPase catalytic loop and does not have phosphatase activity. {ECO:0000305|PubMed:11504939}. degenerate-domain Q96QG7 MTMR9 Homo sapiens (Human) 9606 Myotubularin-related protein 9 (Inactive phosphatidylinositol 3-phosphatase 9) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 333 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q58DX5 NAALADL2 Homo sapiens (Human) 9606 Inactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2 (NAALADase L2) Although related to the peptidase M28 family, it lacks the conserved zinc-binding and active sites and therefore has probably lost hydrolase activity. {ECO:0000305}. degenerate-domain Q9UN36 NDRG2 Homo sapiens (Human) 9606 Protein NDRG2 (N-myc downstream-regulated gene 2 protein) (Protein Syld709613) Has some similarity to hydrolases, but lacks the conserved Ser-His-Asp catalytic triad. Has no hydrolase activity towards p-nitrophenylbutyrate (in vitro). {ECO:0000305}. degenerate-domain Q9HBL8 NMRAL1 Homo sapiens (Human) 9606 NmrA-like family domain-containing protein 1 Lacks the conserved Tyr residue in the active site triad of Ser-Tyr-Lys necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity. {ECO:0000305}. degenerate-domain Q8NE18 NSUN7 Homo sapiens (Human) 9606 Protein NSUN7 (NOL1/NOP2/Sun domain family member 7) In contrast to other NSUN family members, NSUN7 lacks RNA cytosine C5-methyltransferase activity, due to sequence variations in S-adenosyl-L-methionine(SAM)-binding residues. Substitution of the conserved SAM-binding Asp-373 with Leu-373 abolishes SAM binding and likely renders the enzyme catalytically inactive. {ECO:0000250|UniProtKB:Q14AW5}. degenerate-domain Q9BRJ7 NUDT16L1 Homo sapiens (Human) 9606 Tudor-interacting repair regulator protein (NUDT16-like protein 1) (Protein syndesmos) Although strongly related to the nudix NUDT16 protein, lacks the Nudix box and is therefore not related to the rest of the family (PubMed:18820299, PubMed:21070968). Gene organization and evolutionary distribution suggest that syndesmos NUDT16L1 probably originated as a gene duplication event of the more ancient U8 snoRNA-decapping enzyme NUDT16 (PubMed:18820299). Although similar to U8 snoRNA-decapping enzyme NUDT16, lacks a number of residues which are necessary for hydrolase activity and does not play a role in U8 snoRNA decapping activity (PubMed:21070968). {ECO:0000269|PubMed:18820299, ECO:0000269|PubMed:21070968}. degenerate-domain O43809 NUDT21 Homo sapiens (Human) 9606 Cleavage and polyadenylation specificity factor subunit 5 (Cleavage and polyadenylation specificity factor 25 kDa subunit) (CPSF 25 kDa subunit) (Cleavage factor Im complex 25 kDa subunit) (CFIm25) (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Nudix hydrolase 21) (Pre-mRNA cleavage factor Im 68 kDa subunit) Lacks the conserved metal-binding residues in the NUDIX motif and does not have hydrolase activity. {ECO:0000305}. degenerate-domain Q9NUU6 OTULINL Homo sapiens (Human) 9606 Inactive ubiquitin thioesterase OTULINL Although highly similar to the deubiquitinase OTULIN, lacks the conserved active site Cys at position 139 which is replaced by an Asp residue, and does not show deubiquitinase activity. {ECO:0000269|PubMed:31056421, ECO:0000305|PubMed:23708998}. degenerate-domain Q9UQ80 PA2G4 Homo sapiens (Human) 9606 Proliferation-associated protein 2G4 (Cell cycle protein p38-2G4 homolog) (hG4-1) (ErbB3-binding protein 1) Although it belongs to the peptidase M24 family, it does not contain metal cofactors and lacks aminopeptidase activity. {ECO:0000305|PubMed:17765895}. degenerate-domain Q6UXH9 PAMR1 Homo sapiens (Human) 9606 Inactive serine protease PAMR1 (Peptidase domain-containing protein associated with muscle regeneration 1) (Regeneration-associated muscle protease homolog) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 665 which is replaced by a Thr, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain Q9NVE7 PANK4 Homo sapiens (Human) 9606 4'-phosphopantetheine phosphatase (EC 3.1.3.-) (Inactive pantothenic acid kinase 4) (hPanK4) Despite belonging to the type II pantothenate kinase family, the pantothenate kinase domain contains a Val residue at position 147 and a Trp residue at position 211 instead of the two conserved active site residues, Glu and Arg. Lacks pantothenate kinase activity. {ECO:0000269|PubMed:30927326}. degenerate-domain Q8N8J0 PI4KAP1 Homo sapiens (Human) 9606 Putative inactive phosphatidylinositol 4-kinase alpha-like protein P1 Could be the product of a pseudogene. Much shorter than other members of the family and lacks the PI3K/PI4K catalytic domain. {ECO:0000305}. degenerate-domain Q5R387 PLA2G2C Homo sapiens (Human) 9606 Putative inactive group IIC secretory phospholipase A2 (Phosphatidylcholine 2-acylhydrolase-like protein GIIC) Ser-67 is present instead of the conserved His which is one of the active site residues. It is therefore expected that this protein lacks catalytic activity. {ECO:0000305}.; degenerate-domain Q15111 PLCL1 Homo sapiens (Human) 9606 Inactive phospholipase C-like protein 1 (PLC-L1) (Phospholipase C-deleted in lung carcinoma) (Phospholipase C-related but catalytically inactive protein) (PRIP) In the PI-PLC X-box Asn-458 is present instead of the conserved His which is one of the active site residues. It is therefore expected that this protein lacks catalytic activity. {ECO:0000305}. degenerate-domain Q9UPR0 PLCL2 Homo sapiens (Human) 9606 Inactive phospholipase C-like protein 2 (PLC-L(2)) (PLC-L2) (Phospholipase C-L2) (Phospholipase C-epsilon-2) (PLC-epsilon-2) In the PI-PLC X-box Thr-486 is present instead of the conserved His which is one of the active site residues. It is therefore expected that this protein lacks catalytic activity. {ECO:0000305}. degenerate-domain A8MPX8 PP2D1 Homo sapiens (Human) 9606 Protein phosphatase 2C-like domain-containing protein 1 Although it belongs to the protein phosphatase 2C family, it lacks some of the conserved residues that bind manganese, suggesting it has no phosphatase activity. {ECO:0000305}. degenerate-domain P22891 PROZ Homo sapiens (Human) 9606 Vitamin K-dependent protein Z Although related to peptidase S1 family vitamin K-dependent clotting factors, it has lost two of the essential catalytic residues and therefore lacks protease activity. {ECO:0000305}. degenerate-domain Q8N3Z0 PRSS35 Homo sapiens (Human) 9606 Inactive serine protease 35 Although related to peptidase S1 family, lacks the conserved active Ser residue in position 346 which is replaced by a Thr, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain A4D1T9 PRSS37 Homo sapiens (Human) 9606 Probable inactive serine protease 37 (Probable inactive trypsin-X2) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 192 which is replaced by an Ala, suggesting that it has no protease activity. Also lacks metal binding sites Glu in position 67 which is replaced by Asn, and Asn in position 69 which is replaced by Lys. {ECO:0000305}. degenerate-domain Q9UI38 PRSS50 Homo sapiens (Human) 9606 Probable threonine protease PRSS50 (EC 3.4.25.-) (Cancer/testis antigen 20) (Serine protease 50) (Testis-specific protease-like protein 50) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 310 which is replaced by a Thr. {ECO:0000305}. degenerate-domain A0A1B0GVH4 PRSS51 Homo sapiens (Human) 9606 Serine protease-like protein 51 Lacks essential residues of the catalytic triad and is therefore predicted to have no protease activity. {ECO:0000305}. degenerate-domain Q6PEW0 PRSS54 Homo sapiens (Human) 9606 Inactive serine protease 54 (Cancer/testis antigen 67) (CT67) (Plasma kallikrein-like protein 4) Although related to peptidase S1 family, lacks the essential His, Asp, and Ser residues of the catalytic triad at positions 83, 129 and 221 and is therefore predicted to have lost protease activity. {ECO:0000305}. degenerate-domain Q9NRG1 PRTFDC1 Homo sapiens (Human) 9606 Phosphoribosyltransferase domain-containing protein 1 Lacks the conserved active site Asp and has no significant phosphoribosyltransferase activity. {ECO:0000305}. degenerate-domain Q6T310 RASL11A Homo sapiens (Human) 9606 Ras-like protein family member 11A (EC 3.6.5.2) Although highly related to the Ras family, lacks the conserved prenylation motif at the C-terminus, which serves to target Ras proteins to membrane compartments. {ECO:0000305}. degenerate-domain Q6NTF9 RHBDD2 Homo sapiens (Human) 9606 Rhomboid domain-containing protein 2 Although strongly related to the peptidase S54 family, it lacks the conserved active sites, suggesting that it has no peptidase activity. {ECO:0000305}. degenerate-domain Q96CC6 RHBDF1 Homo sapiens (Human) 9606 Inactive rhomboid protein 1 (iRhom1) (Epidermal growth factor receptor-related protein) (Rhomboid 5 homolog 1) (Rhomboid family member 1) (p100hRho) Lacks serine protease activity as it lacks the catalytic Ser residue at position 720. {ECO:0000269|PubMed:21439629, ECO:0000305|PubMed:15965977}. degenerate-domain P50876 RNF144A Homo sapiens (Human) 9606 E3 ubiquitin-protein ligase RNF144A (EC 2.3.2.31) (RING finger protein 144A) (UbcM4-interacting protein 4) (Ubiquitin-conjugating enzyme 7-interacting protein 4) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q7Z419 RNF144B Homo sapiens (Human) 9606 E3 ubiquitin-protein ligase RNF144B (EC 2.3.2.31) (IBR domain-containing protein 2) (RING finger protein 144B) (p53-inducible RING finger protein) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain P34925 RYK Homo sapiens (Human) 9606 Inactive tyrosine-protein kinase RYK (H-Ryk) Although this protein belongs to the kinase superfamily, it lacks key residues required for catalytic activity, suggesting that it does not have kinase activity. A chimeric receptor consisting of the extracellular domain of NTRK1/TRKA fused to the transmembrane and cytoplasmic domains of RYK is catalytically inactive (PubMed:10454588). Does not bind ATP (PubMed:24107129, PubMed:32619402). {ECO:0000269|PubMed:10454588, ECO:0000269|PubMed:24107129, ECO:0000269|PubMed:32619402, ECO:0000305|PubMed:11135307}. degenerate-domain O95248 SBF1 Homo sapiens (Human) 9606 Myotubularin-related protein 5 (Inactive phosphatidylinositol 3-phosphatase 5) (SET-binding factor 1) (Sbf1) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 1422 in the dsPTPase catalytic loop and does not have phosphatase activity (PubMed:9537414). The pocket is however sufficiently preserved to bind phosphorylated substrates, and maybe protect them from phosphatases. {ECO:0000269|PubMed:9537414, ECO:0000305}. degenerate-domain Q86WG5 SBF2 Homo sapiens (Human) 9606 Myotubularin-related protein 13 (Inactive phosphatidylinositol 3-phosphatase 13) (SET-binding factor 2) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 1410 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q53S99 SLC19A4P Homo sapiens (Human) 9606 Putative solute carrier family 19 member 4 (Folate transporter-like protein C2orf83) (Solute carrier family 19 member 4, pseudogene) Although related to reduced folate carrier family, it lacks transmembrane domains, suggesting that it has probably no transporter function. Defined as a pseudogene by HGNC. {ECO:0000305}. degenerate-domain Q8IXA5 SPACA3 Homo sapiens (Human) 9606 Sperm acrosome membrane-associated protein 3 (Cancer/testis antigen 54) (CT54) (Lysozyme-like acrosomal sperm-specific secretory protein ALLP-17) (Lysozyme-like protein 3) (Sperm lysozyme-like protein 1) (Sperm protein reactive with antisperm antibodies) (Sperm protein reactive with ASA) [Cleaved into: Sperm acrosome membrane-associated protein 3, membrane form; Sperm acrosome membrane-associated protein 3, processed form] Although it belongs to the glycosyl hydrolase 22 family, Thr-122 and Asn-139 are present instead of the conserved Glu and Asp which are active site residues. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain Q658P3 STEAP3 Homo sapiens (Human) 9606 Metalloreductase STEAP3 (EC 1.16.1.-) (Dudulin-2) (Six-transmembrane epithelial antigen of prostate 3) (Tumor suppressor-activated pathway protein 6) (hTSAP6) (pHyde) (hpHyde) Was initially thought to have tumor suppressor function in prostate cancer. However, it was shown that it is probably not the case (PubMed:12866033). {ECO:0000305|PubMed:12866033}. degenerate-domain Q9Y6J8 STYXL1 Homo sapiens (Human) 9606 Serine/threonine/tyrosine-interacting-like protein 1 (Dual specificity phosphatase inhibitor MK-STYX) (Dual specificity protein phosphatase 24) (Inactive dual specificity protein phosphatase MK-STYX) (Map kinase phosphatase-like protein MK-STYX) Lacks the two active site residues His and Cys at position 245 and 246 which are essential for dual-specificity phosphatase activity. Lacks phosphatase activity. {ECO:0000269|PubMed:20180778, ECO:0000269|PubMed:23163895}. degenerate-domain Q8NBK3 SUMF1 Homo sapiens (Human) 9606 Formylglycine-generating enzyme (FGE) (EC 1.8.3.7) (C-alpha-formylglycine-generating enzyme 1) (Sulfatase-modifying factor 1) The disulfide bond observed in the structure does not exist in vivo (PubMed:15907468). The enzyme reaction was initially thought to act via a redox-active disulfide bond mechanism; however the disulfide bond only takes place with inactive enzyme that lacks the copper cofactor (PubMed:25931126). The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation (PubMed:25931126). {ECO:0000269|PubMed:15907468, ECO:0000269|PubMed:25931126}. degenerate-domain Q8NBJ7 SUMF2 Homo sapiens (Human) 9606 Inactive C-alpha-formylglycine-generating enzyme 2 (Paralog of formylglycine-generating enzyme) (pFGE) (Sulfatase-modifying factor 2) Although strongly similar to formylglycine-generating enzyme, lacks the catalytic Cys residues at positions 261 and 266 that bind the catalytic copper. The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation. {ECO:0000305}. degenerate-domain Q9Y5B9 SUPT16H Homo sapiens (Human) 9606 FACT complex subunit SPT16 (Chromatin-specific transcription elongation factor 140 kDa subunit) (FACT 140 kDa subunit) (FACTp140) (Facilitates chromatin transcription complex subunit SPT16) (hSPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q15750 TAB1 Homo sapiens (Human) 9606 TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 1) (TGF-beta-activated kinase 1-binding protein 1) (TAK1-binding protein 1) Lacks several key residues involved in metal-binding and catalytic activity, therefore has lost phosphatase activity. {ECO:0000303|PubMed:16879102}. degenerate-domain P01266 TG Homo sapiens (Human) 9606 Thyroglobulin (Tg) The cholinesterase-like (ChEL) region lacks the Ser residue of the catalytic triad suggesting that it has no esterase activity. {ECO:0000305}. degenerate-domain Q15399 TLR1 Homo sapiens (Human) 9606 Toll-like receptor 1 (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9BXR5 TLR10 Homo sapiens (Human) 9606 Toll-like receptor 10 (CD antigen CD290) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain O60603 TLR2 Homo sapiens (Human) 9606 Toll-like receptor 2 (Toll/interleukin-1 receptor-like protein 4) (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain O00206 TLR4 Homo sapiens (Human) 9606 Toll-like receptor 4 (hToll) (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (PubMed:28334607). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (PubMed:28334607). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000269|PubMed:28334607, ECO:0000305}. degenerate-domain Q9Y2C9 TLR6 Homo sapiens (Human) 9606 Toll-like receptor 6 (CD antigen CD286) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain O94759 TRPM2 Homo sapiens (Human) 9606 Transient receptor potential cation channel subfamily M member 2 (Estrogen-responsive element-associated gene 1 protein) (Long transient receptor potential channel 2) (LTrpC-2) (LTrpC2) (Transient receptor potential channel 7) (TrpC7) (Transient receptor potential melastatin 2) The isolated nudix hydrolase domain was shown to have low catalytic activity with ADP-ribose upon heterologous expression (PubMed:11385575). However, a more recent publication demonstrates that the nudix hydrolase domain lacks enzyme activity and suggests that spontaneous degradation of the substrate underlies the previously reported low activity (PubMed:27383051). {ECO:0000269|PubMed:11385575, ECO:0000269|PubMed:27383051}. degenerate-domain Q14166 TTLL12 Homo sapiens (Human) 9606 Tubulin--tyrosine ligase-like protein 12 (Inactive tubulin--tyrosine ligase-like protein 12) Although it belongs to the tubulin--tyrosine ligase family, the TTL domain lacks some of the ATP binding sites predicted to be essential for TTL activity (PubMed:23251473). Lacks tyrosine ligase activity in vitro (PubMed:23251473). Lacks glutamylation activity in vitro (By similarity). Although TTLL12 contains a potential SET-like domain in the N-terminus, it does not have lysine methyltransferase activity towards histone in vitro (PubMed:23251473). {ECO:0000250|UniProtKB:Q3UDE2, ECO:0000269|PubMed:23251473}. degenerate-domain Q8IWF7 UBE2DNL Homo sapiens (Human) 9606 Putative ubiquitin-conjugating enzyme E2 D2-like protein (Ubiquitin carrier protein D2-like) (Ubiquitin-conjugating enzyme E2D N-terminal-like) (Ubiquitin-protein ligase D2-like) Could be the product of a pseudogene. Probably inactive as a ubiquitin-conjugating enzyme since it lacks the essential active site cysteine. {ECO:0000305}. degenerate-domain A6NNY8 USP27X Homo sapiens (Human) 9606 Ubiquitin carboxyl-terminal hydrolase 27 (EC 3.4.19.12) (Deubiquitinating enzyme 27) (Ubiquitin carboxyl-terminal hydrolase 22-like) (Ubiquitin thioesterase 27) (Ubiquitin-specific-processing protease 27) (X-linked ubiquitin carboxyl-terminal hydrolase 27) Although strongly related to USP22, which deubiquitinates histones, lacks the N-terminal UBP-type zinc finger, suggesting it does not have the ability to deubiquitinate histones. {ECO:0000305}. degenerate-domain Q53GS9 USP39 Homo sapiens (Human) 9606 Ubiquitin carboxyl-terminal hydrolase 39 (EC 3.4.19.12) (SAD1 homolog) (U4/U6.U5 tri-snRNP-associated 65 kDa protein) Lacks the conserved His and Cys residues that are essential for the activity of de-ubiquitinating enzymes. Lacks ubiquitin C-terminal hydrolase activity (PubMed:18728397). {ECO:0000269|PubMed:18728397, ECO:0000305|PubMed:11350945}. degenerate-domain Q96FA7 ZBED10P Homo sapiens (Human) 9606 Putative protein ZBED10P (ZBED6 C-terminal-like protein) (zinc finger BED-type containing 10 pseudogene) Could be the product of a pseudogene. Similar to the C-terminus of ZBED6, but lacks BED domains, and therefore is probably not involved in transcriptional regulation. Encoded by a DNA transposon located in the 5'-untranslated region (5'-UTR) of LRRC61. {ECO:0000305}. degenerate-domain Q7YN52 psbN Hookeria lucens (Moss) (Hypnum lucens) 65539 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A1E9L8 psbN Hordeum vulgare (Barley) 4513 Protein PsbN Originally thought to be a component of PSII; based on experiments in this organism, Synechocystis and N.tabacum, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293, ECO:0000305|PubMed:19137553}. degenerate-domain Q6EYH8 psbN Houttuynia cordata (Chameleon plant) 16752 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P16782 RIR1 Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) 10360 Ribonucleoside-diphosphate reductase large subunit-like protein Lacks the conserved sequence Asn-x-Cys-x-Glu essential for ribonucleotide reductase activity. {ECO:0000255|HAMAP-Rule:MF_04027}. degenerate-domain Q6SW87 RIR1 Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5) 295027 Ribonucleoside-diphosphate reductase large subunit-like protein Lacks the conserved sequence Asn-x-Cys-x-Glu essential for ribonucleotide reductase activity. {ECO:0000255|HAMAP-Rule:MF_04027}. degenerate-domain P52343 RIR1 Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B lymphotropic virus) 10370 Ribonucleoside-diphosphate reductase large subunit-like protein Lacks the conserved sequence Asn-x-Cys-x-Glu essential for ribonucleotide reductase activity. {ECO:0000255|HAMAP-Rule:MF_04027}. degenerate-domain Q9QJ39 RIR1 Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic virus) 36351 Ribonucleoside-diphosphate reductase large subunit-like protein Lacks the conserved sequence Asn-x-Cys-x-Glu essential for ribonucleotide reductase activity. {ECO:0000255|HAMAP-Rule:MF_04027}. degenerate-domain P50641 RIR1 Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus) 57278 Ribonucleoside-diphosphate reductase large subunit-like protein Lacks the conserved sequence Asn-x-Cys-x-Glu essential for ribonucleotide reductase activity. {ECO:0000255|HAMAP-Rule:MF_04027}. degenerate-domain Q5SD31 psbN Huperzia lucidula (Shining clubmoss) (Lycopodium lucidulum) 37429 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7HIW4 psbN Hydrastis canadensis (Goldenseal) 13569 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q71NS7 psbN Hylocomium splendens (Glittering wood-moss) (Hypnum splendens) 53007 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q71P68 psbN Hypnum cupressiforme (Cypress-leaved plait-moss) 53011 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B3FWR7 hpm1 Hypomyces subiculosus (Nectria subiculosa) 193393 Cytochrome P450 monooxygenase hmp1 (EC 1.-.-.-) (Hypothemycin biosynthesis cluster protein hpm1) In contrast to other members of the family, it is shorter at the C-terminus and lacks the heme-binding sites. {ECO:0000305}. degenerate-domain P0CC74 ndhB1 Illicium oligandrum (Star anise) 145286 NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase, subunit 2 A) (NADH-plastoquinone oxidoreductase subunit 2 A) This protein is smaller than usual in this organism, and may not be functional. {ECO:0000305}. degenerate-domain P0CC75 ndhB2 Illicium oligandrum (Star anise) 145286 NAD(P)H-quinone oxidoreductase subunit 2 B, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase, subunit 2 B) (NADH-plastoquinone oxidoreductase subunit 2 B) This protein is smaller than usual in this organism, and may not be functional. {ECO:0000305}. degenerate-domain A6MMX2 psbN Illicium oligandrum (Star anise) 145286 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7J190 psbN Illicium parviflorum (Yellow anise tree) (Badianifera parviflora) 13099 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain O04795 Ipomoea batatas (Sweet potato) (Convolvulus batatas) 4120 Anionic peroxidase (EC 1.11.1.7) (SwPA1) Lacks one of the disulfide bridges highly conserved in the class III peroxidase family. {ECO:0000305}. degenerate-domain A7Y3H6 psbN Ipomoea purpurea (Common morning glory) (Pharbitis purpurea) 4121 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q06RA4 psbN Jasminum nudiflorum (Winter jasmine) 126431 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A6W6D1 Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) 266940 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q71KN5 psbN Klebsormidium bilatum (Filamentous green alga) 201239 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q00976 SPT16 Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) 284590 FACT complex subunit SPT16 (Cell division control protein 68) (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q9CG32 ynbA Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) 272623 Tyrosine recombinase XerD-like Although strongly related to XerD, it constitutes a distinct protein family. In contrast to the classic XerD protein, it does not contain the Arg-His-Arg-His (R-H-R-H) sandwich residues that are clustered with the Tyr active site. It also lacks the C-terminal region which is known to mediate the interaction with XerC. It is therefore unknown whether it has tyrosine recombinase activity or acts as a regulator. {ECO:0000305}. degenerate-domain P62692 L3 Lactococcus phage c2 2681624 Endolysin (EC 3.2.1.17) (Lysis protein) (Lysozyme) (Muramidase) Lacks the conserved Asp active site. {ECO:0000255|HAMAP-Rule:MF_04110}. degenerate-domain P62693 L3 Lactococcus phage phivML3 (Lactococcus bacteriophage phi-vML3) 10746 Endolysin (EC 3.2.1.17) (Lysis protein) (Lysozyme) (Muramidase) Lacks the conserved Asp active site. {ECO:0000255|HAMAP-Rule:MF_04110}. degenerate-domain Q9GF77 psbN Lactoris fernandeziana 22303 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q332U9 psbN Lactuca sativa (Garden lettuce) 4236 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P10117 Laticauda colubrina (Yellow-lipped sea krait) (Banded sea krait) 8628 Basic phospholipase A2 homolog 1 (svPLA2 homolog) (Phospholipase A2 homolog I) (PLH-I) In contrast to other phospholipases, it lacks the typical Asp active site (Asp->Asn in position 75). {ECO:0000305}. degenerate-domain A4ZZ93 Leishmania donovani 5661 Inactive deoxyhypusine synthase (Deoxyhypusine synthase-like protein) (Deoxyhypusine synthase-like protein from chromosome 20) (DHSL20) Although similar to deoxyhypusine synthase, lacks the active site Lys at position 344 and does not show deoxyhypusine synthase activity. Converting Leu-344 to a lysine does not restore activity. {ECO:0000305}. degenerate-domain A9L9C4 psbN Lemna minor (Common duckweed) 4472 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A4QLD4 psbN Lepidium virginicum (Virginia pepperweed) 59292 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8WQ47 Lepidoglyphus destructor (Storage mite) (Glycyphagus destructor) 36936 Tubulin alpha chain (EC 3.6.5.-) (allergen Lep d ?) This protein lacks the required Tyr in position 450; it is replaced by a Phe. {ECO:0000305}. degenerate-domain Q6Q888 sirQ Leptosphaeria maculans (Blackleg fungus) (Phoma lingam) 5022 Short chain dehydrogenase sirQ (EC 1.-.-.-) (Sirodesmin biosynthesis protein Q) It is uncertain whether sirQ is an active short chain dehydrogenase since it lacks the conserved active sites. {ECO:0000305}. degenerate-domain Q6Q885 sirR Leptosphaeria maculans (Blackleg fungus) (Phoma lingam) 5022 Short chain dehydrogenase sirR (EC 1.-.-.-) (Sirodesmin biosynthesis protein R) It is uncertain whether sirR is an active short chain dehydrogenase since it lacks the conserved active sites. {ECO:0000305}. degenerate-domain Q6Q878 sirS Leptosphaeria maculans (Blackleg fungus) (Phoma lingam) 5022 Short chain dehydrogenase sirS (EC 1.-.-.-) (Sirodesmin biosynthesis protein S) It is uncertain whether sirS is an active short chain dehydrogenase since it lacks the conserved active sites. {ECO:0000305}. degenerate-domain E5A0U8 ECM14 Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam) 985895 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 504 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q8F2D1 argF Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) 189518 Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3) Lacks the conserved cysteine and leucine residues in positions 269 and 270, respectively, which are part of the ornithine binding site; they are replaced by an aspartate and a methionine residue, respectively. {ECO:0000305}. degenerate-domain Q72T26 argF Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) 267671 Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3) Lacks the conserved cysteine and leucine residues in positions 269 and 270, respectively, which are part of the ornithine binding site; they are replaced by an aspartate and a methionine residue, respectively. {ECO:0000305}. degenerate-domain Q71NV7 psbN Leucodon sciuroides (Moss) 69533 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7HIW2 psbN Lilium superbum (Turk's cap lily) (Lilium canadense subsp. superbum) 4692 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7J187 psbN Liriodendron tulipifera (Tuliptree) (Tulip poplar) 3415 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A4QLM2 psbN Lobularia maritima (Sweet alyssum) (Alyssum maritimum) 226051 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A8Y9B4 psbN Lolium perenne (Perennial ryegrass) 4522 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7YN54 psbN Lopidium concinnum (Moss) (Leskea concinna) 69843 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P68859 psbN Lotus japonicus (Lotus corniculatus var. japonicus) 34305 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain D9J142 Lucilia sericata (Green bottle fly) (Phaenicia sericata) 13632 Inactive lysozyme 1A Although it belongs to the glycosyl hydrolase 22 family, Gly-51 is present instead of the conserved Glu which is an active site residue. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain Q96474 LEG1 Lupinus angustifolius (Narrow-leaved blue lupine) 3871 Albumin-1 (A1) [Cleaved into: Albumin-1 chain b (A1b) (Leginsulin); Albumin-1 chain a (A1a)] While it is structurally defined as a knottin it lacks the conserved Cys residue in position 4. {ECO:0000305}. degenerate-domain B6DD20 Lycosa singoriensis (Wolf spider) (Aranea singoriensis) 434756 U13-lycotoxin-Ls1c (Toxin-like structure LSTX-L2) In contrast to other members of this family, lacks the conserved Cys in position 69, which is replaced by an Arg. {ECO:0000305}. degenerate-domain Q4R5E1 AKTIP Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) 9541 AKT-interacting protein (Fused toes protein homolog) Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q4R7Q1 NSUN7 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) 9541 Protein NSUN7 (NOL1/NOP2/Sun domain family member 7) In contrast to other NSUN family members, NSUN7 lacks RNA cytosine C5-methyltransferase activity, due to sequence variations in S-adenosyl-L-methionine(SAM)-binding residues. Substitution of the conserved SAM-binding Asp-358 with Leu-358 abolishes SAM binding and likely renders the enzyme catalytically inactive. {ECO:0000250|UniProtKB:Q14AW5}. degenerate-domain Q4R4U1 PANK4 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) 9541 4'-phosphopantetheine phosphatase (EC 3.1.3.-) (Inactive pantothenic acid kinase 4) Despite belonging to the type II pantothenate kinase family, the pantothenate kinase domain contains a Val residue at position 147 and a Trp residue at position 211 instead of the two conserved active site residues, Glu and Arg. Lacks pantothenate kinase activity. {ECO:0000250|UniProtKB:Q9NVE7}. degenerate-domain Q4R7Y7 PRSS37 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) 9541 Probable inactive serine protease 37 (Probable inactive trypsin-X2) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 192 which is replaced by an Ala, suggesting that it has no protease activity. Also lacks metal binding sites Glu in position 67 which is replaced by Asn, and Asn in position 69 which is replaced by Lys. {ECO:0000305}. degenerate-domain Q95M53 TLR2 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) 9541 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q1WK24 PRSS35 Macaca mulatta (Rhesus macaque) 9544 Inactive serine protease 35 Although related to peptidase S1 family, lacks the conserved active Ser residue in position 342 which is replaced by a Thr, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain B3Y618 TLR2 Macaca mulatta (Rhesus macaque) 9544 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q8HS28 psbN Magnolia stellata (Star magnolia) (Buergeria stellata) 54733 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q67HT8 psbN Maianthemum racemosum (False Solomon's-seal) (Smilacina racemosa) 39530 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain L0E4F8 malC Malbranchea aurantiaca 78605 Short-chain dehydrogenase/reductase malC (EC 1.1.-.-) (Malbrancheamide biosynthesis cluster protein C) MalC lacks the characteristic Tyr and Lys catalytic amino acids, and also the essential Asn and Ser residues of typical SDR family proteins, suggesting that the active site is reconfigured to fit its unique catalytic roles. {ECO:0000269|PubMed:31548667}. degenerate-domain A9XVQ4 psbN Manihot esculenta (Cassava) (Jatropha manihot) 3983 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P12170 psbN Marchantia polymorpha (Common liverwort) (Marchantia aquatica) 3197 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q601U6 pheT Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae) 295358 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved glutamate residue in position 447 that binds magnesium; it is replaced by an alanine residue. {ECO:0000305}. degenerate-domain Q4A891 pheT Mesomycoplasma hyopneumoniae (strain 7448) (Mycoplasma hyopneumoniae) 262722 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved glutamate residue in position 447 that binds magnesium; it is replaced by an alanine residue. {ECO:0000305}. degenerate-domain Q4AA64 pheT Mesomycoplasma hyopneumoniae (strain J / ATCC 25934 / NCTC 10110) (Mycoplasma hyopneumoniae) 262719 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved glutamate residue in position 447 that binds magnesium; it is replaced by an alanine residue. {ECO:0000305}. degenerate-domain Q9MUV5 psbN Mesostigma viride (Green alga) 41882 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q71L94 psbN Metasequoia glyptostroboides (Dawn redwood) (Sequoia glyptostroboides) 3371 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q58138 cooS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) 243232 Carbon monoxide dehydrogenase (CODH) (EC 1.2.7.4) This protein lacks the conserved Cys in position 45; it is replaced by a Tyr. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form homodimers. {ECO:0000305}. degenerate-domain Q8TWG4 argF Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) 190192 Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3) Lacks the conserved leucine residue in position 272, which is part of the ornithine binding site; it is replaced by a methionine residue. {ECO:0000305}. degenerate-domain Q8TXF5 cdhA2 Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) 190192 Putative acetyl-CoA decarbonylase/synthase complex subunit alpha-like (ACDS complex subunit alpha-like) (ACDS complex carbon monoxide dehydrogenase subunit alpha-like) (ACDS CODH subunit alpha-like) This protein lacks several conserved Cys residues that bind [4Fe-4S] clusters in other CODHs. Therefore, it is not clear whether this protein is active. However, the protein would be able to bind a [Ni-4Fe-4S] cluster, which is the active site of CO oxidation. {ECO:0000305}. degenerate-domain Q8TXX3 cooS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) 190192 Carbon monoxide dehydrogenase (CODH) (EC 1.2.7.4) This protein lacks the conserved Cys in position 54; it is replaced by a Trp. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form homodimers. {ECO:0000305}. degenerate-domain Q8TR73 cooS2 Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) 188937 Carbon monoxide dehydrogenase 2 (CODH 2) (EC 1.2.7.4) This protein lacks the conserved Cys in positions 52 and 300; they are replaced by an Arg and a Glu, respectively. It is therefore possible that the C- and D-clusters are either altered or missing in this protein. {ECO:0000305}. degenerate-domain Q8PUN1 cooS2 Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) 192952 Carbon monoxide dehydrogenase 2 (CODH 2) (EC 1.2.7.4) This protein lacks the conserved Cys in positions 52 and 300; they are replaced by an Arg and a Glu, respectively. It is therefore possible that the C- and D-clusters are either altered or missing in this protein. {ECO:0000305}. degenerate-domain O26978 Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) 187420 Putative lon protease homolog (EC 3.4.21.-) (ATP-dependent protease La homolog) Lacks the conserved Ser-Lys catalytic dyad essential for proteolytic activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain O27190 ppsA Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) 187420 Probable phosphoenolpyruvate synthase (PEP synthase) (EC 2.7.9.2) (Pyruvate, water dikinase) Lacks some of the catalytic-important sites due to premature sequence termination compared to the close ortholog in M.jannaschii. The missing 250 amino acids or so may be retrieved through a serie of sequence corrections. {ECO:0000305}. degenerate-domain P26692 cdhA Methanothrix soehngenii (Methanosaeta concilii) 2223 Acetyl-CoA decarbonylase/synthase complex subunit alpha (ACDS complex subunit alpha) (EC 1.2.7.4) (ACDS complex carbon monoxide dehydrogenase subunit alpha) (ACDS CODH subunit alpha) This protein lacks the conserved Cys in positions 52 and 56; they are replaced by an Asp and a Thr, respectively. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form heterotetramers. {ECO:0000305}. degenerate-domain B0JNP9 psbN1 Microcystis aeruginosa (strain NIES-843 / IAM M-2473) 449447 Protein PsbN 1 Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B0JNP7 psbN2 Microcystis aeruginosa (strain NIES-843 / IAM M-2473) 449447 Protein PsbN 2 Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9K4Y9 argF Moritella abyssi 111292 Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3) Lacks the conserved threonine and leucine residues in positions 50 and 261, respectively, which are part of the carbamoylphosphate and ornithine binding sites; they are replaced by a leucine and a glutamine residue, respectively. {ECO:0000305|PubMed:12644485}. degenerate-domain Q9K4Z4 argF Moritella profunda 111291 Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3) Lacks the conserved threonine and leucine residues in positions 50 and 261, respectively, which are part of the carbamoylphosphate and ornithine binding sites; they are replaced by a leucine and a glutamine residue, respectively. {ECO:0000305}. degenerate-domain Q09WY9 psbN Morus indica (Mulberry) 248361 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q06A28 RIR1 Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus) 10367 Ribonucleoside-diphosphate reductase large subunit-like protein (Viral inhibitor of RIP activation) [Cleaved into: N-terminal peptide; 116 kDa peptide] Lacks the conserved sequence Asn-x-Cys-x-Glu essential for ribonucleotide reductase activity. {ECO:0000255|HAMAP-Rule:MF_04027}. degenerate-domain Q99LE6 Abcf2 Mus musculus (Mouse) 10090 ATP-binding cassette sub-family F member 2 Lacks transmembrane domains and is probably not involved in transport. {ECO:0000305}. degenerate-domain Q8K268 Abcf3 Mus musculus (Mouse) 10090 ATP-binding cassette sub-family F member 3 Lacks transmembrane domains and is probably not involved in transport. {ECO:0000305}. degenerate-domain Q3TCJ1 Abraxas2 Mus musculus (Mouse) 10090 BRISC complex subunit Abraxas 2 (Abraxas brother protein 1) (Protein FAM175B) Although strongly related to the ABRAXAS1 protein, lacks the C-terminal pSXXF that constitutes a specific recognition motif for the BRCT domain of BRCA1. {ECO:0000305}. degenerate-domain D0G895 Ace3 Mus musculus (Mouse) 10090 Angiotensin-converting enzyme-like protein Ace3 Lacks the conserved Glu residue in position 378 necessary for the catalytic activity. {ECO:0000305}. degenerate-domain Q8BLI0 Adamtsl1 Mus musculus (Mouse) 10090 ADAMTS-like protein 1 (ADAMTSL-1) (Punctin-1) Although strongly similar to members of the ADAMTS family it lacks the metalloprotease and disintegrin-like domains which are typical of that family. {ECO:0000305}. degenerate-domain Q7TSK7 Adamtsl2 Mus musculus (Mouse) 10090 ADAMTS-like protein 2 (ADAMTSL-2) (TSP1-repeat-containing protein 1) (TCP-1) Although strongly similar to members of the ADAMTS family it lacks the metalloprotease and disintegrin-like domains which are typical of that family. {ECO:0000305}. degenerate-domain Q80T21 Adamtsl4 Mus musculus (Mouse) 10090 ADAMTS-like protein 4 (ADAMTSL-4) (Thrombospondin repeat-containing protein 1) Although similar to members of the ADAMTS family, it lacks the metalloprotease and disintegrin-like domains which are typical of that family. {ECO:0000305}. degenerate-domain Q9JI20 Adarb2 Mus musculus (Mouse) 10090 Inactive double-stranded RNA-specific editase B2 (RNA-dependent adenosine deaminase 3) (RNA-editing deaminase 2) (RNA-editing enzyme 2) (dsRNA adenosine deaminase B2) Although it is similar to the double-stranded RNA adenosine deaminases ADAR/ADAR1 and ADARB1/ADAR2 and capable of binding RNA, it lacks double-stranded RNA adenosine deaminase activity in vitro. Instead, it inhibits adenosine-to-inosine editing in vivo. {ECO:0000250|UniProtKB:Q9NS39}. degenerate-domain G3UZ78 Adgb Mus musculus (Mouse) 10090 Androglobin May contribute directly or indirectly to the proteolytic cleavage of SEPT10 (PubMed:35700329). However, the calpain domain lacks the conserved active site suggesting it is probably catalytically inactive as a calcium-dependent cysteine-type endopeptidase. {ECO:0000269|PubMed:35700329, ECO:0000305}. degenerate-domain Q8BGK2 Adprhl1 Mus musculus (Mouse) 10090 Inactive ADP-ribosyltransferase ARH2 (ADP-ribosylhydrolase-like protein 1) ([Protein ADP-ribosylarginine] hydrolase-like protein 1) Although it belongs to the ADP-ribosylglycohydrolase family, lacks the metal-binding and substrate-binding residues, suggesting that it has no hydrolase activity. {ECO:0000250|UniProtKB:Q6AZR2}. degenerate-domain Q640N1 Aebp1 Mus musculus (Mouse) 10090 Adipocyte enhancer-binding protein 1 (AE-binding protein 1) (Aortic carboxypeptidase-like protein) Although related to peptidase M14 family, lacks the active site residues and zinc-binding sites, suggesting that it has no carboxypeptidase activity. {ECO:0000305}. degenerate-domain Q64362 Aktip Mus musculus (Mouse) 10090 AKT-interacting protein (FT1) (Fused toes protein) Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q6ZPS6 Ankib1 Mus musculus (Mouse) 10090 Ankyrin repeat and IBR domain-containing protein 1 (EC 2.3.2.31) Lacks one Cys residue in the IBR-type zinc finger domain that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain P28651 Ca8 Mus musculus (Mouse) 10090 Carbonic anhydrase-related protein (CARP) (Carbonic anhydrase VIII) (CA-VIII) Although it belongs to the alpha-carbonic anhydrase family, Arg-117 is present instead of the conserved His which is a zinc-binding residue. It is therefore expected that this protein lacks carbonic anhydrase activity. {ECO:0000305}. degenerate-domain Q61362 Chi3l1 Mus musculus (Mouse) 10090 Chitinase-3-like protein 1 (BRP39 protein) (Breast regression protein 39) (Cartilage glycoprotein 39) (CGP-39) (GP-39) Although it belongs to the glycosyl hydrolase 18 family, Leu-149 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity. {ECO:0000305}. degenerate-domain Q8BUG2 Cndp1 Mus musculus (Mouse) 10090 Beta-Ala-His dipeptidase (EC 3.4.13.20) (CNDP dipeptidase 1) (Carnosine dipeptidase 1) In contrast to the human protein, it is unlikely to be secreted because it lacks the N-terminal signal sequence required for secretion. Furthermore, its activity was assessed from the soluble fraction prepared from tissues or cells not from a secreted fraction. It could also have a slightly different substrate specificity. {ECO:0000305|PubMed:24891507}. degenerate-domain O88545 Cops6 Mus musculus (Mouse) 10090 COP9 signalosome complex subunit 6 (SGN6) (Signalosome subunit 6) (JAB1-containing signalosome subunit 6) Although related to the peptidase M67A family, it lacks the JAMM motif that probably constitutes the catalytic center and therefore it probably does not have a protease activity. {ECO:0000305}. degenerate-domain Q9D2L5 Cpxm2 Mus musculus (Mouse) 10090 Inactive carboxypeptidase-like protein X2 Although related to peptidase M14 family, lacks the active site residues and zinc-binding sites, suggesting that it has no carboxypeptidase activity. {ECO:0000305}. degenerate-domain P97427 Crmp1 Mus musculus (Mouse) 10090 Dihydropyrimidinase-related protein 1 (DRP-1) (Collapsin response mediator protein 1) (CRMP-1) (Inactive dihydropyrimidinase) (Unc-33-like phosphoprotein 3) (ULIP-3) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain O08553 Dpysl2 Mus musculus (Mouse) 10090 Dihydropyrimidinase-related protein 2 (DRP-2) (Unc-33-like phosphoprotein 2) (ULIP-2) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q62188 Dpysl3 Mus musculus (Mouse) 10090 Dihydropyrimidinase-related protein 3 (DRP-3) (Unc-33-like phosphoprotein 1) (ULIP-1) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain O35098 Dpysl4 Mus musculus (Mouse) 10090 Dihydropyrimidinase-related protein 4 (DRP-4) (Collapsin response mediator protein 3) (CRMP-3) (UNC33-like phosphoprotein 4) (ULIP-4) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9EQF6 Dpysl5 Mus musculus (Mouse) 10090 Dihydropyrimidinase-related protein 5 (DRP-5) (Collapsin response mediator protein 5) (CRMP-5) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q8BYG9 Epha10 Mus musculus (Mouse) 10090 Ephrin type-A receptor 10 (Inactive tyrosine-protein kinase EPHA10) Although this protein belongs to the kinase superfamily, it lacks key residues required for catalytic activity, suggesting that it does not have kinase activity. Despite the predicted lack of kinase activity, can bind ATP. {ECO:0000250|UniProtKB:Q5JZY3}. degenerate-domain O08644 Ephb6 Mus musculus (Mouse) 10090 Ephrin type-B receptor 6 (MEP) (Tyrosine-protein kinase-defective receptor EPH-6) Although this protein belongs to the kinase superfamily, it lacks key residues required for catalytic activity, suggesting that it does not have kinase activity. In addition, lacks kinase activity in vitro (PubMed:8761299). Despite the lack of kinase activity, can bind ATP (By similarity). {ECO:0000250|UniProtKB:O15197, ECO:0000269|PubMed:8761299, ECO:0000305|PubMed:8761299}. degenerate-domain Q9D4M9 Galntl5 Mus musculus (Mouse) 10090 Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5 (Polypeptide GalNAc transferase 15) (GalNAc-T15) (pp-GaNTase 15) (Protein-UDP acetylgalactosaminyltransferase 15) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 15) In contrast to other members of the family, lacks the C-terminal ricin B-type lectin domain that contributes to the glycopeptide specificity, and lacks the conserved His residue in position 341. No glycosyltransferase activity has been detected in an in vitro assay (PubMed:24398516). {ECO:0000305|PubMed:24398516}. degenerate-domain Q9WV56 Gdf2 Mus musculus (Mouse) 10090 Growth/differentiation factor 2 (GDF-2) (Bone morphogenetic protein 9) (BMP-9) Can promote osteogenic differentiation in vitro (PubMed:25751889). This is probably not physiologically relevant. {ECO:0000269|PubMed:25751889, ECO:0000305}. degenerate-domain Q8BTX9 Hsdl1 Mus musculus (Mouse) 10090 Inactive hydroxysteroid dehydrogenase-like protein 1 Although it belongs to the SDR family, Phe-218 is present instead of the conserved Tyr which is an active site residue. It is therefore expected that this protein lacks oxidoreductase activity. {ECO:0000305}. degenerate-domain Q62315 Jarid2 Mus musculus (Mouse) 10090 Protein Jumonji (Jumonji/ARID domain-containing protein 2) Despite the presence of a JmjC domain, lacks the conserved residues that bind the iron cofactor, explaining the absence of histone methyltransferase activity. {ECO:0000305}. degenerate-domain Q3UG20 Kmt2e Mus musculus (Mouse) 10090 Histone reader KMT2E (Inactive histone-lysine N-methyltransferase 2E) (Inactive lysine N-methyltransferase 2E) (Myeloid/lymphoid or mixed-lineage leukemia protein 5 homolog) Does not exhibit histone methyltransferase towards histone H3 in vitro (PubMed:18952892). The isolated catalytic SET domain lacks binding activity towards cofactor S-adenosyl-L-methionine; instead of the highly conserved XGXG, Y and NH motifs, KMT2E displays NKKI (Asn-339-Ile-342), F (Phe-381) and RR (Arg-408-Arg-409) motifs. Also lacks binding activity towards histone H3 due to a poor conservation of the key residues involved in the binding and the presence of large loop which prevents the docking of the H3 'Lys-4' side chain. {ECO:0000250|UniProtKB:Q8IZD2, ECO:0000269|PubMed:18952892}. degenerate-domain Q61097 Ksr1 Mus musculus (Mouse) 10090 Kinase suppressor of Ras 1 (mKSR1) (EC 2.7.11.1) (Protein Hb) Although it belongs to the protein kinase superfamily, the ATP-binding motif VAIK has an arginine instead of a lysine residue suggesting that KSR1 cannot bind ATP and therefore lacks protein kinase activity. However, KSR1 is capable of binding ATP (PubMed:21441104). Has protein kinase activity towards MAP2K1 in presence of RAF1/c-RAF in vitro (PubMed:21441104). {ECO:0000269|PubMed:21441104, ECO:0000305}. degenerate-domain Q8K1F9 Lctl Mus musculus (Mouse) 10090 Lactase-like protein (Klotho/lactase-phlorizin hydrolase-related protein) Although it belongs to the glycosyl hydrolase 1 family, Asp-200 is present instead of the conserved Glu which is an active site residue. It is therefore expected that this protein lacks glycosidase activity. {ECO:0000305}. degenerate-domain Q8BVA5 Ldah Mus musculus (Mouse) 10090 Lipid droplet-associated hydrolase (EC 3.1.1.13) (Lipid droplet-associated serine hydrolase) (mLDAH) The catalytic activity is unsure despite catalytic sites being conserved (PubMed:23525007, PubMed:27836991). One report shows that LDAH has low cholesterol esterase activity when overexpressed in RAW 264.7 macrophages or in HeLa cells (PubMed:24357060). However, in another study, LDAH lacks cholesterol esterase activity when overexpressed in Hela cells (PubMed:27836991). LDAH is not the only cellular cholesterol esterase and its activity may be too low to detect under certain experimental conditions. Lacks lipolytic activity towards trioleoylglycerol, dioleoylglycerol or monooleoylglycerol when overexpressed in COS-7 cells or Hela cells (PubMed:23525007, PubMed:27836991). {ECO:0000269|PubMed:23525007, ECO:0000269|PubMed:24357060, ECO:0000269|PubMed:27836991, ECO:0000305}. degenerate-domain Q9D925 Lyzl4 Mus musculus (Mouse) 10090 Lysozyme-like protein 4 (Lysozyme-4) Although it belongs to the glycosyl hydrolase 22 family, Gly-72 is present instead of the conserved Asp which is an active site residue. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain Q9CY73 Mrpl44 Mus musculus (Mouse) 10090 Large ribosomal subunit protein mL44 (39S ribosomal protein L44, mitochondrial) (L44mt) (MRP-L44) Lacks RNase activity due to the absence of RNase-specific catalytic domain. {ECO:0000305|PubMed:26221731}. degenerate-domain Q7TPM9 Mtmr10 Mus musculus (Mouse) 10090 Myotubularin-related protein 10 (Inactive phosphatidylinositol 3-phosphatase 10) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 399 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q3V1L6 Mtmr11 Mus musculus (Mouse) 10090 Myotubularin-related protein 11 (Inactive phosphatidylinositol 3-phosphatase 11) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 380 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q80TA6 Mtmr12 Mus musculus (Mouse) 10090 Myotubularin-related protein 12 (Inactive phosphatidylinositol 3-phosphatase 12) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 391 in the dsPTPase catalytic loop and does not have phosphatase activity. {ECO:0000250|UniProtKB:Q9C0I1}. degenerate-domain Q9Z2D0 Mtmr9 Mus musculus (Mouse) 10090 Myotubularin-related protein 9 (Inactive phosphatidylinositol 3-phosphatase 9) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 333 in the dsPTPase catalytic loop, suggesting that it has no carboxypeptidase activity. {ECO:0000305}. degenerate-domain Q8K2T1 Nmral1 Mus musculus (Mouse) 10090 NmrA-like family domain-containing protein 1 Lacks the conserved Tyr residue in the active site triad of Ser-Tyr-Lys necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity. {ECO:0000305}. degenerate-domain Q14AW5 Nsun7 Mus musculus (Mouse) 10090 Protein NSUN7 (NOL1/NOP2/Sun domain family member 7) In contrast to other NSUN family members, NSUN7 lacks RNA cytosine C5-methyltransferase activity, due to sequence variations in S-adenosyl-L-methionine(SAM)-binding residues. Substitution of the conserved SAM-binding Asp-378 with Leu-378 abolishes SAM binding and likely renders the enzyme catalytically inactive. {ECO:0000269|PubMed:41381527}. degenerate-domain Q8VHN8 Nudt16l1 Mus musculus (Mouse) 10090 Tudor-interacting repair regulator protein (NUDT16-like protein 1) (Protein syndesmos) Although strongly related to the nudix NUDT16 protein, lacks the Nudix box and is therefore not related to the rest of the family. Lacks a number of residues which are necessary for hydrolase activity and does not play a role in U8 snoRNA decapping activity. {ECO:0000305}. degenerate-domain Q9CQF3 Nudt21 Mus musculus (Mouse) 10090 Cleavage and polyadenylation specificity factor subunit 5 (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Nudix hydrolase 21) Lacks the conserved metal-binding residues in the NUDIX motif and is not expected to have hydrolase activity. {ECO:0000305}. degenerate-domain Q3TVP5 Otulinl Mus musculus (Mouse) 10090 Inactive ubiquitin thioesterase OTULINL Although highly similar to the deubiquitinase OTULIN, lacks the conserved active site Cys at position 136 which is replaced by an Asp residue, and does not show deubiquitinase activity. {ECO:0000250|UniProtKB:Q9NUU6}. degenerate-domain P50580 Pa2g4 Mus musculus (Mouse) 10090 Proliferation-associated protein 2G4 (IRES-specific cellular trans-acting factor 45 kDa) (ITAF45) (Mpp1) (Proliferation-associated protein 1) (Protein p38-2G4) Although it belongs to the peptidase M24 family, it does not contain metal cofactors and lacks aminopeptidase activity. {ECO:0000305|PubMed:17690690}. degenerate-domain Q8BU25 Pamr1 Mus musculus (Mouse) 10090 Inactive serine protease PAMR1 (Peptidase domain-containing protein associated with muscle regeneration 1) (Regeneration-associated muscle protease homolog) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 665 which is replaced by a Thr, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain Q80YV4 Pank4 Mus musculus (Mouse) 10090 4'-phosphopantetheine phosphatase (EC 3.1.3.-) (Inactive pantothenic acid kinase 4) (mPanK4) Despite belonging to the type II pantothenate kinase family, the pantothenate kinase domain contains a Val residue at position 147 and a Trp residue at position 211 instead of the two conserved active site residues, Glu and Arg. Lacks pantothenate kinase activity. {ECO:0000250|UniProtKB:Q9NVE7}. degenerate-domain Q3USB7 Plcl1 Mus musculus (Mouse) 10090 Inactive phospholipase C-like protein 1 (PLC-L1) (Phospholipase C-related but catalytically inactive protein) (PRIP) In the PI-PLC X-box Asn-459 is present instead of the conserved His which is one of the active site residues. It is therefore expected that this protein lacks catalytic activity. {ECO:0000305}. degenerate-domain Q8K394 Plcl2 Mus musculus (Mouse) 10090 Inactive phospholipase C-like protein 2 (PLC-L(2)) (PLC-L2) (Phospholipase C-L2) (Phospholipase C-epsilon-2) (PLC-epsilon-2) In the PI-PLC X-box Thr-487 is present instead of the conserved His which is one of the active site residues. It is therefore expected that this protein lacks catalytic activity. {ECO:0000305}. degenerate-domain Q3UNN8 Pld5 Mus musculus (Mouse) 10090 Inactive phospholipase D5 (Inactive PLD 5) (Inactive choline phosphatase 5) (Inactive phosphatidylcholine-hydrolyzing phospholipase D5) In contrast to other members of the family, it lacks the conserved active sites, suggesting that it has no phospholipase activity. {ECO:0000305}. degenerate-domain Q8BVT6 Pp2d1 Mus musculus (Mouse) 10090 Protein phosphatase 2C-like domain-containing protein 1 Although it belongs to the protein phosphatase 2C family, it lacks some of the conserved residues that bind manganese, suggesting it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q8C0F9 Prss35 Mus musculus (Mouse) 10090 Inactive serine protease 35 Although related to peptidase S1 family, lacks the conserved active Ser residue in position 342 which is replaced by a Thr, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain Q9DAA4 Prss37 Mus musculus (Mouse) 10090 Probable inactive serine protease 37 (Probable inactive trypsin-X2) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 192 which is replaced by an Ala, suggesting that it has no protease activity. Also lacks metal binding sites Glu in position 67 which is replaced by Asn, and Asn in position 69 which is replaced by Lys. {ECO:0000305}. degenerate-domain O70169 Prss39 Mus musculus (Mouse) 10090 Inactive serine protease 39 (Inactive testicular serine protease 1) In contrast to other members of the family, lacks the conserved Asp at position 158, which is replaced by an Asn residue, suggesting it is inactive. {ECO:0000305}. degenerate-domain Q8K4I7 Prss45 Mus musculus (Mouse) 10090 Inactive serine protease 45 (Inactive testis serine protease 5) (Trypsin-like protease p98) In contrast to other members of the family, lacks the conserved Ser at position 243 which is replaced by a Pro residue, suggesting it is inactive. {ECO:0000305}. degenerate-domain Q8BLH5 Prss50 Mus musculus (Mouse) 10090 Probable threonine protease PRSS50 (EC 3.4.25.-) (Serine protease 50) (Testis-specific protease-like protein 50) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 364 which is replaced by a Thr. {ECO:0000305}. degenerate-domain Q7M756 Prss54 Mus musculus (Mouse) 10090 Inactive serine protease 54 (Plasma kallikrein-like protein 4) Although related to peptidase S1 family, lacks the essential His, Asp, and Ser residues of the catalytic triad at positions 73, 119 and 210 and is therefore predicted to have lost protease activity. {ECO:0000305}. degenerate-domain Q66GT5 Ptpmt1 Mus musculus (Mouse) 10090 Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (EC 3.1.3.27) (PTEN-like phosphatase) (Phosphoinositide lipid phosphatase) (Protein-tyrosine phosphatase mitochondrial 1) (EC 3.1.3.16, EC 3.1.3.48) Was originally (PubMed:15247229) thought to have phosphatidylinositol 5-phosphatase activity, however, it was later shown (PubMed:16039589) that it is probably not the case in vivo. {ECO:0000305|PubMed:15247229, ECO:0000305|PubMed:16039589}. degenerate-domain Q6IMB1 Rasl11a Mus musculus (Mouse) 10090 Ras-like protein family member 11A (EC 3.6.5.2) Although highly related to the Ras family, lacks the conserved prenylation motif at the C-terminus, which serves to target Ras proteins to membrane compartments. {ECO:0000305}. degenerate-domain Q8VEK2 Rhbdd2 Mus musculus (Mouse) 10090 Rhomboid domain-containing protein 2 (Rhomboid-like protein 7) Although strongly related to the peptidase S54 family, it lacks the conserved active sites, suggesting that it has no peptidase activity. {ECO:0000305}. degenerate-domain Q80WQ6 Rhbdf2 Mus musculus (Mouse) 10090 Inactive rhomboid protein 2 (iRhom2) (Rhomboid family member 2) (Rhomboid veinlet-like protein 6) (Rhomboid-related protein) Lacks serine protease activity as it lacks the catalytic Ser residue at position 692. {ECO:0000269|PubMed:21439629}. degenerate-domain Q5GAM9 Rnase11 Mus musculus (Mouse) 10090 Putative inactive ribonuclease 11 (RNase 11) In contrast to other members of the family, lacks the conserved His active site in position 75, suggesting it is inactive. {ECO:0000305}. degenerate-domain Q925F3 Rnf144a Mus musculus (Mouse) 10090 E3 ubiquitin-protein ligase RNF144A (EC 2.3.2.31) (RING finger protein 144A) (UbcM4-interacting protein 4) (Ubiquitin-conjugating enzyme 7-interacting protein 4) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q8BKD6 Rnf144b Mus musculus (Mouse) 10090 E3 ubiquitin-protein ligase RNF144B (EC 2.3.2.31) (IBR domain-containing protein 2) (RING finger protein 144B) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q01887 Ryk Mus musculus (Mouse) 10090 Inactive tyrosine-protein kinase RYK (Kinase VIK) (Met-related kinase) (NYK-R) Although this protein belongs to the kinase superfamily, it lacks key residues required for catalytic activity, suggesting that it does not have kinase activity. No kinase activity has been detected in kinase assays using the cytoplasmic domain of the protein (PubMed:1334548). Does not bind ATP (By similarity). {ECO:0000250|UniProtKB:P34925, ECO:0000269|PubMed:1334548, ECO:0000305|PubMed:11135307}. degenerate-domain Q6ZPE2 Sbf1 Mus musculus (Mouse) 10090 Myotubularin-related protein 5 (Inactive phosphatidylinositol 3-phosphatase 5) (SET-binding factor 1) (Sbf1) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 1422 in the dsPTPase catalytic loop and does not have phosphatase activity (By similarity). The pocket is however sufficiently preserved to bind phosphorylated substrates, and maybe protect them from phosphatases. {ECO:0000250|UniProtKB:O95248, ECO:0000305}. degenerate-domain E9PXF8 Sbf2 Mus musculus (Mouse) 10090 Myotubularin-related protein 13 (Inactive phosphatidylinositol 3-phosphatase 13) (SET-binding factor 2) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 1433 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}.; degenerate-domain Q9JHI9 Slc40a1 Mus musculus (Mouse) 10090 Ferroportin (Ferroportin-1) (Iron-regulated transporter 1) (Metal transporter protein 1) (MTP1) (Solute carrier family 40 member 1) Manganese (Mn) transport by SLC40A1 remains controversial. Some in vitro studies have suggested that SLC40A1 transports minimal amounts of Mn(2+) (By similarity). Other groups have suggested that it does not (By similarity). The predicted apparent affinity of SLC40A1 for manganese is extremely low compared with iron, implying that any SLC40A1-mediated Mn transport in vivo would likely be trivial (By similarity). A recent study examined the role of SLC40A1 in Mn homeostasis by using Tmprss6-O mice, which express high levels of hepcidin/HAMP and therefore have very low SLC40A1 levels in their tissues. These mice show frank iron deficiency and reduced iron levels in most tissues, but manganese levels are largely unaffected (PubMed:30888356). These studies suggest that manganese is probably not the physiological substrate of SLC40A1. {ECO:0000250|UniProtKB:Q9NP59, ECO:0000269|PubMed:30888356, ECO:0000305}. degenerate-domain Q9D9X8 Spaca3 Mus musculus (Mouse) 10090 Sperm acrosome membrane-associated protein 3 (Lysozyme-like protein 3) (Sperm lysozyme-like protein 1) (mSLLP1) [Cleaved into: Sperm acrosome membrane-associated protein 3, membrane form; Sperm acrosome membrane-associated protein 3, processed form] Although it belongs to the glycosyl hydrolase 22 family, Thr-128 and Asn-145 are present instead of the conserved Glu and Asp which are active site residues. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain Q8R0F3 Sumf1 Mus musculus (Mouse) 10090 Formylglycine-generating enzyme (FGE) (EC 1.8.3.7) (C-alpha-formylglycine-generating enzyme 1) (Sulfatase-modifying factor 1) The enzyme reaction was initially thought to act via a redox-active disulfide bond mechanism; however the disulfide bond only takes place with inactive enzyme that lacks the copper cofactor. The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation. {ECO:0000250|UniProtKB:Q8NBK3}. degenerate-domain Q8BPG6 Sumf2 Mus musculus (Mouse) 10090 Inactive C-alpha-formylglycine-generating enzyme 2 (Sulfatase-modifying factor 2) Although strongly similar to formylglycine-generating enzyme, lacks the catalytic Cys residues that bind the catalytic copper. The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation. {ECO:0000305}. degenerate-domain Q920B9 Supt16h Mus musculus (Mouse) 10090 FACT complex subunit SPT16 (Chromatin-specific transcription elongation factor 140 kDa subunit) (FACT 140 kDa subunit) (FACTp140) (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q8CF89 Tab1 Mus musculus (Mouse) 10090 TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 1) (TGF-beta-activated kinase 1-binding protein 1) (TAK1-binding protein 1) Lacks several key residues involved in metal-binding and catalytic activity, therefore has lost phosphatase activity. {ECO:0000250|UniProtKB:Q15750}. degenerate-domain O08710 Tg Mus musculus (Mouse) 10090 Thyroglobulin (Tg) The cholinesterase-like (ChEL) region lacks the Ser residue of the catalytic triad suggesting that it has no esterase activity. {ECO:0000305}. degenerate-domain Q9EPQ1 Tlr1 Mus musculus (Mouse) 10090 Toll-like receptor 1 (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q6R5N8 Tlr13 Mus musculus (Mouse) 10090 Toll-like receptor 13 In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9QUN7 Tlr2 Mus musculus (Mouse) 10090 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9QUK6 Tlr4 Mus musculus (Mouse) 10090 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9EPW9 Tlr6 Mus musculus (Mouse) 10090 Toll-like receptor 6 (CD antigen CD286) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q3UDE2 Ttll12 Mus musculus (Mouse) 10090 Tubulin--tyrosine ligase-like protein 12 (Inactive tubulin--tyrosine ligase-like protein 12) Although it belongs to the tubulin--tyrosine ligase family, the TTL domain lacks some of the ATP binding sites predicted to be essential for TTL activity (By similarity). Lacks tyrosine ligase activity in vitro (By similarity). Lacks glutamylation activity in vitro (PubMed:17499049). Although TTLL12 contains a potential SET-like domain in the N-terminus, it does not have lysine methyltransferase activity towards histone in vitro (By similarity). {ECO:0000250|UniProtKB:Q14166, ECO:0000269|PubMed:17499049}. degenerate-domain Q8CEG8 Usp27x Mus musculus (Mouse) 10090 Ubiquitin carboxyl-terminal hydrolase 27 (EC 3.4.19.12) (Deubiquitinating enzyme 27) (Ubiquitin thioesterase 27) (Ubiquitin-specific-processing protease 27) (X-linked ubiquitin carboxyl-terminal hydrolase 27) Although strongly related to USP22, which deubiquitinates histones, lacks the N-terminal UBP-type zinc finger, suggesting it does not have the ability to deubiquitinate histones. {ECO:0000305}. degenerate-domain Q3TIX9 Usp39 Mus musculus (Mouse) 10090 Ubiquitin carboxyl-terminal hydrolase 39 (EC 3.4.19.12) (U4/U6.U5 tri-snRNP-associated 65 kDa protein) Lacks the conserved His and Cys residues that are essential for the activity of de-ubiquitinating enzymes. Lacks ubiquitin C-terminal hydrolase activity. {ECO:0000250|UniProtKB:Q53GS9, ECO:0000305}. degenerate-domain Q67HT0 psbN Muscari comosum (Tassel grape hyacinth) (Leopoldia comosa) 81770 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P0A609 sodC Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) 233413 Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) Lacks two conserved histidine residues that bind copper and zinc. {ECO:0000305}. degenerate-domain Q9CBC6 Mycobacterium leprae (strain TN) 272631 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q9CBI6 sodC Mycobacterium leprae (strain TN) 272631 Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) Lacks three conserved histidine residues and one conserved aspartate residue that bind copper and zinc. {ECO:0000305}. degenerate-domain A5U5A1 rnz Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) 419947 Ribonuclease Z (RNase Z) (EC 3.1.26.11) (tRNA 3 endonuclease) (tRNase Z) Lacks two conserved zinc binding sites. {ECO:0000305}. degenerate-domain P9WQ67 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Uncharacterized protein Rv3778c Lacks the conserved Lysine residue that is involved in covalent pyridoxal phosphate binding in other members of the family. {ECO:0000305}. degenerate-domain P9WK89 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Probable inactive lipase Rv1592c Although related to the lipase family, lacks the conserved His active site at position 344 which is replaced by a Gln residue, suggesting it is inactive. {ECO:0000305}. degenerate-domain P9WGZ5 rnz Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Ribonuclease Z (RNase Z) (EC 3.1.26.11) (tRNA 3 endonuclease) (tRNase Z) Lacks two conserved zinc binding sites. {ECO:0000305}. degenerate-domain P9WGE9 sodC Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) Lacks two conserved histidine residues that bind copper and zinc. {ECO:0000305}. degenerate-domain P9WKC5 tgs3 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Probable diacyglycerol O-acyltransferase tgs3 (TGS3) (EC 2.3.1.20) (Probable triacylglycerol synthase tgs3) Lacks the conserved His residue in position 138 suggested to serve as a proton acceptor for this family, however this protein still has diacyglycerol O-acyltransferase activity in E.coli. {ECO:0000305}. degenerate-domain P9WK88 Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) 83331 Probable inactive lipase MT1628 Although related to the lipase family, lacks the conserved His active site at position 344 which is replaced by a Gln residue, suggesting it is inactive. {ECO:0000305}. degenerate-domain P9WQ66 Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) 83331 Uncharacterized protein MT3887 Lacks the conserved Lysine residue that is involved in covalent pyridoxal phosphate binding in other members of the family. {ECO:0000305}. degenerate-domain P9WGE8 sodC Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) 83331 Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) Lacks two conserved histidine residues that bind copper and zinc. {ECO:0000305}. degenerate-domain P9WKC4 tgs3 Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) 83331 Probable diacyglycerol O-acyltransferase tgs3 (TGS3) (EC 2.3.1.20) (Probable triacylglycerol synthase tgs3) Lacks the conserved His residue in position 138 suggested to serve as a proton acceptor for this family. {ECO:0000305}. degenerate-domain A0PTY0 rnz Mycobacterium ulcerans (strain Agy99) 362242 Ribonuclease Z (RNase Z) (EC 3.1.26.11) (tRNA 3 endonuclease) (tRNase Z) Lacks one conserved zinc binding site. {ECO:0000305}. degenerate-domain Q9AGW2 sodC Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) (Mycobacterium paratuberculosis) 262316 Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) Lacks three conserved histidine residues that bind copper and zinc. {ECO:0000305}. degenerate-domain A1T2N5 Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii) 350058 Probable inactive acetaldehyde dehydrogenase 1 (Acetaldehyde dehydrogenase [acetylating] 1) In contrast to other members of the family, lacks the conserved Cys active site in position 129, suggesting it is inactive. {ECO:0000305}. degenerate-domain P75433 Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasma pneumoniae) 272634 Putative type I restriction enzyme MpnIIP endonuclease subunit C-terminal part (R protein C-terminal part) (Putative type-1 restriction enzyme MpnORFDP R protein part 3) (MpnORFDBP) Could be the product of a pseudogene; in this organism the endonuclease subunit carries 2 frameshift mutations (resulting in 3 short ORFs) and is probably not expressed. {ECO:0000305|PubMed:23300489, ECO:0000305|PubMed:8948633}. degenerate-domain P75431 Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasma pneumoniae) 272634 Putative type I restriction enzyme MpnIIP endonuclease subunit N-terminal part (R protein N-terminal part) (Putative type I restriction enzyme MpnORFDP endonuclease subunit part 1) (MpnORFDAP) Could be the product of a pseudogene; in this organism the endonuclease subunit carries 2 frameshift mutations (resulting in 3 short ORFs) and is probably not expressed. {ECO:0000305|PubMed:23300489, ECO:0000305|PubMed:8948633}. degenerate-domain P75432 Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasma pneumoniae) 272634 Putative type I restriction enzyme MpnIIP endonuclease subunit middle part (R protein middle part) Could be the product of a pseudogene; in this organism the endonuclease subunit carries 2 frameshift mutations (resulting in 3 short ORFs) and is probably not expressed. {ECO:0000305|PubMed:23300489, ECO:0000305|PubMed:8948633}. degenerate-domain Q4P2U5 SPT16 Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis) 5270 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q09FT3 psbN Nandina domestica (Heavenly bamboo) 41776 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q74NK2 Nanoarchaeum equitans (strain Kin4-M) 228908 Bifunctional methyltransferase-like/endonuclease [Includes: Probable methylated-DNA--protein-cysteine methyltransferase-like; Endonuclease V (EC 3.1.21.7) (Deoxyinosine 3'endonuclease) (Deoxyribonuclease V) (DNase V)] Lacks the potential active site region of the MGMT family and therefore has probably lost the methyltransferase activity. {ECO:0000305}. degenerate-domain A4QLW1 psbN Nasturtium officinale (Watercress) (Rorippa nasturtium-aquaticum) 65948 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6EYH4 psbN Nelumbo lutea (American lotus) (Nelumbo nucifera subsp. lutea) 4431 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A7RRG3 Nematostella vectensis (Starlet sea anemone) 45351 Protein AKTIP homolog (Fused toes protein homolog) Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q9TKW6 psbN Nephroselmis olivacea (Green alga) 31312 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8X0X6 ctc-2 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) 367110 FACT complex subunit ctc-2 (Chromatin transcription complex 2) (Facilitates chromatin transcription complex subunit ctc-2) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain P23955 mpp Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) 367110 Mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (Inactive zinc metalloprotease alpha) (Matrix processing peptidase) Was originally thought to be the catalytic subunit (PubMed:2967109). The low processing activity which was previously observed with alpha-MPP which has been immunoprecipitated from a mitochondrial extract is most likely due to contamination by the beta-subunit (PubMed:8106471). Does not seem to have protease activity as it lacks the zinc-binding site. {ECO:0000305, ECO:0000305|PubMed:2967109, ECO:0000305|PubMed:8106471}. degenerate-domain P23762 nmr Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) 367110 Nitrogen metabolite repression protein nmr (Negative-acting nitrogen regulatory protein nmr) (Nitrogen metabolite regulation protein) (NMR) Lacks the conserved Tyr residue in position 211 in the active site triad of Ser-Tyr-Lys necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity. {ECO:0000305}. degenerate-domain Q7SI01 un-7 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) 367110 Protein png-1 Although strongly related to the peptide:N-glycanase enzyme, it lacks the conserved active site Cys in position 208, which is replaced by a Ala residue suggesting that it has no activity. {ECO:0000305}. degenerate-domain Q3C1K1 psbN Nicotiana sylvestris (Wood tobacco) (South American tobacco) 4096 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P62114 pbf1 Nicotiana tabacum (Common tobacco) 4097 Photosystem biogenesis factor 1 (Protein PsbN) Originally thought to be a component of PSII; based on experiments in this organism, Synechocystis and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293, ECO:0000269|PubMed:23738654}. degenerate-domain Q33C04 psbN Nicotiana tomentosiformis (Tobacco) 4098 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q82SY2 lpxK Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298) 228410 Tetraacyldisaccharide 4'-kinase (EC 2.7.1.130) (Lipid A 4'-kinase) Lacks the conserved motif Gly-Gly-x-Gly-Lys-Thr that is the consensus ATP-binding site for this enzyme. {ECO:0000305}. degenerate-domain Q0AEA0 lpxK Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57) 335283 Tetraacyldisaccharide 4'-kinase (EC 2.7.1.130) (Lipid A 4'-kinase) Lacks the conserved motif Gly-Gly-x-Gly-Lys-Thr that is the consensus ATP-binding site for this enzyme. {ECO:0000305}. degenerate-domain Q5Z2A5 Nocardia farcinica (strain IFM 10152) 247156 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q80J95 Norovirus (isolate Mouse/NoV/United States/MNV1/2002/GV) (MNV-1) (Murine Norovirus 1) 223997 Genome polyprotein [Cleaved into: NS1-2 (NS1.2) (NS1/2) (Protein p37); NS1; NS2; NTPase (EC 3.6.1.15) (NS3) (p41); NS4 (Protein p20); Viral genome-linked protein (VPg) (NS5); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (NS6); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (NS7)] Lacks conserved residue(s) required for the propagation of feature annotation. {ECO:0000255|PROSITE-ProRule:PRU00870}. degenerate-domain B2JA12 psbN Nostoc punctiforme (strain ATCC 29133 / PCC 73102) 63737 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8YM40 Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) 103690 Alpha-2-macroglobulin homolog Lacks the conserved thioester bond that is characteristic of the alpha-2-macroglobulins. {ECO:0000305}. degenerate-domain Q8YYK1 psbN Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) 103690 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6EW24 psbN Nymphaea alba (White water-lily) (Castalia alba) 34301 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7IW41 psbN Nymphaea odorata (White water lily) 4419 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B2X1X9 psbN Oedogonium cardiacum (Filamentous green alga) 55995 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P68858 psbN Oenothera argillicola (Appalachian evening primrose) 3940 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B0Z4Y8 psbN Oenothera biennis (German evening primrose) (Onagra biennis) 3942 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P68857 psbN Oenothera elata subsp. hookeri (Hooker's evening primrose) (Oenothera hookeri) 85636 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B0Z572 psbN Oenothera glazioviana (Large-flowered evening primrose) (Oenothera erythrosepala) 482428 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B0Z5F6 psbN Oenothera parviflora (Small-flowered evening primrose) (Oenothera cruciata) 482429 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A4QJV9 psbN Olimarabidopsis pumila (Dwarf rocket) (Arabidopsis griffithiana) 74718 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q20F18 psbN Oltmannsiellopsis viridis (Marine flagellate) (Oltmannsiella viridis) 51324 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6YPX7 pheT Onion yellows phytoplasma (strain OY-M) 262768 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved glutamate residue in position 500 that binds magnesium; it is replaced by a serine residue. {ECO:0000305}. degenerate-domain Q6ENE6 psbN Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea) 4536 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P0C418 psbN Oryza sativa (Rice) 4530 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A2Y4R8 Oryza sativa subsp. indica (Rice) 39946 PHD finger protein ALFIN-LIKE 5 Lacks the Tyr (here Asp-212), a conserved feature of the aromatic cage required for the interaction with histone H3K4me3/2. {ECO:0000305}. degenerate-domain A2WXR5 Oryza sativa subsp. indica (Rice) 39946 PHD finger protein ALFIN-LIKE 6 Lacks the Tyr (here Asp-226), a conserved feature of the aromatic cage required for the interaction with histone H3K4me3/2. {ECO:0000305}. degenerate-domain Q9SAY3 Cht7 Oryza sativa subsp. indica (Rice) 39946 Chitinase 7 (EC 3.2.1.14) (Class I chitinase d) (OsChia1d) (Pathogenesis related (PR)-3 chitinase 7) Enzyme activity is uncertain. Was shown to have endochitinase activity (in vitro) (PubMed:10890535). Lacks the conserved Glu residue that is essential for catalytic activity, suggesting it lacks enzyme activity. {ECO:0000269|PubMed:10890535, ECO:0000305}. degenerate-domain Q01JR9 MRS2-D Oryza sativa subsp. indica (Rice) 39946 Putative magnesium transporter MRS2-D Lacks the GMN motif, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain A2Z9W7 MRS2-G Oryza sativa subsp. indica (Rice) 39946 Putative magnesium transporter MRS2-G Lacks the GMN motif, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain A2XCA0 MRS2-H Oryza sativa subsp. indica (Rice) 39946 Putative magnesium transporter MRS2-H Lacks the GMN motif, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain B8B7E7 PLP3 Oryza sativa subsp. indica (Rice) 39946 Patatin-like protein 3 (EC 3.1.1.-) Lacks the conserved Asp residue expected to act as the active site proton acceptor. {ECO:0000305}. degenerate-domain A2YQ93 PRR37 Oryza sativa subsp. indica (Rice) 39946 Two-component response regulator-like PRR37 (Pseudo-response regulator 37) (OsPRR37) Lacks the phospho-accepting Asp (here Glu-114), present in the receiver domain, which is one of the conserved features of two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain A2XFB7 PRR73 Oryza sativa subsp. indica (Rice) 39946 Two-component response regulator-like PRR73 (Pseudo-response regulator 73) (OsPRR73) Lacks the phospho-accepting Asp (here Glu-133), present in the receiver domain, which is one of the conserved features of two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain P0C419 psbN Oryza sativa subsp. indica (Rice) 39946 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q60DW3 Oryza sativa subsp. japonica (Rice) 39947 PHD finger protein ALFIN-LIKE 5 Lacks the Tyr (here Asp-212), a conserved feature of the aromatic cage required for the interaction with histone H3K4me3/2. {ECO:0000305}. degenerate-domain Q7F2Z1 Oryza sativa subsp. japonica (Rice) 39947 PHD finger protein ALFIN-LIKE 6 Lacks the Tyr (here Asp-226), a conserved feature of the aromatic cage required for the interaction with histone H3K4me3/2. {ECO:0000305}. degenerate-domain Q7XR62 Oryza sativa subsp. japonica (Rice) 39947 Probable inactive carboxylesterase Os04g0669700 Lacks the Asp residue of the conserved catalytic triad Ser-Asp-His. {ECO:0000305}. degenerate-domain Q7XXD4 Oryza sativa subsp. japonica (Rice) 39947 Probable inactive methyltransferase Os04g0175900 (EC 2.1.1.-) Lacks the typical His active site around position 277, suggesting it has no methyltransferase activity. {ECO:0000305}. degenerate-domain Q0J9V5 Oryza sativa subsp. japonica (Rice) 39947 Thioredoxin-like protein CXXS1 (OsCXXS1) (OsTrx15) Lacks the conserved cysteine (here Ser-49), present in the redox-active center, which is one of the conserved features of the thioredoxin family. {ECO:0000305}. degenerate-domain Q6H7J4 Oryza sativa subsp. japonica (Rice) 39947 Putative protein phosphatase 2C 23 (OsPP2C23) (EC 3.1.3.16) Although related to the protein phosphatase 2C family, lacks 1 of the conserved residues that bind manganese, suggesting it has no phosphatase activity. {ECO:0000305}.; degenerate-domain Q0D629 Oryza sativa subsp. japonica (Rice) 39947 Putative protein phosphatase 2C 63 (OsPP2C63) (EC 3.1.3.16) Although related to the protein phosphatase 2C family, lacks the conserved residues that bind manganese, suggesting it has no phosphatase activity. {ECO:0000305}.; degenerate-domain Q10CV4 AMT4-1 Oryza sativa subsp. japonica (Rice) 39947 Putative ammonium transporter 4 member 1 (OsAMT4;1) This protein lacks transmembrane domains and is probably not involved in transport. {ECO:0000305}. degenerate-domain Q7XPY7 BGLU14 Oryza sativa subsp. japonica (Rice) 39947 Probable inactive beta-glucosidase 14 (Os4bglu14) Lacks the conserved Glu residue acting as catalytic proton donor. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q0J0G1 BGLU33 Oryza sativa subsp. japonica (Rice) 39947 Probable inactive beta-glucosidase 33 (Os9bglu33) Lacks the conserved Glu residue acting as catalytic proton donor. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q5Z5C9 BURP11 Oryza sativa subsp. japonica (Rice) 39947 BURP domain-containing protein 11 (OsBURP11) Lacks the conserved signal peptide, which is one of the features of the BURP domain-containing proteins. {ECO:0000305}. degenerate-domain Q69XK5 CESA11 Oryza sativa subsp. japonica (Rice) 39947 Putative cellulose synthase A catalytic subunit 11 [UDP-forming] (EC 2.4.1.12) (OsCesA11) Lacks the conserved zinc finger domain, which is one of the features of the CESA family. {ECO:0000305}.; degenerate-domain C7J3A2 CYP701A7 Oryza sativa subsp. japonica (Rice) 39947 Ent-kaurene oxidase-like protein 1 (OsKOL1) (Cytochrome P450 701A7) Could be the product of a pseudogene. In contrast to other members of the family, it is shorter at the C-terminus and lacks the heme-binding sites. {ECO:0000305}. degenerate-domain Q5NB11 Cht10 Oryza sativa subsp. japonica (Rice) 39947 Chitinase 10 (EC 3.2.1.14) (Pathogenesis related (PR)-3 chitinase 10) Lacks the chitin binding type-1 domain which is one of the conserved features of the chitinase class I and class IV subfamilies. {ECO:0000305}. degenerate-domain Q10S66 Cht11 Oryza sativa subsp. japonica (Rice) 39947 Chitinase 11 (EC 3.2.1.14) (Pathogenesis related (PR)-3 chitinase 11) Lacks the chitin binding type-1 domain which is one of the conserved features of the chitinase class I and class IV subfamilies. {ECO:0000305}. degenerate-domain Q7Y1Z1 Cht7 Oryza sativa subsp. japonica (Rice) 39947 Chitinase 7 (EC 3.2.1.14) (Class I chitinase d) (OsChia1d) (Pathogenesis related (PR)-3 chitinase 7) Enzyme activity is uncertain. Was shown to have endochitinase activity (in vitro) (PubMed:10890535). Lacks the conserved Glu residue that is essential for catalytic activity, suggesting it lacks enzyme activity. {ECO:0000269|PubMed:10890535, ECO:0000305}. degenerate-domain Q7XCK6 Cht8 Oryza sativa subsp. japonica (Rice) 39947 Chitinase 8 (EC 3.2.1.14) (Class II chitinase a) (OsChia2a) (Pathogenesis related (PR)-3 chitinase 8) Lacks the chitin binding type-1 domain which is one of the conserved features of the chitinase class I and class IV subfamilies. {ECO:0000305}. degenerate-domain Q2QYR5 DRM1B Oryza sativa subsp. japonica (Rice) 39947 Probable inactive DNA (cytosine-5)-methyltransferase DRM1B (Protein DOMAINS REARRANGED METHYLASE 1B) Lacks the conserved tripeptide Ser-Pro-Cys in position 405 necessary for the methyltransferase activity in DRM protein (AC Q9M548). degenerate-domain Q6AUQ7 DRM3 Oryza sativa subsp. japonica (Rice) 39947 Probable inactive DNA (cytosine-5)-methyltransferase DRM3 (Protein DOMAINS REARRANGED METHYLASE 3) Lacks the conserved tripeptide Ser-Pro-Cys in position 625 necessary for the methyltransferase activity in DRM protein (AC Q9M548). degenerate-domain Q6Z6T2 FOS1 Oryza sativa subsp. japonica (Rice) 39947 Inactive protein FON2 SPARE1 (CLAVATA3/ESR (CLE)-related protein 202) (OsCLE202) Due to an amino acid substitution at the processing site, the putative signal sequence is probably not cleaved and the protein is inactive. {ECO:0000305}. degenerate-domain Q10K62 HO2 Oryza sativa subsp. japonica (Rice) 39947 Probable inactive heme oxygenase 2, chloroplastic Lacks the conserved His residue involved in heme iron binding and essential for heme oxygenase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q7XMJ2 KIN10B Oryza sativa subsp. japonica (Rice) 39947 Kinesin-like protein KIN-10B Lacks the ATP-binding motif which is one of the conserved features of the kinesin family. {ECO:0000305}. degenerate-domain Q6H647 KIN7B Oryza sativa subsp. japonica (Rice) 39947 Putative inactive kinesin-like protein KIN-7B Could be the product of a pseudogene. The kinesin motor domain is truncated at the N-terminus and lacks the ATP-binding site which is one of the conserved features of the KIN7 family. {ECO:0000305}. degenerate-domain Q0DHL5 LAC11 Oryza sativa subsp. japonica (Rice) 39947 Putative laccase-11 (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase 11) (Diphenol oxidase 11) (Urishiol oxidase 11) Lacks the signal peptide, which is one of the conserved features of the laccases. {ECO:0000305}.; degenerate-domain Q7XE50 LAC16 Oryza sativa subsp. japonica (Rice) 39947 Putative laccase-16 (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase 16) (Diphenol oxidase 16) (Urishiol oxidase 16) Lacks the signal peptide, which is one of the conserved features of the laccases. {ECO:0000305}.; degenerate-domain Q7XQQ1 MRS2-D Oryza sativa subsp. japonica (Rice) 39947 Putative magnesium transporter MRS2-D Lacks the GMN motif, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain A3BV82 MRS2-G Oryza sativa subsp. japonica (Rice) 39947 Putative magnesium transporter MRS2-G Lacks the GMN motif, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain Q10S25 MRS2-H Oryza sativa subsp. japonica (Rice) 39947 Putative magnesium transporter MRS2-H Lacks the GMN motif, which is a conserved feature of the family. {ECO:0000305}. degenerate-domain Q0JJE3 PHP1 Oryza sativa subsp. japonica (Rice) 39947 Pseudo histidine-containing phosphotransfer protein 1 (OsHpt1) Lacks the conserved active histidine at position 115 that mediates the phosphotransfer. Shows a conserved HPt domain that may have some alternative degenerated phosphorelay role in cell signaling. {ECO:0000305}. degenerate-domain Q0DK78 PHP2 Oryza sativa subsp. japonica (Rice) 39947 Pseudo histidine-containing phosphotransfer protein 2 (OsHpt4) Lacks the conserved active histidine at position 79 that mediates the phosphotransfer. Shows a conserved HPt domain that may have some alternative degenerated phosphorelay role in cell signaling. {ECO:0000305}. degenerate-domain Q6F303 PHP5 Oryza sativa subsp. japonica (Rice) 39947 Pseudo histidine-containing phosphotransfer protein 5 (OsHpt5) Lacks the conserved active histidine at position 79 that mediates the phosphotransfer. Shows a conserved HPt domain that may have some alternative degenerated phosphorelay role in cell signaling. {ECO:0000305}. degenerate-domain Q8H5D4 PLP3 Oryza sativa subsp. japonica (Rice) 39947 Patatin-like protein 3 (OsPLP3) (EC 3.1.1.-) Lacks the conserved Asp residue expected to act as the active site proton acceptor. {ECO:0000305}. degenerate-domain Q689G9 PRR1 Oryza sativa subsp. japonica (Rice) 39947 Two-component response regulator-like PRR1 (Pseudo-response regulator 1) (OsPRR1) Lacks the phospho-accepting Asp (here Glu-80), present in the receiver domain, which is one of the conserved features of the two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q0D3B6 PRR37 Oryza sativa subsp. japonica (Rice) 39947 Two-component response regulator-like PRR37 (Protein DAYS TO HEADING 7) (Protein HEADING DATE 2) (Pseudo-response regulator 37) (OsPRR37) Lacks the phospho-accepting Asp (here Glu-114), present in the receiver domain, which is one of the conserved features of two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q10N34 PRR73 Oryza sativa subsp. japonica (Rice) 39947 Two-component response regulator-like PRR73 (Pseudo-response regulator 73) (OsPRR73) Lacks the phospho-accepting Asp (here Glu-133), present in the receiver domain, which is one of the conserved features of two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q689G6 PRR95 Oryza sativa subsp. japonica (Rice) 39947 Two-component response regulator-like PRR95 (Pseudo-response regulator 95) (OsPRR95) Lacks the phospho-accepting Asp (here Glu-95), present in the receiver domain, which is one of the conserved features of two-component response regulators (ARRs) family. {ECO:0000305}. degenerate-domain Q7X923 SPT16 Oryza sativa subsp. japonica (Rice) 39947 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q2R4I5 UBP5 Oryza sativa subsp. japonica (Rice) 39947 Inactive ubiquitin-specific protease 5 (OsUBP5) (Protein FLOWER AND LEAF COLOR ABERRANT) Lacks the conserved Cys and His active sites that are essential for the activity of deubiquitinating enzymes. Lacks ubiquitin terminal hydrolase activity. {ECO:0000269|PubMed:30603810}. degenerate-domain P68853 psbN Oryza sativa subsp. japonica (Rice) 39947 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q0P3N3 psbN Ostreococcus tauri (Marine green alga) 70448 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q28755 Ovis aries (Sheep) 9940 Pregnancy-associated glycoprotein 1 (PAG 1) (Inactive aspartic protease PAG-1) (Pregnancy-associated glycoprotein 66d) (ovPAG 66d) Lacks the conserved Asp active site at position 272. {ECO:0000305|PubMed:1946444}. degenerate-domain Q6TMG6 CHI3L1 Ovis aries (Sheep) 9940 Chitinase-3-like protein 1 (Secretory glycoprotein of 40 kDa) (Signal-processing protein) Although it belongs to the glycosyl hydrolase 18 family, Leu-119 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity. {ECO:0000305}. degenerate-domain B2LT65 TLR2 Ovis aries (Sheep) 9940 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain A0A443HK52 VdtD Paecilomyces variotii (Byssochlamys spectabilis) 264951 Inactive carboxylesterase-like protein VdtD (Viriditoxin biosynthesis cluster protein D) Lacks the conserved active serine at position 228 and does not have carboxylesterase activity. {ECO:0000305|PubMed:31304040}. degenerate-domain B3Y614 TLR2 Pan paniscus (Pygmy chimpanzee) (Bonobo) 9597 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q9TTN0 TLR4 Pan paniscus (Pygmy chimpanzee) (Bonobo) 9597 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain P0C0K6 EPHB6 Pan troglodytes (Chimpanzee) 9598 Ephrin type-B receptor 6 (Tyrosine-protein kinase-defective receptor EPH-6) Although this protein belongs to the kinase superfamily, it lacks key residues required for catalytic activity, suggesting that it does not have kinase activity. In addition, lacks kinase activity in vitro. Despite the lack of kinase activity, can bind ATP. {ECO:0000250|UniProtKB:O15197}. degenerate-domain B6VH76 SPACA3 Pan troglodytes (Chimpanzee) 9598 Sperm acrosome membrane-associated protein 3 (Sperm protein reactive with antisperm antibodies) (Sperm protein reactive with ASA) [Cleaved into: Sperm acrosome membrane-associated protein 3, membrane form; Sperm acrosome membrane-associated protein 3, processed form] Although it belongs to the glycosyl hydrolase 22 family, Thr-122 and Asn-139 are present instead of the conserved Glu and Asp which are active site residues. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain B3Y613 TLR2 Pan troglodytes (Chimpanzee) 9598 Toll-like receptor 2 (CD antigen CD282) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q68RX9 psbN Panax ginseng (Korean ginseng) 4054 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P59888 Pandinus imperator (Emperor scorpion) 55084 Phospholipase A2 imperatoxin-1 (Imperatoxin I) (IpTx1) (IpTxi) (Imperatoxin inhibitor) [Cleaved into: Imperatoxin-1 large subunit (EC 3.1.1.4) (Imperatoxin I large subunit); Imperatoxin-1 small subunit (Imperatoxin I small subunit)] In contrast to other phospholipases, it lacks the typical Asp active site (Asp->Glu in position 93). {ECO:0000305}. degenerate-domain Q9TSP2 TLR4 Papio anubis (Olive baboon) 9555 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain B6VH79 SPACA3 Papio hamadryas (Hamadryas baboon) 9557 Sperm acrosome membrane-associated protein 3 (Sperm protein reactive with antisperm antibodies) (Sperm protein reactive with ASA) [Cleaved into: Sperm acrosome membrane-associated protein 3, membrane form; Sperm acrosome membrane-associated protein 3, processed form] Although it belongs to the glycosyl hydrolase 22 family, Thr-122 and Asn-139 are present instead of the conserved Glu and Asp which are active site residues. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain C0SAI5 ECM14 Paracoccidioides brasiliensis (strain Pb03) 482561 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 489 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain C1GDH9 ECM14 Paracoccidioides brasiliensis (strain Pb18) 502780 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 489 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain C1HE31 ECM14 Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis) 502779 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 489 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q94715 Paramecium tetraurelia 5888 Putative cathepsin L 3 (EC 3.4.22.15) This protein may be non-functional as it lacks the cysteine active site residue which is replaced by Gly-132. {ECO:0000305}. degenerate-domain Q7U4S9 nrdR Parasynechococcus marenigrum (strain WH8102) 84588 Transcriptional repressor NrdR Lacks the conserved Cys in position 6 which is part of a zinc-finger along with Cys-3, Cys 31 and Cys-34. {ECO:0000305}. degenerate-domain Q7U9I8 psbN Parasynechococcus marenigrum (strain WH8102) 84588 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q06FP0 psbN Pelargonium hortorum (Common geranium) (Pelargonium inquinans x Pelargonium zonale) 4031 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B6H233 ecm14 Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) 500485 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 467 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q6YD92 Petrosia ficiformis (Common Mediterranean sponge) 68564 Silicatein (EC 3.4.22.-) After extraction of the protein with ammonium fluoride and hydrofluoric acid, His-137 and Cys-279 were reported to be oxidized but could be the artifactual results of sample handling. Leu-123 was also reported to be mono- and dimethylated. Despite sequence similarity with cathepsins, silicatein lacks the intra- and interchain disulfide bonds for conserved cysteines. No numeric data was provided to support the mass-spectrometric interpretations. {ECO:0000305|PubMed:19522542}. degenerate-domain A0T0B0 psbN Phaeodactylum tricornutum (strain CCAP 1055/1) 556484 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q3BAK9 psbN Phalaenopsis aphrodite subsp. formosana (Moth orchid) 308872 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P0CD28 ndhB1 Phaseolus vulgaris (Kidney bean) (French bean) 3885 NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase, subunit 2 A) (NADH-plastoquinone oxidoreductase subunit 2 A) This protein is smaller than usual in this organism, and may not be functional. {ECO:0000305}. degenerate-domain P0CD29 ndhB2 Phaseolus vulgaris (Kidney bean) (French bean) 3885 NAD(P)H-quinone oxidoreductase subunit 2 B, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase, subunit 2 B) (NADH-plastoquinone oxidoreductase subunit 2 B) This protein is smaller than usual in this organism, and may not be functional. {ECO:0000305}. degenerate-domain A4GGD3 psbN Phaseolus vulgaris (Kidney bean) (French bean) 3885 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P83909 Phoneutria reidyi (Brazilian Amazonian armed spider) (Ctenus reidyi) 272752 U2-ctenitoxin-Pr1a (U2-CNTX-Pr1a) (Neurotoxin PRTx22C1) While it is structurally defined as a knottin it lacks the conserved Cys residue in position 9. {ECO:0000305}. degenerate-domain Q67HX4 psbN Phormium tenax (New Zealand flax) 51475 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6EYG3 psbN Phytolacca americana (American pokeweed) (Phytolacca decandra) 3527 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain G4ZHR3 XLP1 Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines) 1094619 Inactive glycoside hydrolase XLP1 (Glycoside hydrolase family 12 protein XLP1) (GH12 protein XLP1) (XEG1-like protein 1) Lacks the conserved Glu residue in position 222 essential activity and has thereforelost enzyme activity. {ECO:0000269|PubMed:28082413}. degenerate-domain B1XIE2 psbN Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) 32049 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain V5NAL9 Pinctada imbricata (Atlantic pearl-oyster) (Pinctada martensii) 66713 Toll-like receptor 4 (PmTLR4) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q7GUC9 psbN Pinus koraiensis (Korean pine) 88728 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P41626 psbN Pinus thunbergii (Japanese black pine) (Pinus thunbergiana) 3350 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q06GN2 psbN Piper cenocladum (Ant piper) 398741 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9XQR4 psbN Pisum sativum (Garden pea) (Lathyrus oleraceus) 3888 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A0A509AQ20 UIS2 Plasmodium berghei (strain Anka) 5823 Serine/threonine-protein phosphatase UIS2 (Up-regulated in infective sporozoite protein 2) (EC 3.1.3.16) The protein phosphatase family which UIS2 belongs to is unclear. Due to its cofactor requirements, it is thought to belong to the PP2C family, however, the protein lacks the canonical PP2C catalytic domain features (PubMed:26735921). Appears to show high similarity to purple acid phosphatases. {ECO:0000303|PubMed:26735921, ECO:0000305}. degenerate-domain C0H582 AKLP2 Plasmodium falciparum (isolate 3D7) 36329 Inactive adenylate kinase (Adenylate kinase-like protein 2) Although it belongs to the adenylate kinase family, lacks several residues involved in ATP and AMP binding and has no adenylate kinase activity. {ECO:0000269|PubMed:22819813}. degenerate-domain A0A2I0BUK1 SOPT Plasmodium falciparum (isolate NF54) 5843 Inactive subtilisin-like protease SOPT (Subtilisin-like ookinete protein important for transmission) In contrast to other members of the peptidase S8 family, contains Gly and Glu residues at the position of the canonical catalytic Asp and His, respectively, suggesting that the protein lacks protease activity. {ECO:0000305}. degenerate-domain Q6EYF1 psbN Platanus occidentalis (Sycamore) (American plane tree) 4403 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A6YG90 psbN Pleurastrum terricola (Filamentous green alga) (Leptosira terrestris) 34116 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q5R9Z5 ABCF3 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 ATP-binding cassette sub-family F member 3 Lacks transmembrane domains and is probably not involved in transport. {ECO:0000305}. degenerate-domain Q5RCJ0 ADPRHL1 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Inactive ADP-ribosyltransferase ARH2 (ADP-ribosylhydrolase-like protein 1) ([Protein ADP-ribosylarginine] hydrolase-like protein 1) Although it belongs to the ADP-ribosylglycohydrolase family, lacks the metal-binding and substrate-binding residues, suggesting that it has no hydrolase activity. {ECO:0000250|UniProtKB:Q6AZR2}. degenerate-domain Q5RE48 AKTIP Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 AKT-interacting protein (Fused toes protein homolog) Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q5RBP6 CHI3L1 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Chitinase-3-like protein 1 Although it belongs to the glycosyl hydrolase 18 family, Leu-167 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity. {ECO:0000305}. degenerate-domain Q5REY0 COPS6 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 COP9 signalosome complex subunit 6 (SGN6) (Signalosome subunit 6) Although related to the peptidase M67A family, it lacks the JAMM motif that probably constitutes the catalytic center and therefore it probably does not have a protease activity. {ECO:0000305}. degenerate-domain Q5R9Y6 DPYSL2 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Dihydropyrimidinase-related protein 2 (DRP-2) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q5R7K0 HSDL1 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Inactive hydroxysteroid dehydrogenase-like protein 1 Although it belongs to the SDR family, Phe-218 is present instead of the conserved Tyr which is an active site residue. It is therefore expected that this protein lacks oxidoreductase activity. {ECO:0000305}. degenerate-domain Q5R989 MTMR12 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Myotubularin-related protein 12 (Inactive phosphatidylinositol 3-phosphatase 12) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 391 in the dsPTPase catalytic loop and does not have phosphatase activity. {ECO:0000250|UniProtKB:Q9C0I1}. degenerate-domain Q5RAI8 NUDT21 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Cleavage and polyadenylation specificity factor subunit 5 (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Nudix hydrolase 21) Lacks the conserved metal-binding residues in the NUDIX motif and is not expected to have hydrolase activity. {ECO:0000305}. degenerate-domain Q5RDI1 PAMR1 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Inactive serine protease PAMR1 (Peptidase domain-containing protein associated with muscle regeneration 1) (Regeneration-associated muscle protease homolog) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 665 which is replaced by a Thr, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain Q5R5F8 PANK4 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 4'-phosphopantetheine phosphatase (EC 3.1.3.-) (Inactive pantothenic acid kinase 4) Despite belonging to the type II pantothenate kinase family, the pantothenate kinase domain contains a Val residue at position 147 and a Trp residue at position 211 instead of the two conserved active site residues, Glu and Arg. Lacks pantothenate kinase activity. {ECO:0000250|UniProtKB:Q9NVE7}. degenerate-domain Q5RCR5 SUMF2 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Inactive C-alpha-formylglycine-generating enzyme 2 (Sulfatase-modifying factor 2) Although strongly similar to formylglycine-generating enzyme, lacks the catalytic Cys residues that bind the catalytic copper. The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation. {ECO:0000305}. degenerate-domain Q5R761 USP39 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Ubiquitin carboxyl-terminal hydrolase 39 (EC 3.4.19.12) (U4/U6.U5 tri-snRNP-associated 65 kDa protein) Lacks the conserved His and Cys residues that are essential for the activity of de-ubiquitinating enzymes. Lacks ubiquitin C-terminal hydrolase activity. {ECO:0000250|UniProtKB:Q53GS9, ECO:0000305}. degenerate-domain B6VH77 SPACA3 Pongo pygmaeus (Bornean orangutan) 9600 Sperm acrosome membrane-associated protein 3 (Sperm protein reactive with antisperm antibodies) (Sperm protein reactive with ASA) [Cleaved into: Sperm acrosome membrane-associated protein 3, membrane form; Sperm acrosome membrane-associated protein 3, processed form] Although it belongs to the glycosyl hydrolase 22 family, Thr-122 and Asn-139 are present instead of the conserved Glu and Asp which are active site residues. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain Q8SPE9 TLR4 Pongo pygmaeus (Bornean orangutan) 9600 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q14FC9 psbN Populus alba (White poplar) 43335 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P68860 psbN Populus deltoides (Eastern poplar) (Eastern cottonwood) 3696 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P51324 psbN Porphyra purpurea (Red seaweed) (Ulva purpurea) 2787 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A2BP51 psbN Prochlorococcus marinus (strain AS9601) 146891 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A9BDM3 psbN Prochlorococcus marinus (strain MIT 9211) 93059 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A8G2R2 psbN Prochlorococcus marinus (strain MIT 9215) 93060 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A3PAX4 psbN Prochlorococcus marinus (strain MIT 9301) 167546 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A2CCI4 psbN Prochlorococcus marinus (strain MIT 9303) 59922 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q31CT0 psbN Prochlorococcus marinus (strain MIT 9312) 74546 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7V4V1 psbN Prochlorococcus marinus (strain MIT 9313) 74547 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A2BUN3 psbN Prochlorococcus marinus (strain MIT 9515) 167542 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7VDT4 psbN Prochlorococcus marinus (strain SARG / CCMP1375 / SS120) 167539 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7V340 psbN Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4) 59919 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9HVT2 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 Alpha-2-macroglobulin homolog Lacks the conserved thioester bond that is characteristic of the alpha-2-macroglobulins. {ECO:0000305}. degenerate-domain P68747 argK Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv. phaseolicola) 319 Ornithine carbamoyltransferase 2, anabolic (OTCase 2) (EC 2.1.3.3) (Ornithine carbamoyltransferase 2, phaseolotoxin-insensitive) (Phaseolotoxin-resistant ornithine carbamoyltransferase) (Toxin-resistant enzyme) (ROCT) Lacks the conserved threonine residue in position 60, which is part of the carbamoylphosphate binding site; it is replaced by a glycine residue. {ECO:0000305}. degenerate-domain O33478 amnA Pseudomonas sp 306 2-aminophenol 1,6-dioxygenase alpha subunit In contrast to other members of the family, lacks the conserved iron-binding sites, suggesting it has no oxidoreductase activity. {ECO:0000305}. degenerate-domain P68746 argK Pseudomonas syringae pv. actinidiae 103796 Ornithine carbamoyltransferase 2, phaseolotoxin-insensitive (OTCase 2) (EC 2.1.3.3) (ROCT) Lacks the conserved threonine residue in position 60, which is part of the carbamoylphosphate binding site; it is replaced by a glycine residue. {ECO:0000305}. degenerate-domain Q8WHZ5 psbN Psilotum nudum (Whisk fern) (Lycopodium nudum) 3240 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q1XDG2 psbN Pyropia yezoensis (Susabi-nori) (Porphyra yezoensis) 2788 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q66H39 Abcf3 Rattus norvegicus (Rat) 10116 ATP-binding cassette sub-family F member 3 Lacks transmembrane domains and is probably not involved in transport. {ECO:0000305}. degenerate-domain Q4FZU4 Adamtsl4 Rattus norvegicus (Rat) 10116 ADAMTS-like protein 4 (ADAMTSL-4) Although similar to members of the ADAMTS family, it lacks the metalloprotease and disintegrin-like domains which are typical of that family. {ECO:0000305}. degenerate-domain P97616 Adarb2 Rattus norvegicus (Rat) 10116 Inactive double-stranded RNA-specific editase B2 (RNA-dependent adenosine deaminase 3) (RNA-editing deaminase 2) (RNA-editing enzyme 2) (dsRNA adenosine deaminase B2) Although it is similar to the double-stranded RNA adenosine deaminases ADAR/ADAR1 and ADARB1/ADAR2 and capable of binding RNA, it lacks double-stranded RNA adenosine deaminase activity in vitro. Instead, it inhibits adenosine-to-inosine editing in vivo. {ECO:0000269|PubMed:8943218}. degenerate-domain Q5XIB3 Adprhl1 Rattus norvegicus (Rat) 10116 Inactive ADP-ribosyltransferase ARH2 (ADP-ribosylhydrolase-like protein 1) ([Protein ADP-ribosylarginine] hydrolase-like protein 1) Although it belongs to the ADP-ribosylglycohydrolase family, lacks the metal-binding and substrate-binding residues, suggesting that it has no hydrolase activity. {ECO:0000250|UniProtKB:Q6AZR2}. degenerate-domain A2RUV9 Aebp1 Rattus norvegicus (Rat) 10116 Adipocyte enhancer-binding protein 1 (AE-binding protein 1) (Aortic carboxypeptidase-like protein) Although related to peptidase M14 family, lacks the active site residues and zinc-binding sites, suggesting that it has no carboxypeptidase activity. {ECO:0000305}. degenerate-domain Q5FVH4 Aktip Rattus norvegicus (Rat) 10116 AKT-interacting protein (Fused toes protein homolog) Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q5PPN4 Ca8 Rattus norvegicus (Rat) 10116 Carbonic anhydrase-related protein (CARP) (Carbonic anhydrase VIII) (CA-VIII) Although it belongs to the alpha-carbonic anhydrase family, Arg-116 is present instead of the conserved His which is a zinc-binding residue. It is therefore expected that this protein lacks carbonic anhydrase activity. {ECO:0000305}. degenerate-domain Q9WTV1 Chi3l1 Rattus norvegicus (Rat) 10116 Chitinase-3-like protein 1 (Cartilage glycoprotein 39) (CGP-39) (GP-39) Although it belongs to the glycosyl hydrolase 18 family, Leu-138 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity. {ECO:0000305}. degenerate-domain Q66HG3 Cndp1 Rattus norvegicus (Rat) 10116 Beta-Ala-His dipeptidase (EC 3.4.13.20) (CNDP dipeptidase 1) (Carnosine dipeptidase 1) In contrast to the human protein, it is unlikely to be secreted because it lacks the N-terminal signal sequence required for secretion. Furthermore, its activity was assessed from the soluble fraction prepared from tissues or cells not from a secreted fraction (By similarity). It could also have a slightly different substrate specificity (By similarity). {ECO:0000250|UniProtKB:Q8BUG2}. degenerate-domain Q62950 Crmp1 Rattus norvegicus (Rat) 10116 Dihydropyrimidinase-related protein 1 (DRP-1) (Collapsin response mediator protein 1) (CRMP-1) (Inactive dihydropyrimidinase) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain P47942 Dpysl2 Rattus norvegicus (Rat) 10116 Dihydropyrimidinase-related protein 2 (DRP-2) (Collapsin response mediator protein 2) (CRMP-2) (Turned on after division 64 kDa protein) (TOAD-64) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q62952 Dpysl3 Rattus norvegicus (Rat) 10116 Dihydropyrimidinase-related protein 3 (DRP-3) (Collapsin response mediator protein 4) (CRMP-4) (TOAD-64/Ulip/CRMP) (TUC-4b) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q62951 Dpysl4 Rattus norvegicus (Rat) 10116 Dihydropyrimidinase-related protein 4 (DRP-4) (Collapsin response mediator protein 3) (CRMP-3) (UNC33-like phosphoprotein 4) (ULIP-4) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9JHU0 Dpysl5 Rattus norvegicus (Rat) 10116 Dihydropyrimidinase-related protein 5 (DRP-5) (UNC33-like phosphoprotein 6) (ULIP-6) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain P0C0K7 Ephb6 Rattus norvegicus (Rat) 10116 Ephrin type-B receptor 6 (Tyrosine-protein kinase-defective receptor EPH-6) Although this protein belongs to the kinase superfamily, it lacks key residues required for catalytic activity, suggesting that it does not have kinase activity. In addition, lacks kinase activity in vitro. Despite the lack of kinase activity, can bind ATP. {ECO:0000250|UniProtKB:O15197}. degenerate-domain Q4V8B7 Hsdl1 Rattus norvegicus (Rat) 10116 Inactive hydroxysteroid dehydrogenase-like protein 1 Although it belongs to the SDR family, Phe-218 is present instead of the conserved Tyr which is an active site residue. It is therefore expected that this protein lacks oxidoreductase activity. {ECO:0000305}. degenerate-domain D4ABW7 Lyzl4 Rattus norvegicus (Rat) 10116 Lysozyme-like protein 4 (Lysozyme-4) Although it belongs to the glycosyl hydrolase 22 family, Gly-72 is present instead of the conserved Asp which is an active site residue. It is therefore expected that this protein lacks hydrolase activity. {ECO:0000305}. degenerate-domain Q5FVM6 Mtmr12 Rattus norvegicus (Rat) 10116 Myotubularin-related protein 12 (Inactive phosphatidylinositol 3-phosphatase 12) (Phosphatidylinositol 3-phosphatase-associated protein) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 392 in the dsPTPase catalytic loop and does not have phosphatase activity. {ECO:0000250|UniProtKB:Q9C0I1}. degenerate-domain P86172 Nmral1 Rattus norvegicus (Rat) 10116 NmrA-like family domain-containing protein 1 Lacks the conserved Tyr residue in the active site triad of Ser-Tyr-Lys necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity. {ECO:0000305}. degenerate-domain Q4KM65 Nudt21 Rattus norvegicus (Rat) 10116 Cleavage and polyadenylation specificity factor subunit 5 (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Nudix hydrolase 21) Lacks the conserved metal-binding residues in the NUDIX motif and is not expected to have hydrolase activity. {ECO:0000305}. degenerate-domain Q3B7D8 Otulinl Rattus norvegicus (Rat) 10116 Inactive ubiquitin thioesterase OTULINL Although highly similar to the deubiquitinase OTULIN, lacks both the conserved active site residue Cys at position 136 which is replaced by an Asp residue and the conserved active site residue His at residue 347 which is replaced by a Gln residue, and does not have deubiquitinase activity. {ECO:0000250|UniProtKB:Q9NUU6}. degenerate-domain Q923S8 Pank4 Rattus norvegicus (Rat) 10116 4'-phosphopantetheine phosphatase (EC 3.1.3.-) (Inactive pantothenic acid kinase 4) (rPanK4) Despite belonging to the type II pantothenate kinase family, the pantothenate kinase domain contains a Val residue at position 147 and a Trp residue at position 211 instead of the two conserved active site residues, Glu and Arg. Lacks pantothenate kinase activity. {ECO:0000250|UniProtKB:Q9NVE7}. degenerate-domain Q62688 Plcl1 Rattus norvegicus (Rat) 10116 Inactive phospholipase C-like protein 1 (PLC-L1) (PRIP1) (Phospholipase C-related but catalytically inactive protein) (p130) In the PI-PLC X-box Asn-459 is present instead of the conserved His which is one of the active site residues. It is therefore expected that this protein lacks catalytic activity. {ECO:0000305}. degenerate-domain Q5R212 Prss35 Rattus norvegicus (Rat) 10116 Inactive serine protease 35 Although related to peptidase S1 family, lacks the conserved active Ser residue in position 339 which is replaced by a Thr, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain Q6IE62 Prss45 Rattus norvegicus (Rat) 10116 Inactive serine protease 45 (Inactive testis serine protease 5) In contrast to other members of the family, lacks the conserved Ser at position 243 which is replaced by a Pro residue, suggesting it is inactive. {ECO:0000305}. degenerate-domain Q6AY28 Prss54 Rattus norvegicus (Rat) 10116 Inactive serine protease 54 (Plasma kallikrein-like protein 4) Although related to peptidase S1 family, lacks the essential His, Asp, and Ser residues of the catalytic triad at positions 73, 119 and 210 and is therefore predicted to have lost protease activity. {ECO:0000305}. degenerate-domain Q6IMA3 Rasl11a Rattus norvegicus (Rat) 10116 Ras-like protein family member 11A (EC 3.6.5.2) Although highly related to the Ras family, lacks the conserved prenylation motif at the C-terminus, which serves to target Ras proteins to membrane compartments. {ECO:0000305}. degenerate-domain Q923U9 Slc40a1 Rattus norvegicus (Rat) 10116 Ferroportin (CAR1) (Cell adhesion regulator) (Ferroportin-1) (Solute carrier family 40 member 1) Manganese (Mn) transport by SLC40A1 remains controversial. Some in vitro studies have suggested that SLC40A1 transports minimal amounts of Mn(2+) (By similarity). Other groups have suggested that it does not. The affinity of SLC40A1 for manganese is extremely low compared with iron, implying that any SLC40A1-mediated Mn transport in vivo would likely be trivial (By similarity). A recent study examined the role of SLC40A1 in Mn homeostasis by using Tmprss6-O mice, which express high levels of hepcidin/HAMP and therefore have very low SLC40A1 levels in their tissues. These mice show frank iron deficiency and reduced iron levels in most tissues, but manganese levels are largely unaffected (By similarity). These studies suggest that manganese is probably not the physiological substrate of SLC40A1. {ECO:0000250|UniProtKB:Q9JHI9, ECO:0000250|UniProtKB:Q9NP59, ECO:0000305}. degenerate-domain P06882 Tg Rattus norvegicus (Rat) 10116 Thyroglobulin (Tg) The cholinesterase-like (ChEL) region lacks the Ser residue of the catalytic triad suggesting that it has no esterase activity. {ECO:0000305}. degenerate-domain Q9QX05 Tlr4 Rattus norvegicus (Rat) 10116 Toll-like receptor 4 (Toll4) (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain A6MW33 psbN Rhodomonas salina (Pyrenomonas salina) 3034 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q3E7Y4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Putative uncharacterized helicase-like protein YBL112C Could be the product of a pseudogene. Although strongly related to DNA helicases, it lacks the helicase ATP-binding domains, suggesting that it has no helicase activity. {ECO:0000305}. degenerate-domain P40361 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Inactive deaminase YJL070C Lacks the conserved His residues essential for binding the catalytic zinc ion. Lacks the conserved residues important for substrate binding and catalysis. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q3E7Y5 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Uncharacterized helicase-like protein YBL111C Although strongly related to DNA helicases, it lacks the helicase C-terminal domain, suggesting that it has no helicase activity. {ECO:0000305}. degenerate-domain P38150 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Inactive deaminase YBR284W Lacks the conserved His residues essential for binding the catalytic zinc ion. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q08993 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Putative uncharacterized protein YPR202W Could be the product of a pseudogene. Although strongly related to DNA helicases, it lacks the helicase domains, suggesting that it has no helicase activity. {ECO:0000305}. degenerate-domain O13556 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Putative uncharacterized protein YLR462W Could be the product of a pseudogene. Although strongly related to DNA helicases, it lacks the helicase domains, suggesting that it has no helicase activity. {ECO:0000305}. degenerate-domain P0CX16 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Putative uncharacterized protein YEL076C-A Could be the product of a pseudogene. Although strongly related to DNA helicases, it lacks the helicase domains, suggesting that it has no helicase activity. {ECO:0000305}. degenerate-domain Q08994 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Putative uncharacterized protein YPR203W Could be the product of a pseudogene. Although strongly related to DNA helicases, it lacks the helicase domains, suggesting that it has no helicase activity. {ECO:0000305}. degenerate-domain A0A023PXF5 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Putative uncharacterized helicase-like protein YHR218W-A Could be the product of a pseudogene unlikely to encode a functional protein. Although strongly related to DNA helicases, it lacks the helicase ATP-binding domains, suggesting that it has no helicase activity. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set. {ECO:0000305|PubMed:24374639}. degenerate-domain P0CX17 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Putative uncharacterized protein YLR464W Could be the product of a pseudogene. Although strongly related to DNA helicases, it lacks the helicase domains, suggesting that it has no helicase activity. {ECO:0000305}. degenerate-domain Q08361 AAD15 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Putative aryl-alcohol dehydrogenase AAD15 (EC 1.1.1.-) In contrast to other aldo/keto reductase 2 proteins, it lacks the N-terminal half which contains the active site. It is therefore unlikely that it acts as a functional oxydoreductase. {ECO:0000305}. degenerate-domain P38836 ECM14 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Inactive metallocarboxypeptidase ECM14 (Extracellular mutant protein 14) Lacks the conserved Glu residue in position 391 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000269|PubMed:33256608}. degenerate-domain P40492 FYV10 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 GID complex subunit 9 (EC 2.3.2.27) (Function required for yeast viability protein 10) (Glucose-induced degradation protein 9) (Probable E3 ubiquitin-protein ligase GID9) It is not certain that this protein has E3 ubiquitin-protein ligase activity by itself. Lacks a detectable RING-type zinc finger domain; the sequence in this region is highly divergent and lacks most of the expected Cys residues. Still, Cys-434 in this highly divergent region is required for ubiquitination of FBP1, suggesting a direct role in catalyzing ubiquitination. {ECO:0000305|PubMed:22044534}. degenerate-domain Q02733 IRC15 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Increased recombination centers protein 15 Although strongly related to the LPD1 dihydrolipoyl dehydrogenase, it lacks the redox-active disulfide bond suggesting that it has no dehydrogenase activity. {ECO:0000305}. degenerate-domain Q04638 ITT1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 E3 ubiquitin-protein ligase ITT1 (EC 2.3.2.31) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain P11914 MAS2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (Inactive zinc metalloprotease alpha) (Matrix processing peptidase) (MPP) (Mitochondrial assembly protein 2) (Mitochondrial import function protein 2) Was originally thought to be the catalytic subunit (PubMed:3061797). The low processing activity which was previously observed with alpha-MPP which has been purified from a mitochondrial extract is most likely due to contamination by the beta-subunit. Does not seem to have protease activity as it lacks the zinc-binding site (PubMed:9299349). {ECO:0000305, ECO:0000305|PubMed:3061797, ECO:0000305|PubMed:9299349}. degenerate-domain P16658 SEN2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 tRNA-splicing endonuclease subunit SEN2 (EC 4.6.1.16) (Splicing endonuclease protein 2) (tRNA-intron endonuclease SEN2) According to PubMed:9200603, it contains a transmembrane domain and may be responsible to anchor the complex into membranes, however, PubMed:12925762 showed that it is peripherically associated with membranes, and is probably not a transmembrane protein. {ECO:0000305}. degenerate-domain Q9URQ3 TAD3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 tRNA-specific adenosine-34 deaminase regulatory subunit TAD3 In contrast to other cytidine and deoxycytidylate deaminase, lacks to conserved Glu active site in position 218 which is replaced by a Val residue, suggesting that it acts as a regulatory subunit. {ECO:0000305}. degenerate-domain O13527 TY1B-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Truncated transposon Ty1-A Gag-Pol polyprotein (TY1B) (Transposon Ty1 TYB polyprotein) [Cleaved into: Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] Transposon Ty1-A (YARCTy1-1) contains a frameshift at position 610, which disrupts the ORF coding for protein TY1B. This is the truncated, C-terminal part of TY1B translated from an in-frame start codon, and it is probably not functional. {ECO:0000305}. degenerate-domain A0A0B7P3V8 TY4B-P Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Transposon Ty4-P Gag-Pol polyprotein (TY4A-TY4B) (Transposon Ty4 TYA-TYB polyprotein) [Includes: Capsid protein (CA); Ty4 protease (PR) (EC 3.4.23.-); Integrase (IN); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)] Could be the product of a pseudogene. Transposon Ty4-P (YPLCTy4-1) contains a frameshift at position 1105, which disrupts the ORF coding for protein TY4B. It is probably not functional. {ECO:0000305}. degenerate-domain Q06685 VIP1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) (InsP6 and PP-IP5 kinase) Although related to histidine acid phosphatase proteins, it lacks the conserved active sites, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain A4FQE4 Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338) 405948 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q6L374 psbN Saccharum hybrid (Sugarcane) 15819 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6ENT6 psbN Saccharum officinarum (Sugarcane) 4547 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8HS19 psbN Sagittaria latifolia (Broadleaf arrowhead) (Sagittaria chinensis) 15008 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7GZA1 psbN Salicornia europaea (Common glasswort) (Salicornia herbacea) 206448 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain B5X1G6 aktip Salmo salar (Atlantic salmon) 8030 AKT-interacting protein (Fused toes protein homolog) Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q57I19 ccmAE Salmonella choleraesuis (strain SC-B67) 321314 Putative bifunctional cytochrome c-type biogenesis protein CcmAE [Includes: Cytochrome c biogenesis ATP-binding export protein CcmA 2 (EC 7.6.2.5) (Heme exporter protein A 2); Cytochrome c-type biogenesis protein CcmE 2 (Cytochrome c maturation protein E 2) (Heme chaperone CcmE 2)] This sequence is a fusion of the duplicated copies ccmA2 and ccmE2, however, important parts of the proteins are missing and it is therefore probably not functional. {ECO:0000305}.; degenerate-domain Q5PGB8 yccX Salmonella paratyphi A (strain ATCC 9150 / SARB42) 295319 Acylphosphatase (EC 3.6.1.7) (Acylphosphate phosphohydrolase) Lacks the conserved active site Arg in position 20. There is a histidine in this position. {ECO:0000305}. degenerate-domain Q7CPJ9 panM Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 PanD regulatory factor Lacks the conserved catalytic glutamate found in many enzymatically active members of the Gcn5-like N-acetyltransferase (GNAT) family. {ECO:0000305|PubMed:22782525}. degenerate-domain A0A834RHI5 Sarcoptes scabiei (Itch mite) (Acarus scabiei) 52283 Complement inhibitor S-D1 (Inactive serine protease S-D1) (Scabies mite inactivated protease paralog S-D1) (SMIPPS D1) Although it belongs to the peptidase S1 family, lacks the active site residues and has no protease activity. {ECO:0000269|PubMed:19427318, ECO:0000269|PubMed:19494305}. degenerate-domain Q6VPT6 Sarcoptes scabiei (Itch mite) (Acarus scabiei) 52283 Complement inhibitor S-I1 (Inactive serine protease S-I1) (Scabies mite inactivated protease paralog S-I1) (SMIPPS I1) Although it belongs to the peptidase S1 family, lacks the active site serine residue and has no protease activity. {ECO:0000269|PubMed:19427318, ECO:0000269|PubMed:19494305}. degenerate-domain Q6EYE3 psbN Saruma henryi (Upright wild ginger) 13258 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7J186 psbN Saururus cernuus (Lizard's tail) 13260 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8HS15 psbN Schisandra chinensis (Chinese magnolia vine) (Kadsura chinensis) 50507 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9P6J8 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Uncharacterized deaminase C1683.02 (EC 3.5.4.-) Although clearly a member of the adenine deaminase type 2 family, it lacks the conserved Glu active site residue in position 212 characteristic for this family. Its exact enzymatic activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9UT22 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Methylthioribulose-1-phosphate dehydratase-like protein In contrast to other members of the family, it lacks the conserved zinc-binding residues. {ECO:0000305}. degenerate-domain O43023 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Inactive zinc metalloprotease C354.09c Although related to the peptidase M28 family, it lacks the conserved zinc-binding and active sites and therefore has probably lost hydrolase activity. {ECO:0000305}. degenerate-domain G2TRN7 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Truncated RecQ DNA helicase-like protein C212.06c Is probably not a functional DNA helicase since the N-ter is truncated and missing the ATP-binding domain. {ECO:0000305}. degenerate-domain O74429 asp1 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) (Cortical actin cytoskeleton protein asp1) (InsP6 and PP-IP5 kinase) Although related to histidine acid phosphatase proteins, it lacks the conserved active sites, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain O74818 ecm14 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 458 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q09918 hsp3105 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Putative glutathione-independent glyoxalase hsp3105 (EC 4.2.1.130) (Glyoxalase 3 homolog 5) (Heat shock protein 31 homolog 5) Lacks the conserved active site residues critical for glyoxalase activity. Its enzyme activity is therefore unsure. {ECO:0000305|PubMed:24758716}. degenerate-domain Q10447 ppk2 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Protein kinase domain-containing protein ppk2 Lacks the active site aspartate. {ECO:0000305}. degenerate-domain O13846 scs7 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Ceramide very long chain fatty acid hydroxylase scs7 (Ceramide VLCFA hydroxylase scs7) (EC 1.14.18.-) Lacks the conserved N-terminal cytochrome b5 heme-binding domain. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q9P7N4 tad3 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 tRNA-specific adenosine-34 deaminase regulatory subunit tad3 In contrast to other cytidine and deoxycytidylate deaminase, lacks the conserved Glu active site in position 213 which is replaced by a Val residue, suggesting that it acts as a regulatory subunit. {ECO:0000250|UniProtKB:Q9URQ3, ECO:0000305}. degenerate-domain Q6YLT7 psbN Sciadopitys verticillata (Japanese umbrella-pine) (Taxus verticillata) 28979 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A7EUC0 ecm14 Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) 665079 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 506 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain P68856 psbN Secale cereale (Rye) 4550 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8EK29 argF Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1) 211586 Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3) Lacks the conserved threonine residue in position 50, which is part of the carbamoylphosphate binding site; it is replaced by a leucine residue. {ECO:0000305}. degenerate-domain Q31YW9 rihB Shigella boydii serotype 4 (strain Sb227) 300268 Putative pyrimidine-specific ribonucleoside hydrolase RihB (EC 3.2.2.8) (Cytidine/uridine-specific hydrolase) This sequence is 71 amino acid shorter than orthologs and therefore lacks two conserved residues involved in calcium binding and active site activity. The two other residues involved in calcium binding are present but it is not known if they still bind calcium. {ECO:0000305}. degenerate-domain Q32ER0 rihB Shigella dysenteriae serotype 1 (strain Sd197) 300267 Putative pyrimidine-specific ribonucleoside hydrolase RihB (EC 3.2.2.8) (Cytidine/uridine-specific hydrolase) This sequence is 42 amino acid shorter than orthologs and therefore lacks two conserved residues involved in calcium binding and active site activity. The two other residues involved in calcium binding are present but it is not known if they still bind calcium. {ECO:0000305}. degenerate-domain Q9RCT3 Shigella flexneri 623 Putative hemolysin E-like protein Could be the product of a pseudogene. Although it is strongly related to the hemolysin E toxin from E.coli K12 strain, it lacks all the C-terminal part of the protein, due to a deletion that creates a frameshift, and it is therefore not functional. {ECO:0000305}. degenerate-domain P0AE51 ytfP Shigella flexneri 623 Gamma-glutamylcyclotransferase family protein YtfP Lacks the conserved Glu residue at position 70 that serves as proton acceptor in enzymes with gamma-glutamylcyclotransferase activity. {ECO:0000305}. degenerate-domain P55559 Sinorhizobium fredii (strain NBRC 101917 / NGR234) 394 Integrase-like protein y4lS Lacks the conserved serine which acts in the transient covalent linkage to DNA during strand cleavage and rejoining. {ECO:0000305}. degenerate-domain Q67HX0 psbN Sisyrinchium montanum (Strict blue-eyed grass) 207934 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q2MIG0 psbN Solanum bulbocastanum (Ornamental nightshade) 147425 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9THX6 CLEB3J9 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) 4081 Thylakoid lumenal 29 kDa protein, chloroplastic (TL29) (EC 1.-.-.-) (LeAPx09) (P29) Probably not an ascorbate peroxidase (APx), as it lacks the heme-binding site, the proton acceptor and the transition state stabilizer, which are conserved features of the ascorbate peroxidase. {ECO:0000305}. degenerate-domain Q2MI73 psbN Solanum lycopersicum (Tomato) (Lycopersicon esculentum) 4081 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q3YJS9 pat3-k1 Solanum tuberosum (Potato) 4113 Probable inactive patatin-3-Kuras 1 Lacks the conserved Ser residue involved in nucleophilic attack and essential for hydrolase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q2VEF2 psbN Solanum tuberosum (Potato) 4113 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain C5WWY0 Sorghum bicolor (Sorghum) (Sorghum vulgare) 4558 Probable inactive acireductone dioxygenase 2 This enzyme lacks one or more conserved metal-binding sites. It may be non-functional. {ECO:0000305}. degenerate-domain A1E9V2 psbN Sorghum bicolor (Sorghum) (Sorghum vulgare) 4558 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7HIV8 psbN Spathiphyllum wallisii (Peace lily) 85269 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6W630 psbN Sphagnum cuspidatum (Bog moss) 41840 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P62116 psbN Spinacia oleracea (Spinach) 3562 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q71KP7 psbN Spirogyra maxima (Green alga) 3180 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q71L86 psbN Stangeria eriopus (Natal grass cycad) (Lomaria eriopus) 34343 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q32RU3 psbN Staurastrum punctulatum (Green alga) (Cosmoastrum punctulatum) 102822 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q6EYD5 psbN Stewartia pseudocamellia (Japanese stewartia) (Stewartia koreana) 59679 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q06SI7 psbN Stigeoclonium helveticum (Green alga) 55999 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9EUR3 xerD Streptococcus mitis 28037 Tyrosine recombinase XerD-like Although named XerD by PubMed:11763967, it is not the ortholog of XerD and constitutes a distinct protein family. In contrast to the classic XerD protein, it does not contain the Arg-His-Arg-His (R-H-R-H) sandwich residues that are clustered with the Tyr active site. It also lacks the C-terminal region which is known to mediate the interaction with XerC. It is therefore unknown whether it has tyrosine recombinase activity or act as a regulator. {ECO:0000305}. degenerate-domain Q8DNP8 queF Streptococcus pneumoniae (strain ATCC BAA-255 / R6) 171101 Putative NADPH-dependent 7-cyano-7-deazaguanine reductase (EC 1.7.1.13) (7-cyano-7-carbaguanine reductase) (NADPH-dependent nitrile oxidoreductase) (PreQ(0) reductase) Lacks the conserved cysteine residue that is involved in the formation of the covalent thioimide linkage with the substrate; it is replaced by a glycine residue (Gly-45). The enzyme may thus be inactive. {ECO:0000305}. degenerate-domain P0A4T0 xerD Streptococcus pneumoniae (strain ATCC BAA-255 / R6) 171101 Tyrosine recombinase XerD-like Although named XerD by PubMed:11763967, it is not the ortholog of XerD and constitutes a distinct protein family. In contrast to the classic XerD protein, it does not contain the Arg-His-Arg-His (R-H-R-H) sandwich residues that are clustered with the Tyr active site. It also lacks the C-terminal region which is known to mediate the interaction with XerC. It is therefore unknown whether it has tyrosine recombinase activity or act as a regulator. {ECO:0000305}. degenerate-domain Q97P67 queF Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) 170187 Putative NADPH-dependent 7-cyano-7-deazaguanine reductase (EC 1.7.1.13) (7-cyano-7-carbaguanine reductase) (NADPH-dependent nitrile oxidoreductase) (PreQ(0) reductase) Lacks the conserved cysteine residue that is involved in the formation of the covalent thioimide linkage with the substrate; it is replaced by a glycine residue (Gly-45). The enzyme may thus be inactive. {ECO:0000305}. degenerate-domain Q9RR30 oleL Streptomyces antibioticus 1890 Probable dTDP-4-oxo-2,6-dideoxy-D-glucose 3,5-epimerase (EC 5.1.3.-) In contrast to other members of the family, lacks the conserved His active site in position 60, which is replaced by an Thr residue, suggesting a different reaction mechanism. {ECO:0000305}. degenerate-domain Q82G68 Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) 227882 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q9F3C7 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) 100226 Formylglycine-generating enzyme (FGE) (sc-FGE) (EC 1.8.3.7) The disulfide bond observed in the structure does not exist in vivo (PubMed:18390551). The enzyme reaction was initially thought to act via a redox-active disulfide bond mechanism; however the disulfide bond only takes place with inactive enzyme that lacks the copper cofactor (PubMed:25931126). The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation (PubMed:25931126). {ECO:0000269|PubMed:18390551, ECO:0000269|PubMed:25931126}. degenerate-domain Q9K4F9 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) 100226 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain P95746 tylMIII Streptomyces fradiae (Streptomyces roseoflavus) 1906 Protein TylM3 Although TylM3 shows significant similarity to cytochrome P450 family, it lacks the heme-binding sites. The conservation of amino acid sequence is confined primarily to the C-terminal half of the protein. {ECO:0000305}. degenerate-domain Q9L4U5 AknT Streptomyces galilaeus 33899 Protein AknT Although AknT shows significant similarity to cytochrome P450 family, it lacks the heme-binding sites. The conservation of amino acid sequence is confined primarily to the C-terminal half of the protein. {ECO:0000305}. degenerate-domain B1VS45 Streptomyces griseus subsp. griseus (strain JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235) 455632 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain E0D204 gfsC Streptomyces halstedii 1944 Polyketide synthase GfsC (EC 2.3.1.-) (FD-891 synthase GfsC, module 8) Lacks conserved residue(s) required for the propagation of feature annotation. {ECO:0000255|PROSITE-ProRule:PRU01363}. degenerate-domain Q54823 dnrQ Streptomyces peucetius 1950 Anthracycline biosynthesis protein DnrQ Although DnrQ shows significant similarity to cytochrome P450 family, it lacks the heme-binding sites. The conservation of amino acid sequence is confined primarily to the C-terminal half of the protein. {ECO:0000305}. degenerate-domain Q9ZGH8 desVIII Streptomyces venezuelae 54571 Protein DesVIII (Inactive cytochrome DesVIII) Although DesVIII shows significant similarity to cytochrome P450 family, it lacks the heme-binding sites. The conservation of amino acid sequence is confined primarily to the C-terminal half of the protein. {ECO:0000305}. degenerate-domain Q7YNI0 psbN Suaeda aralocaspica (Seablite) (Borszczowia aralocaspica) 224144 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7YNT5 psbN Suaeda maritima (Annual sea blite) (Suaeda spicata) 126913 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q29411 CHI3L1 Sus scrofa (Pig) 9823 Chitinase-3-like protein 1 (38 kDa heparin-binding glycoprotein) (Signal-processing protein) (gp38k) Although it belongs to the glycosyl hydrolase 18 family, Leu-140 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity. {ECO:0000305}. degenerate-domain O19112 CILP Sus scrofa (Pig) 9823 Cartilage intermediate layer protein 1 (CILP-1) [Cleaved into: Cartilage intermediate layer protein 1 C2] Was originally (PubMed:9332376, PubMed:7860751) thought to constitute the ATP pyrophosphatase enzyme (NTPPH). However, it was later shown that it is probably not the case. {ECO:0000305}. degenerate-domain A7TX81 COPS6 Sus scrofa (Pig) 9823 COP9 signalosome complex subunit 6 (SGN6) (Signalosome subunit 6) Although related to the peptidase M67A family, it lacks the JAMM motif that probably constitutes the catalytic center and therefore it probably does not have a protease activity. {ECO:0000305}. degenerate-domain P50828 HPX Sus scrofa (Pig) 9823 Hemopexin (Hyaluronidase) (EC 3.2.1.35) Lacks the conserved His heme iron ligand in position 81. There is a Gln in this position. {ECO:0000305}. degenerate-domain F1RRV3 TG Sus scrofa (Pig) 9823 Thyroglobulin The cholinesterase-like (ChEL) region lacks the Ser residue of the catalytic triad suggesting that it has no esterase activity. {ECO:0000305}. degenerate-domain Q68Y56 TLR4 Sus scrofa (Pig) 9823 Toll-like receptor 4 (CD antigen CD284) In some plant proteins and in human SARM1, the TIR domain has NAD(+) hydrolase (NADase) activity (By similarity). However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity). Based on this, it is unlikely that Toll-like receptors have NADase activity. {ECO:0000250|UniProtKB:O00206, ECO:0000305}. degenerate-domain Q31RR3 psbN Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2) 1140 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q5N2J1 psbN Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) 269084 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q0IDC9 psbN Synechococcus sp. (strain CC9311) 64471 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q3AMZ4 psbN Synechococcus sp. (strain CC9605) 110662 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q3AUQ9 psbN Synechococcus sp. (strain CC9902) 316279 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q2JLQ9 psbN Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) 321332 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q2JUV5 psbN Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime) 321327 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A5GWI1 psbN Synechococcus sp. (strain RCC307) 316278 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A5GIH3 psbN Synechococcus sp. (strain WH7803) 32051 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P26286 psbN Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) 1111708 Protein PsbN Originally thought to be a component of PSII; based on experiments in this organism, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293, ECO:0000269|PubMed:8431425}. degenerate-domain Q5NU13 mkrn2 Takifugu rubripes (Japanese pufferfish) (Fugu rubripes) 31033 E3 ubiquitin-protein ligase makorin-2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase makorin-2) Although the makorin-type Cys-His region lacks the final His residue, the following Asp residue may be able to coordinate Zn(2+). {ECO:0000305}. degenerate-domain B6Q972 ecm14 Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) (Penicillium marneffei) 441960 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 493 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain B8M2K0 ecm14 Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum) 441959 Inactive metallocarboxypeptidase ecm14 Lacks the conserved Glu residue in position 490 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain S4S1V9 Tamarindus indica (Tamarind) 58860 Chitinase-like lectin (CLL) (Chitinase-like protein) (CLP) Although it belongs to the glycosyl hydrolase 18 family, Pro-125 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity. {ECO:0000305}. degenerate-domain Q6EYC3 psbN Taxus brevifolia (Pacific yew) 46220 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7GZA5 psbN Tecticornia australasica (Australasian samphire) 224193 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q1KVV4 psbN Tetradesmus obliquus (Green alga) (Acutodesmus obliquus) 3088 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P19965 Tetronarce californica (Pacific electric ray) (Torpedo californica) 7787 SITS-binding protein (SP105) Although related to the glycosyl hydrolase 31 family, lacks the conserved active sites, suggesting it has no glycosidase activity. {ECO:0000305}. degenerate-domain A0T0P7 psbN Thalassiosira pseudonana (Marine diatom) (Cyclotella nana) 35128 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q47KW7 Thermobifida fusca (strain YX) 269800 Ferric nitrobindin-like protein Lacks the conserved His residue that binds heme iron in the nitrobindin family. {ECO:0000305}. degenerate-domain Q9HLX6 Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) 273075 Putative lon protease homolog (EC 3.4.21.-) (ATP-dependent protease La homolog) Lacks the conserved Ser-Lys catalytic dyad essential for proteolytic activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain P58275 Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) 273116 Putative lon protease homolog (EC 3.4.21.-) (ATP-dependent protease La homolog) Lacks the conserved Ser-Lys catalytic dyad essential for proteolytic activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q8DJ42 psbN Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1) 197221 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in this organism and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293, ECO:0000269|PubMed:19219048}. degenerate-domain Q9X1E1 rex2 Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) 243274 Redox-sensing transcriptional repressor Rex 2 This protein lacks the conserved Gly residues in positions 90 and 93 that are potentially involved in NAD(H) binding. They are replaced by an Asn and an Ala, respectively. {ECO:0000305}. degenerate-domain P96134 argF Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) 262724 Ornithine carbamoyltransferase (OTC) (OTCase) (EC 2.1.3.3) Lacks the conserved threonine residue in position 57, which is part of the carbamoylphosphate binding site; it is replaced by a leucine residue (PMIS:9346304). {ECO:0000305}. degenerate-domain Q6EYB9 psbN Thuja plicata (Western red-cedar) (Giant arborvitae) 3316 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain A0A7J6KD88 BPK1 Toxoplasma gondii 5811 Bradyzoite pseudokinase 1 (Inactive serine/threonine-protein kinase BPK1) Although it belongs to the protein kinase superfamily, lacks the active site residue Asp at position 227 and the Asp residue at position 245 involved in Mg(2+) chelation, suggesting that it has no protein kinase activity. {ECO:0000305|PubMed:30850550}. degenerate-domain Q5Y808 ROP4 Toxoplasma gondii 5811 Rhoptry protein 4 Lacks the active site residue so is predicted to be catalytically inactive. {ECO:0000269|PubMed:15470260}. degenerate-domain O74631 FDD123 Trametes versicolor (White-rot fungus) (Coriolus versicolor) 5325 Protein FDD123 (CvHSP30/1) Lacks the conserved Lys residue in position 228 required for covalent retinal binding. {ECO:0000305}. degenerate-domain O83759 nadE Treponema pallidum (strain DSM 117211 / Nichols) 243276 Putative glutamine-dependent NAD(+) synthetase (EC 6.3.5.1) (NAD(+) synthase [glutamine-hydrolyzing]) Lacks the conserved active sites for the glutaminase activity. {ECO:0000305}. degenerate-domain Q110N4 psbN Trichodesmium erythraeum (strain IMS101) 203124 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain D4DIW7 ECM14 Trichophyton verrucosum (strain HKI 0517) 663202 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 512 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q3M4N7 psbN Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) 240292 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P49515 psbN Trieres chinensis (Marine centric diatom) (Odontella sinensis) 1514140 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain P0C6B6 Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops albolabris) 8765 Zinc metalloproteinase homolog-disintegrin albolatin The metalloproteinase domain lacks the active site. {ECO:0000305}. degenerate-domain Q8AY82 Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri) 39682 Snake venom serine protease homolog 1 (Serine proteinase-like protein 1) Lacks the conserved His at position 67, which is expected to be an active site residue. {ECO:0000305}. degenerate-domain Q71QI0 Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri) 39682 Snake venom serine protease homolog KN7 (Serine proteinase-like protein KN7) Lacks the conserved His at position 67, which is expected to be an active site residue. {ECO:0000305}. degenerate-domain Q71QJ4 Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri) 39682 Snake venom serine protease homolog KN4 (Serine proteinase-like protein KN4) Lacks the conserved His at position 67, which is expected to be an active site residue. {ECO:0000305}. degenerate-domain P68855 psbN Triticum aestivum (Wheat) 4565 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q7J185 psbN Trochodendron aralioides (Wheel tree) 4407 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q4GZD1 DHSp Trypanosoma brucei brucei (strain 927/4 GUTat10.1) 185431 Deoxyhypusine synthase regulatory subunit (Inactive deoxyhypusine synthase) Lacks the conserved active site Lys, and therefore lacks catalytic activity. {ECO:0000269|PubMed:23525104}. degenerate-domain Q3ZJ27 psbN Tupiella akineta (Green alga) (Pseudendoclonium akinetum) 160070 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q67I33 psbN Typha angustifolia (Narrow leaf cattail) 59011 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q52PV9 Tyrophagus putrescentiae (Mold mite) (Acarus putrescentiae) 59818 Tubulin alpha chain (EC 3.6.5.-) (Alpha-tubulin) (allergen Tyr p 33) This protein lacks the Tyr in position 450 required for a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue; it is replaced by a Phe. {ECO:0000305}. degenerate-domain C4JEE1 ECM14 Uncinocarpus reesii (strain UAMH 1704) (Gymnoascus siglerae) 336963 Inactive metallocarboxypeptidase ECM14 Lacks the conserved Glu residue in position 490 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}. degenerate-domain Q9PQK7 pyrG Ureaplasma parvum serovar 3 (strain ATCC 700970) 273119 Putative CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase) Lacks the conserved cysteine and histidine residues potentially involved in the active site of the GAT domain. {ECO:0000305}. degenerate-domain P21116 Vaccinia virus (strain Copenhagen) (VACV) 10249 Truncated interleukin-1-binding protein (Protein B16) B16R of strain Copenhagen contains a stop codon at position 31, which disrupts the ORF. It only encodes the truncated N-terminal part of interleukin-1-binding protein, which is probably not functional. {ECO:0000305}. degenerate-domain A0A9E7V465 Vespa tropica (Greater banded hornet) (Sphex tropica) 7450 Inactive hyaluronidase VesT2b (Inactive HAase VesT2b) (Inactive HAase b) (Allergen Ves V 2b) (Venom spreading factor) (allergen Ves V 2b) Lacks the typical Glu active site in position 130 that is replaced by a Asn residue, preventing the hyaluronidase activity. {ECO:0000305|PubMed:27790249}. degenerate-domain C0HLL4 Vespa velutina (Asian yellow-legged hornet) 202808 Inactive hyaluronidase A (Inactive Hya A) (Hyase-like protein) (Inactive hyaluronoglucosaminidase A) (Vesp v 2A) Lacks the typical Glu active site in position 113 that is replaced by an Asn residue. Some catalytic activity was found but in a fraction that contained both Hyaluronidase A and Hyaluronidase B. {ECO:0000305|PubMed:31923175}. degenerate-domain Q05FZ1 Vespula germanica (German yellow jacket) (Paravespula germanica) 30212 Inactive hyaluronidase Ves g 2b (Inactive hyase Ves g 2b) (Hyase-like protein) (allergen Ves g 2b) Lacks the typical Glu active site in position 111 that is replaced by a His residue, preventing the hyaluronidase activity. {ECO:0000305}. degenerate-domain Q5D7H4 Vespula vulgaris (Yellow jacket) (Wasp) 7454 Inactive hyaluronidase B (Hya B) (Allergen Ves v 2.0201) (Hyaluronidase-like glycoprotein Ves v 2b) (Hyaluronoglucosaminidase B) (Hyase-like protein) (allergen Ves v 2b) Lacks the typical Glu active site in position 111 that is replaced by a His residue, preventing the hyaluronidase activity. {ECO:0000305}. degenerate-domain P0DJH0 angR Vibrio anguillarum (Listonella anguillarum) 55601 Anguibactin system regulator Lacks the conserved Ser at position 1000 required for covalent attachment of 4-phosphopantetheine. {ECO:0000305}. degenerate-domain Q6W4T3 angR Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum) 882102 Anguibactin system regulator Lacks the conserved Ser at position 1000 required for covalent attachment of 4-phosphopantetheine. {ECO:0000305}. degenerate-domain A5F8G9 acyP Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) 345073 Acylphosphatase (EC 3.6.1.7) (Acylphosphate phosphohydrolase) Lacks the conserved active site Arg in position 20. There is a cysteine in this position. {ECO:0000305}. degenerate-domain P96172 argF Vibrio sp. (strain 2693) 79682 Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3) Lacks the conserved threonine and leucine residues in positions 50 and 261, respectively, which are part of the carbamoylphosphate and ornithine binding sites; they are replaced by a leucine and a glutamine residue, respectively. {ECO:0000305}. degenerate-domain A0A1I9KNP0 Vipera ammodytes ammodytes (Western sand viper) 8705 Vaa serine proteinase homolog 1 (VaaSPH-1) (Enzymatically inactive serine proteinase-like protein SPH-1) (Snake venom serine protease homolog) Lacks the canonical catalytic triad. Two of the three residues necessary for catalytic activity are mutated: Asp-112 is present, while the other two are Asn-205 (instead of Ser) and Arg-67 (instead of His). As a result, the protein is not proteolytically active. {ECO:0000305|PubMed:30235482}. degenerate-domain P04084 Vipera ammodytes meridionalis (Eastern sand viper) 73841 Acidic phospholipase A2 homolog vipoxin A chain (svPLA2 homolog) (Acidic phospholipase A2 inhibitor vipoxin A chain) (Vipoxin acidic component) (VAC) (Vipoxin non-toxic component) In contrast to other phospholipases, it lacks the typical His active site (His->Gln in position 47). {ECO:0000305}.; degenerate-domain A4VBF0 Vipera nikolskii (Nikolsky's adder) (Vipera berus nikolskii) 1808362 Acidic phospholipase A2 inhibitor chain HPD-1I (svPLA2 homolog) (Heterodimeric neurotoxic phospholipases A2 acidic subunit) In contrast to other phospholipases, it lacks the typical His active site (His->Gln in position 63). {ECO:0000305}. degenerate-domain Q0ZIZ1 psbN Vitis vinifera (Grape) 29760 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8HS08 psbN Welwitschia mirabilis (Tree tumbo) (Welwitschia bainesii) 3377 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8D3B5 pheT Wigglesworthia glossinidia brevipalpis 36870 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved glutamate residue in position 469 that binds magnesium; it is replaced by a serine residue. {ECO:0000305}. degenerate-domain Q7M7Q6 speE Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes) 273121 Polyamine aminopropyltransferase (Putrescine aminopropyltransferase) (PAPT) (Spermidine synthase) (SPDS) (SPDSY) (EC 2.5.1.16) Lacks the conserved Asp active site. {ECO:0000305}. degenerate-domain Q4UVN8 gluQ Xanthomonas campestris pv. campestris (strain 8004) 314565 Glutamyl-Q tRNA(Asp) synthetase (Glu-Q-RSs) (EC 6.1.1.-) Lacks the conserved Tyr, which is one of four residues to bind the zinc atom. {ECO:0000305}. degenerate-domain Q8P8E9 gluQ Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) 190485 Glutamyl-Q tRNA(Asp) synthetase (Glu-Q-RSs) (EC 6.1.1.-) Lacks the conserved Tyr, which is one of four residues to bind the zinc atom. {ECO:0000305}. degenerate-domain Q8PJX7 gluQ Xanthomonas citri pv. citri (strain 306) 190486 Glutamyl-Q tRNA(Asp) synthetase (Glu-Q-RSs) (EC 6.1.1.-) Lacks the conserved Tyr, which is one of four residues to bind the zinc atom. {ECO:0000305}. degenerate-domain Q5GZ90 gluQ Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85) 291331 Glutamyl-Q tRNA(Asp) synthetase (Glu-Q-RSs) (EC 6.1.1.-) Lacks the conserved Tyr, which is one of four residues to bind the zinc atom. {ECO:0000305}. degenerate-domain A2IA89 Xenopsylla cheopis (Oriental rat flea) (Pulex cheopis) 163159 Acid phosphatase-like protein XcAP-1 (XcAP-1) Lacks acid phosphatase catalytic activity. {ECO:0000269|PubMed:38110569}. degenerate-domain A2IA93 Xenopsylla cheopis (Oriental rat flea) (Pulex cheopis) 163159 Acid phosphatase-like protein XcAP-2 (XcAP-2) Lacks acid phosphatase catalytic activity. {ECO:0000269|PubMed:38110569}. degenerate-domain A2IA90 Xenopsylla cheopis (Oriental rat flea) (Pulex cheopis) 163159 Acid phosphatase-like protein XcAP-3 (XcAP-3) Lacks acid phosphatase catalytic activity. {ECO:0000269|PubMed:38110569}. degenerate-domain Q6AZR2 adprhl1 Xenopus laevis (African clawed frog) 8355 Inactive ADP-ribosyltransferase arh2 (ADP-ribosylhydrolase-like protein 1) ([Protein ADP-ribosylarginine] hydrolase-like protein 1) Although it belongs to the ADP-ribosylglycohydrolase family, lacks metal-binding and substrate-binding residues, suggesting that it has no hydrolase activity. {ECO:0000305|PubMed:27217161}. degenerate-domain Q498F8 aktip-a Xenopus laevis (African clawed frog) 8355 AKT-interacting protein homolog A Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q5XGV8 aktip-b Xenopus laevis (African clawed frog) 8355 AKT-interacting protein homolog B Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q6NUC2 cops6 Xenopus laevis (African clawed frog) 8355 COP9 signalosome complex subunit 6 (Signalosome subunit 6) Although related to the peptidase M67A family, it lacks the JAMM motif that probably constitutes the catalytic center and therefore it probably does not have a protease activity. {ECO:0000305}. degenerate-domain O13022 dpysl3-a Xenopus laevis (African clawed frog) 8355 Dihydropyrimidinase-related protein 3-A (DRP-3-A) (Neural-specific protein 1) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q640K6 dpysl3-b Xenopus laevis (African clawed frog) 8355 Dihydropyrimidinase-related protein 3-B (DRP-3-B) (Collapsin response mediator protein 4) (CRMP-4) (xCRMP4) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q6INU7 frrs1 Xenopus laevis (African clawed frog) 8355 Ferric reductase 1 (EC 1.-.-.-) The cytochrome b561 domain lacks the conserved His residue that binds iron in the heme. {ECO:0000305}. degenerate-domain O57428 has-rs Xenopus laevis (African clawed frog) 8355 Hyaluronan synthase-related protein (Hyaluronan synthase-related sequence) (xHAS-rs) Probably inactive because it lacks critical residues conserved in other family members, including an Asp in the motif DSDT, which is NSDI in has-rs, and an Arg residue in the motif QXXRW, which is QQTPW in has-rs. Also inactive in the functional assays of PubMed:9442026. {ECO:0000305}. degenerate-domain B0F0H3 mkrn2 Xenopus laevis (African clawed frog) 8355 E3 ubiquitin-protein ligase makorin-2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase makorin-2) Although the makorin-type Cys-His region lacks the final His residue, the following Asp residue may be able to coordinate Zn(2+). {ECO:0000305}. degenerate-domain Q5U581 mtmr10-a Xenopus laevis (African clawed frog) 8355 Myotubularin-related protein 10-A (Inactive phosphatidylinositol 3-phosphatase 10-A) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 391 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q6NU08 mtmr10-b Xenopus laevis (African clawed frog) 8355 Myotubularin-related protein 10-B (Inactive phosphatidylinositol 3-phosphatase 10-B) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 390 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q6DJE4 nudt21 Xenopus laevis (African clawed frog) 8355 Cleavage and polyadenylation specificity factor subunit 5 (Nudix hydrolase 21) Lacks the conserved metal-binding residues in the NUDIX motif and is not expected to have hydrolase activity. {ECO:0000305}. degenerate-domain Q6DCP3 prtfdc1 Xenopus laevis (African clawed frog) 8355 Phosphoribosyltransferase domain-containing protein 1 Lacks the conserved active site Asp and is not expected to have phosphoribosyltransferase activity. {ECO:0000305}. degenerate-domain Q4KLT0 rnf217 Xenopus laevis (African clawed frog) 8355 E3 ubiquitin-protein ligase RNF217 (EC 2.3.2.31) (RING finger protein 217) Lacks the His residue in the RING-type domain 1 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q6NTN5 sbf2 Xenopus laevis (African clawed frog) 8355 Myotubularin-related protein 13 (Inactive phosphatidylinositol 3-phosphatase 13) (SET-binding factor 2) Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 1439 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. {ECO:0000305}. degenerate-domain Q9W603 supt16h Xenopus laevis (African clawed frog) 8355 FACT complex subunit SPT16 (DNA unwinding factor 140 kDa subunit) (DUF140) (Facilitates chromatin transcription complex subunit spt16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q6P4W0 abraxas2 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 BRISC complex subunit Abraxas 2 (Abraxas brother protein 1) (BRISC complex subunit Abro1) (Protein FAM175B) Although strongly related to the abraxas1 protein, lacks the C-terminal pSXXF that constitutes a specific recognition motif for the BRCT domain of brca1. {ECO:0000305}. degenerate-domain Q28IA3 aktip Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 AKT-interacting protein (Fused toes protein homolog) Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity. {ECO:0000305}. degenerate-domain Q07G98 cops6 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 COP9 signalosome complex subunit 6 (Signalosome subunit 6) Although related to the peptidase M67A family, it lacks the JAMM motif that probably constitutes the catalytic center and therefore it probably does not have a protease activity. {ECO:0000305}. degenerate-domain Q6GL72 dpysl3 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 Dihydropyrimidinase-related protein 3 (DRP-3) (Dihydropyrimidinase-like 3) Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure. {ECO:0000305}. degenerate-domain Q6GLD9 mkrn2 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 E3 ubiquitin-protein ligase makorin-2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase makorin-2) Although the makorin-type Cys-His region lacks the final His residue, the following Asp residue may be able to coordinate Zn(2+). {ECO:0000305}. degenerate-domain Q6DIV5 pamr1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 Inactive serine protease PAMR1 (Peptidase domain-containing protein associated with muscle regeneration 1) (Regeneration-associated muscle protease homolog) Although related to peptidase S1 family, lacks the conserved active Ser residue in position 667 which is replaced by a Thr, suggesting that it has no protease activity. {ECO:0000305}. degenerate-domain A4II60 prtfdc1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 Phosphoribosyltransferase domain-containing protein 1 Lacks the conserved active site Asp and is not expected to have phosphoribosyltransferase activity. {ECO:0000305}. degenerate-domain A4IIY1 rnf144a Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 Probable E3 ubiquitin-protein ligase RNF144A (EC 2.3.2.31) (RING finger protein 144A) Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family. {ECO:0000305}. degenerate-domain Q6C931 SPT16 Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) 284591 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain Q8ZDJ2 Yersinia pestis 632 Alpha-2-macroglobulin homolog Lacks the conserved thioester bond that is characteristic of the alpha-2-macroglobulins. {ECO:0000305}. degenerate-domain Q67HS2 psbN Yucca glauca (Soapweed yucca) (Yucca angustifolia) 207936 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q9MSR1 psbN Zamia furfuracea (Cardboard cycad) (Jamaican sago tree) 42329 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q8H6B1 SPT16 Zea mays (Maize) 4577 FACT complex subunit SPT16 (Facilitates chromatin transcription complex subunit SPT16) (Global transcription factor group C protein 102) Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. {ECO:0000305}. degenerate-domain P68854 psbN Zea mays (Maize) 4577 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q32RQ4 psbN Zygnema circumcarinatum (Green alga) 35869 Protein PsbN Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true. {ECO:0000255|HAMAP-Rule:MF_00293}. degenerate-domain Q5NMC3 pheT Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) 264203 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Lacks the conserved aspartate or glutamate residue in position 458 that binds magnesium; it is replaced by an alanine residue. {ECO:0000305}. possible-artifact P0CJ30 Ascaphus truei (Coastal tailed frog) 8439 Ascaphin-6 May represent an artifactually modified form of ascaphin-7 arising from hydrolysis during the purification procedure. {ECO:0000305}. possible-artifact O05516 tsaB Bacillus subtilis (strain 168) 224308 tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB) The well-known t(6)A modification appears to be a hydrolyzed artifact of natural cyclic t(6)A (ct(6)A) that occurs during the preparation and handling of tRNA in B.subtilis and many other species (PubMed:23242255). In these species, the t(6)A modification is processed further by dehydration into ct(6)A, a reaction catalyzed by TcdA. {ECO:0000305}. possible-artifact O05518 tsaD Bacillus subtilis (strain 168) 224308 tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD) (tRNA threonylcarbamoyladenosine biosynthesis protein TsaD) The well-known t(6)A modification appears to be a hydrolyzed artifact of natural cyclic t(6)A (ct(6)A) that occurs during the preparation and handling of tRNA in B.subtilis and many other species (PubMed:23242255). In these species, the t(6)A modification is processed further by dehydration into ct(6)A, a reaction catalyzed by TcdA. {ECO:0000305}. possible-artifact O05515 tsaE Bacillus subtilis (strain 168) 224308 tRNA threonylcarbamoyladenosine biosynthesis protein TsaE (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE) The well-known t(6)A modification appears to be a hydrolyzed artifact of natural cyclic t(6)A (ct(6)A) that occurs during the preparation and handling of tRNA in B.subtilis and many other species (PubMed:23242255). In these species, the t(6)A modification is processed further by dehydration into ct(6)A, a reaction catalyzed by TcdA. {ECO:0000305}. possible-artifact P39153 ywlC Bacillus subtilis (strain 168) 224308 Threonylcarbamoyl-AMP synthase (TC-AMP synthase) (EC 2.7.7.87) (L-threonylcarbamoyladenylate synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein YwlC) (tRNA threonylcarbamoyladenosine biosynthesis protein YwlC) The well-known t(6)A modification appears to be a hydrolyzed artifact of natural cyclic t(6)A (ct(6)A) that occurs during the preparation and handling of tRNA in B.subtilis and many other species (PubMed:23242255). In these species, the t(6)A modification is processed further by dehydration into ct(6)A, a reaction catalyzed by TcdA. {ECO:0000305}. possible-artifact P02698 GNGT1 Bos taurus (Bovine) 9913 Guanine nucleotide-binding protein G(T) subunit gamma-T1 (Transducin gamma chain) In PubMed:3917402 the authors propose that Cys-36 and Cys-37 are disulfide bonded because they could not be observed during peptide sequencing, but were observed after reduction by dithiothreitol and reaction with labeled iodoacetamide. The crystallographic structures do not support these cysteines being disulfide bonded. Artifactual oxidation and some other cysteine modifications might be consistent with these observations. {ECO:0000305}. possible-artifact Q02940 penA Burkholderia multivorans (strain ATCC 17616 / 249) 395019 Beta-lactamase (EC 3.5.2.6) (Penicillinase) This protein could be artifactual, it seems to contain pieces of several different proteins. {ECO:0000305|PubMed:7514860}. possible-artifact Q9U1Q0 eipr-1 Caenorhabditis elegans 6239 EARP-interacting protein 1 (Endosome-associated recycling protein-interacting protein) The subcellular location of endogenous eipr-1 could not be identified; diffuse expression of a eipr-1 construct in the cytoplasm may be an artifact due to over-expression of the construct. {ECO:0000303|PubMed:27191843}. possible-artifact Q8WQA4 exc-4 Caenorhabditis elegans 6239 Chloride intracellular channel exc-4 (Excretory canal abnormal protein 4) The structure contains a calcium molecule but it is unclear if this is an artifact of the crystallization process or if it has a physiological role in the activity regulation/formation of the channel. {ECO:0000305|PubMed:17985355}. possible-artifact P59049 OMT1 Chrysosplenium americanum (American golden saxifrage) 36749 Flavone 3'-O-methyltransferase OMT1 (EC 2.1.1.42) It is not sure whether OMT1 and OMT2 are really encoded by two different genes or if they represent cloning artifacts. {ECO:0000305}. possible-artifact Q42653 OMT2 Chrysosplenium americanum (American golden saxifrage) 36749 Flavone 3'-O-methyltransferase OMT2 (EC 2.1.1.42) It is not sure whether OMT1 and OMT2 are really encoded by two different genes or if they represent cloning artifacts. {ECO:0000305}. possible-artifact Q46444 qheDH Comamonas testosteroni (Pseudomonas testosteroni) 285 Quinohemoprotein alcohol dehydrogenase (QH-ADH) (EC 1.1.9.1) (Alcohol dehydrogenase (azurin)) (PQQ-containing alcohol dehydrogenase) (PQQ-dependent ADH) (Quinohaemoprotein ethanol dehydrogenase type I) (QH-EDHI) The oxidation form of Trp-543 is subject of controversy and could be the artifactual result of sample handling. {ECO:0000305|PubMed:11714714}. possible-artifact P34125 dgkA Dictyostelium discoideum (Social amoeba) 44689 Diacylglycerol kinase A (EC 2.7.1.107) (Myosin heavy chain kinase) (MHCK) The initially described myosin heavy chain kinase activity is probably artifactual due to numerous errors in the sequence used for characterization. {ECO:0000305|PubMed:1321427}. possible-artifact Q9VY78 Clic Drosophila melanogaster (Fruit fly) 7227 Chloride intracellular channel Clic The structure contains a calcium molecule but it is unclear if this is an artifact of the crystallization process or if it has a physiological role in the activity regulation/formation of the channel. {ECO:0000305|PubMed:17985355}. possible-artifact Q9VRJ0 Gen Drosophila melanogaster (Fruit fly) 7227 Flap endonuclease GEN (EC 3.1.-.-) (Flap structure-specific endonuclease GEN) (Xpg-like endonuclease) (DmGEN) 3' to 5' exonuclease activity reported in PubMed:15576351 is probably artifactual, due to the presence of other nucleases in the preparation. {ECO:0000305}. possible-artifact P13217 norpA Drosophila melanogaster (Fruit fly) 7227 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) (1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta) (No receptor potential A protein) (Phosphoinositide phospholipase C) (Phosphoinositide phospholipase C-beta) 3D structural studies were performed with a synthetic heptapeptide that contained Cys, corresponding to position 1094, therefore the detected disulfide bridge is an artifact. {ECO:0000305|PubMed:11500369}. possible-artifact P69168 III Enterobacteria phage M13 (Bacteriophage M13) 1977402 Attachment protein G3P (Gene 3 protein) (G3P) (Minor coat protein) (pIII) The oxidation form of Trp-39 is subject of controversy and could be the artifactual result of sample handling. {ECO:0000305|PubMed:9461080}. possible-artifact O46512 CYP19A1 Equus caballus (Horse) 9796 Aromatase (EC 1.14.14.14) (CYPXIX) (Cytochrome P-450AROM) (Cytochrome P450 17-alpha) (Cytochrome P450 19A1) (Estrogen synthase) Clone A1 form may be a splice variant or an artifact. {ECO:0000305}. possible-artifact P31658 hchA Escherichia coli (strain K12) 83333 Protein/nucleic acid deglycase 1 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Glyoxalase III) (EC 4.2.1.130) (Holding molecular chaperone) (Hsp31) (Maillard deglycase) The protein deglycation activity has been ascribed to a TRIS buffer artifact by a publication (PubMed:27903648), which has then been rebutted by clear biochemical experiments showing that DJ-1 family deglycases are bona fide deglycases (PubMed:28013050). Deglycase activity is further strengthened by a novel article that reports nucleotide deglycation activity (PubMed:28596309). {ECO:0000305}. possible-artifact P76256 tsaB Escherichia coli (strain K12) 83333 tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB) The well-known t(6)A modification appears to be a hydrolyzed artifact of natural cyclic t(6)A (ct(6)A) that occurs during the preparation and handling of tRNA in E.coli and many other species (PubMed:23242255). In these species, the t(6)A modification is processed further by dehydration into ct(6)A, a reaction catalyzed by TcdA. {ECO:0000305}. possible-artifact P0AF67 tsaE Escherichia coli (strain K12) 83333 tRNA threonylcarbamoyladenosine biosynthesis protein TsaE (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE) The well-known t(6)A modification appears to be a hydrolyzed artifact of natural cyclic t(6)A (ct(6)A) that occurs during the preparation and handling of tRNA in E.coli and many other species (PubMed:23242255). In these species, the t(6)A modification is processed further by dehydration into ct(6)A, a reaction catalyzed by TcdA. {ECO:0000305}. possible-artifact P45470 yhbO Escherichia coli (strain K12) 83333 Protein/nucleic acid deglycase 2 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) The protein deglycation activity has been ascribed to a TRIS buffer artifact by a publication (PubMed:27903648), which has then been rebutted by clear biochemical experiments showing that DJ-1 family deglycases are bona fide deglycases (PubMed:28013050). Deglycase activity is even strengthened by a novel article that reports nucleotide deglycation activity (PubMed:28596309). {ECO:0000305}. possible-artifact P84848 Halochromatium salexigens (Chromatium salexigens) 49447 Green heme protein (GHP) Oxidation of Cys-43 to form cysteic acid is most probably an artifact generated during sample preparation. {ECO:0000305|PubMed:16817906}. possible-artifact P01024 C3 Homo sapiens (Human) 9606 Complement C3 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b (Complement C3b-alpha' chain); Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2] An article reported the interaction surface between C3 and CR2 (PubMed:11387479). According to a another paper, it is however an artifact and can be ascribed to the presence of zinc acetate in the buffer (PubMed:21527715). {ECO:0000269|PubMed:11387479, ECO:0000269|PubMed:21527715}.; possible-artifact Q9BXS0 COL25A1 Homo sapiens (Human) 9606 Collagen alpha-1(XXV) chain (Alzheimer disease amyloid-associated protein) (AMY) (CLAC-P) [Cleaved into: Collagen-like Alzheimer amyloid plaque component (CLAC)] The pyrrolidone carboxylic acid reported in PubMed:11927537 probably formed artifactually from Glu-113 during the extraction procedure in 70% formic acid. In PubMed:15522881, the protein was found to have unblocked Glu at the N-terminus. {ECO:0000305}. possible-artifact P17302 GJA1 Homo sapiens (Human) 9606 Gap junction alpha-1 protein (Connexin-43) (Cx43) (Gap junction 43 kDa heart protein) PubMed:7715640 reported a mutation Pro-364 linked to congenital heart diseases. PubMed:8873667 later shown that it is an artifact. {ECO:0000305}.; possible-artifact P68871 HBB Homo sapiens (Human) 9606 Hemoglobin subunit beta (Beta-globin) (Hemoglobin beta chain) [Cleaved into: LVV-hemorphin-7; Spinorphin] The modification form of Leu-142 is subject of controversy and could be the artifactual result of sample handling. {ECO:0000305|PubMed:1520632}.; possible-artifact P69891 HBG1 Homo sapiens (Human) 9606 Hemoglobin subunit gamma-1 (Gamma-1-globin) (Hb F Agamma) (Hemoglobin gamma-1 chain) (Hemoglobin gamma-A chain) The modification form of Leu-142 is subject of controversy and could be the artifactual result of sample handling. {ECO:0000305|PubMed:7690768}. possible-artifact Q9Y5S8 NOX1 Homo sapiens (Human) 9606 NADPH oxidase 1 (NOX-1) (EC 1.6.3.-) (Mitogenic oxidase 1) (MOX-1) (NADH/NADPH mitogenic oxidase subunit P65-MOX) (NOH-1) An isoform named NOH-1S resulting from alternative splicing was first described as a voltage-gated proton channel that mediates the H(+) currents (PubMed:10615049). However later studies showed that this isoform was an artifact most likely due to a stable loop formation of the NOX1 mRNA (Ref.3). {ECO:0000269|PubMed:10615049, ECO:0000269|Ref.3}. possible-artifact Q8WUF5 PPP1R13L Homo sapiens (Human) 9606 RelA-associated inhibitor (Inhibitor of ASPP protein) (Protein iASPP) (NFkB-interacting protein 1) (PPP1R13B-like protein) An alternative product iASPP(RAI) has been described (PubMed:10336463, PubMed:15489900). However, it is not detected in vivo and is most probably a cloning artifact (PubMed:15489900). {ECO:0000269|PubMed:10336463, ECO:0000269|PubMed:15489900}. possible-artifact P80090 Lymnaea stagnalis (Great pond snail) (Helix stagnalis) 6523 Molluscan insulin-related peptide 3 (MIP III) [Cleaved into: Molluscan insulin-related peptide 3 B chain; Molluscan insulin-related peptide 3 A chain] PubMed:1572366 reported the formation of pyroglutamic acid by the N-terminal glutamic acid and of gamma-ethyl glutamate in peptide A. This is most probably an artifact of isolation. {ECO:0000305}. possible-artifact P27467 Wnt3a Mus musculus (Mouse) 10090 Protein Wnt-3a The formation of disulfide-linked oligomers may be an artifact that occurs upon heterologous expression in vitro (PubMed:25771893, PubMed:26902720). Formation of disulfide-linked oligomers is not observed when the protein is coexpressed with AFM (PubMed:26902720). {ECO:0000269|PubMed:25771893, ECO:0000269|PubMed:26902720}.; possible-artifact P85128 Oldenlandia affinis (Blue diamond flower) (Hedyotis affinis) 60225 Kalata-B10 The oxidation form of Trp-24 is subject of controversy and could be the artifactual result of sample handling. {ECO:0000305|PubMed:17534989}. possible-artifact P56254 OAK1 Oldenlandia affinis (Blue diamond flower) (Hedyotis affinis) 60225 Kalata-B1 The oxidation forms of Trp-111 are subject of controversy and could be the artifactual results of sample handling. {ECO:0000305|PubMed:17534989}. possible-artifact P58454 OAK4 Oldenlandia affinis (Blue diamond flower) (Hedyotis affinis) 60225 Kalata-B2 The oxidation forms of Trp-89, Trp-143 and Trp-197 are subject of controversy and could be the artifactual results of sample handling. {ECO:0000305|PubMed:17534989}. possible-artifact P36885 Periplaneta americana (American cockroach) (Blatta americana) 6978 Sulfakinin-1 (PerAm-SK-1) (Perisulfakinin) (Pea-SK-I) PubMed:10406966 reported, in addition to the presence of glutamate methyl ester, the partial formation of pyroglutamic acid by the N-terminal glutamic acid. These are most probably artifacts of isolation. {ECO:0000305}. possible-artifact P0A182 qhnDH Pseudomonas putida (Arthrobacter siderocapsulatus) 303 Quinohemoprotein amine dehydrogenase subunit gamma (QH-AmDH) (EC 1.4.9.-) (Quinohemoprotein amine dehydrogenase 9 kDa subunit) (Quinohemoprotein amine dehydrogenase catalytic subunit) The oxidation form of Met-30 is subject of controversy and could be the artifactual result of sample handling. {ECO:0000305|PubMed:11555656}. possible-artifact P08945 Ranoidea aurea (Green and golden bell frog) (Litoria aurea) 8371 Litorin PubMed:908397 reported the formation of a glutamate methyl ester from Gln-2. This is most probably an artifact of isolation. {ECO:0000305}. possible-artifact P04710 AAC1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 ADP/ATP translocase 1 (ADP,ATP carrier protein 1) (Adenine nucleotide translocator 1) (ANT 1) Was suggested to function as a homodimer (PubMed:12740376), however subsequent studies reported that this carrier exists in a monomeric state and that dimer formation is an artifact of experimental conditions. {ECO:0000269|PubMed:12740376}. possible-artifact P18238 AAC3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 ADP/ATP translocase 3 (ADP,ATP carrier protein 3) (Adenine nucleotide translocator 3) (ANT 3) Was suggested to function as a homodimer, however subsequent studies reported that this carrier exists in a monomeric state and that dimer formation is an artifact of experimental conditions (PubMed:12893834, PubMed:20152151, PubMed:23744064). {ECO:0000269|PubMed:12893834, ECO:0000269|PubMed:20152151, ECO:0000269|PubMed:23744064}. possible-artifact P18239 PET9 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 ADP/ATP translocase 2 (ADP,ATP carrier protein 2) (Adenine nucleotide translocator 2) (ANT 2) (Petite colonies protein 9) Was suggested to function as a homodimer, however subsequent studies reported that this carrier exists in a monomeric state and that dimer formation is an artifact of experimental conditions (PubMed:17056710, PubMed:17572439, PubMed:17566106). {ECO:0000269|PubMed:17056710, ECO:0000269|PubMed:17566106, ECO:0000269|PubMed:17572439}. possible-artifact Q10154 rtf2 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Splicing factor rtf2 PubMed:19416828 concluded that rtf2 mediates replication termination at the site-specific replication barrier RTS1 and interacts with pcn1/PCNA, however PubMed:37615341 reports that this function occurs downstream of rtf2, and that the interaction may be an artifact from overexpression. {ECO:0000269|PubMed:19416828, ECO:0000269|PubMed:37615341}. possible-artifact P06003 psbC Spinacia oleracea (Spinach) 3562 Photosystem II CP43 reaction center protein (PSII 43 kDa protein) (Photosystem II 44 kDa chlorophyll apoprotein) (Protein CP-43) The oxidation form of Trp-365 is subject of controversy and could be the artifactual result of sample handling. {ECO:0000305|PubMed:12417747}. possible-artifact P00752 Sus scrofa (Pig) 9823 Glandular kallikrein (EC 3.4.21.35) (Tissue kallikrein) Native porcine kallikrein is a monomer. Chains of the pancreatic beta-kallikrein are heterogeneous artifacts of proteolytic degradation during isolation. {ECO:0000305}. possible-artifact Q9GLG4 CHGB Sus scrofa (Pig) 9823 Secretogranin-1 (Chromogranin-B) (CgB) (Secretogranin I) (SgI) [Cleaved into: PE-11; Peptide SR-17; Peptide HQ-34; Peptide KR-11; CCB peptide] PubMed:11168356 reported the oxidation of Met-651 to sulfoxide. This is most probably an artifact of isolation. {ECO:0000305}. possible-artifact P03974 VCP Sus scrofa (Pig) 9823 Transitional endoplasmic reticulum ATPase (TER ATPase) (EC 3.6.4.6) (15S Mg(2+)-ATPase p97 subunit) (Valosin-containing protein) (VCP) Valosin is an artifact of purification procedure, generated in vitro by cleavage of the whole protein upon acid extraction of tissues. {ECO:0000305}. possible-artifact P40626 Tetrahymena thermophila 5911 High mobility group protein B (Non-histone chromosomal protein LG-2) It is not sure if the block at the amino end is natural or artifactual. {ECO:0000305}. possible-artifact P84254 Wheat yellow head virus (WYHV) 299385 Nucleoprotein (Coat protein) (CP) (Nucleocapsid protein) (Protein N) (Protein pc3) This protein is few amino acids shorter in its N-terminus than to all other tenuiviruses. It has been described as N-acetylated unlike all other negative stranded virus nucleoproteins. Since no genome sequence is available for this virus, the N-acetylmethionine may be an artifact of protein sequencing. {ECO:0000305}. reclassified-function P10569 MIC Acanthamoeba castellanii (Amoeba) 5755 Myosin IC heavy chain Was originally thought to be myosin IB. {ECO:0000305}. reclassified-function B0C142 dapA Acaryochloris marina (strain MBIC 11017) 329726 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B0CE31 dapB Acaryochloris marina (strain MBIC 11017) 329726 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3DE17 dapA Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) 203119 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P54008 Achlya ambisexualis (Water mold) 4768 RNA cytidine acetyltransferase (EC 2.3.1.-) (18S rRNA cytosine acetyltransferase) Was originally thought to be a steroid receptor on the basis of non-significant sequence similarities. {ECO:0000305|PubMed:1689271}. reclassified-function A9NGC2 dapA Acholeplasma laidlawii (strain PG-8A) 441768 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7ZAG8 sqr Acidianus ambivalens (Desulfurolobus ambivalens) 2283 Sulfide-quinone reductase (SQR) (EC 1.8.5.4) (Sulfide:quinone oxidoreductase) Was originally identified as FMN-containing NADH dehydrogenase (PubMed:12417325), based on the NADH oxidase activity of the C-terminally truncated protein. Was then shown to function as sulfide:quinone reductase. The full-length protein does not have NADH oxidase activity (PubMed:19438211). {ECO:0000269|PubMed:19438211, ECO:0000305}. reclassified-function A5FZS7 dapA Acidiphilium cryptum (strain JF-5) 349163 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5FXD9 dapB Acidiphilium cryptum (strain JF-5) 349163 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7J6C4 dapA Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)) 243159 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B5ELM5 dapA Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31) (Leptospirillum ferrooxidans (ATCC 53993)) 380394 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C1F658 dapA Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB 13165 / 161) 240015 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0LV15 dapA Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) 351607 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B9MER6 dapA Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)) 535289 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1W4S3 dapA Acidovorax sp. (strain JS42) 232721 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B7I2B0 dapB Acinetobacter baumannii (strain AB0057) 480119 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7GV10 dapB Acinetobacter baumannii (strain AB307-0294) 557600 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2I2G4 dapB Acinetobacter baumannii (strain ACICU) 405416 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3MA87 dapB Acinetobacter baumannii (strain ATCC 17978 / DSM 105126 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377) 400667 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0VA26 dapB Acinetobacter baumannii (strain AYE) 509173 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0VPZ8 dapB Acinetobacter baumannii (strain SDF) 509170 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P07774 catM Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) 62977 HTH-type transcriptional regulator CatM (Cat operon transcriptional regulator) Was originally (PubMed:2793826) reported to be a transcriptional repressor of cat genes. However, further investigations have shown it to be a transcriptional activator. {ECO:0000305|PubMed:2793826}. reclassified-function Q6F6R2 dapB Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) 62977 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0BPI4 dapA Actinobacillus pleuropneumoniae serotype 3 (strain JL03) 434271 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B0BNW4 dapB Actinobacillus pleuropneumoniae serotype 3 (strain JL03) 434271 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3N0Q9 dapA Actinobacillus pleuropneumoniae serotype 5b (strain L20) 416269 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A3N048 dapB Actinobacillus pleuropneumoniae serotype 5b (strain L20) 416269 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B3GXP5 dapA Actinobacillus pleuropneumoniae serotype 7 (strain AP76) 537457 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B3H1A7 dapB Actinobacillus pleuropneumoniae serotype 7 (strain AP76) 537457 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6VPE4 dapB Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z) 339671 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P02592 Aequorea victoria (Water jellyfish) (Mesonema victoria) 6100 Aequorin-2 Was originally thought to have an internal disulfide bond. {ECO:0000305|PubMed:8405461}. reclassified-function P07164 Aequorea victoria (Water jellyfish) (Mesonema victoria) 6100 Aequorin-1 Was originally thought to have an internal disulfide bond. {ECO:0000305|PubMed:8405461}. reclassified-function P09166 aerA Aeromonas enteropelogenes (Aeromonas trota) 29489 Aerolysin Was originally thought to originate from A.sobria. {ECO:0000305}. reclassified-function A4SLF8 dapB Aeromonas salmonicida (strain A449) 382245 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B6JGA4 dapA Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5) (Oligotropha carboxidovorans) 504832 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B6JCI8 dapB Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5) (Oligotropha carboxidovorans) 504832 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O52727 lolB Aggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans) 714 Outer-membrane lipoprotein LolB Was originally thought to be involved in delta-aminolevulinic acid biosynthesis. {ECO:0000305}. reclassified-function Q8UGL3 dapA Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) 176299 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) The DapA family was originally thought to be dihydrodipicolinate synthases (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. This enzyme is still named DHDPS in PubMed:22949190 and PubMed:24677246, but since DHDPS is considered as a misleading name, it was not used in this entry. {ECO:0000305}. reclassified-function Q8UIV8 dapB Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) 176299 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2UMF1 dapB Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) 349741 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q21WN2 dapA Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Rhodoferax ferrireducens) 338969 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q0VRH4 dapA Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2) 393595 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8ET60 dapA Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri) 367737 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8EWI3 dapB Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri) 367737 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5E3I3 dapA Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri) 312309 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5E7N0 dapB Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri) 312309 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B5FGX4 dapA Aliivibrio fischeri (strain MJ11) (Vibrio fischeri) 388396 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B5FA64 dapB Aliivibrio fischeri (strain MJ11) (Vibrio fischeri) 388396 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B6EJT2 dapA Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) 316275 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B6ENC8 dapB Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) 316275 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0A5S1 dapA Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1) 187272 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q0A7E5 dapB Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1) 187272 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6TT16 dapB Alkaliphilus metalliredigens (strain QYMF) 293826 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8MF40 dapA Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) 350688 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8MF41 dapB Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) 350688 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B9JYQ3 dapB Allorhizobium ampelinum (strain ATCC BAA-846 / DSM 112012 / S4) (Agrobacterium vitis (strain S4)) 311402 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O94095 ALTA2 Alternaria alternata (Alternaria rot fungus) (Torula alternata) 5599 Allergen Alt a 2 (allergen Alt a 2) Was originally (PubMed:10482844) identified to be a major allergen, but a second study (PubMed:15940136) reported a very low prevalence. {ECO:0000305|PubMed:10482844, ECO:0000305|PubMed:15940136}. reclassified-function Q2IGX5 dapA Anaeromyxobacter dehalogenans (strain 2CP-C) 290397 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2IGX0 dapB Anaeromyxobacter dehalogenans (strain 2CP-C) 290397 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8JAN5 dapA Anaeromyxobacter dehalogenans (strain ATCC BAA-258 / DSM 21875 / 2CP-1) 455488 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8JAN4 dapB Anaeromyxobacter dehalogenans (strain ATCC BAA-258 / DSM 21875 / 2CP-1) 455488 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7H773 dapA Anaeromyxobacter sp. (strain Fw109-5) 404589 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7H774 dapB Anaeromyxobacter sp. (strain Fw109-5) 404589 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B4UHY1 dapA Anaeromyxobacter sp. (strain K) 447217 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B4UHF2 dapB Anaeromyxobacter sp. (strain K) 447217 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B9KI57 dapA Anaplasma marginale (strain Florida) 320483 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5PB64 dapA Anaplasma marginale (strain St. Maries) 234826 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5PA93 dapB Anaplasma marginale (strain St. Maries) 234826 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O61470 Dox-A2 Anopheles gambiae (African malaria mosquito) 7165 Probable 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome subunit S3) (26S proteasome regulatory subunit RPN3) (Diphenol oxidase A2 component) (DOX-A2) Was originally thought to be the diphenol oxidase A2 component involved in catecholamine metabolism, melanin formation, and sclerotization of the cuticle. {ECO:0000305|PubMed:9988317}. reclassified-function Q9U5Z8 DOXA2 Anopheles stephensi (Indo-Pakistan malaria mosquito) 30069 Probable 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome subunit S3) (26S proteasome regulatory subunit RPN3) (Diphenol oxidase A2 component) (DOX-A2) Was originally thought to be the diphenol oxidase A2 component involved in catecholamine metabolism, melanin formation and sclerotization of the cuticle. {ECO:0000305|PubMed:10835480}. reclassified-function P90680 BLOP Apis mellifera (Honeybee) 7460 Opsin, blue-sensitive (Blue-sensitive opsin) (AmBLop) Was originally thought to be the ultraviolet sensitive opsin. {ECO:0000305|PubMed:9057845}. reclassified-function P07712 Aplysia californica (California sea hare) 6500 Abdominal ganglion neuropeptides L5-67 [Cleaved into: Luqin; Luqin-B; Luqin-C; Proline-rich mature peptide (PRMP)] Was previously thought to be expressed in L5. {ECO:0000305}. reclassified-function O67216 dapA Aquifex aeolicus (strain VF5) 224324 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function O67061 dapB Aquifex aeolicus (strain VF5) 224324 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9LTV6 Arabidopsis thaliana (Mouse-ear cress) 3702 Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing] (EC 1.3.1.124) Was originally assigned as At3g12790. {ECO:0000305}. reclassified-function Q9ZUY3 ADT3 Arabidopsis thaliana (Mouse-ear cress) 3702 Arogenate dehydratase 3, chloroplastic (AtADT3) (EC 4.2.1.91) (Prephenate dehydratase 1) (AtPDT1) Was reported to be a cytosolic prephenate dehydratase interacting with a G protein alpha-subunit. {ECO:0000305|PubMed:16415218}. reclassified-function Q9SCX5 AKT5 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable potassium channel AKT5 Was originally erroneously termed AKT6. {ECO:0000305|PubMed:10852932}. reclassified-function Q8GXE6 AKT6 Arabidopsis thaliana (Mouse-ear cress) 3702 Potassium channel AKT6 (Potassium channel SPIK) (Shaker pollen inward rectifier K(+) channel) Was originally erroneously termed AKT5. {ECO:0000305|PubMed:10852932}. reclassified-function Q9FYL3 ALB4 Arabidopsis thaliana (Mouse-ear cress) 3702 ALBINO3-like protein 1, chloroplastic (Arabidopsis thaliana envelope membrane integrase) (Protein ALBINA 4) (Ath4) (Protein ARTEMIS) (Suppressor of tic40 protein 1) Was originally thought to be the product of one gene (ARTEMIS) that in fact corresponds to two separate genes At1g24485 and At1g24490. {ECO:0000305|PubMed:12169665}. reclassified-function O23702 AN Arabidopsis thaliana (Mouse-ear cress) 3702 C-terminal binding protein AN (CtBP) (Protein ANGUSTIFOLIA) (Protein DETORQUEO) Was initially thought to function as a transcriptional corepressor. {ECO:0000305|PubMed:11889033}. reclassified-function Q94JM3 ARF2 Arabidopsis thaliana (Mouse-ear cress) 3702 Auxin response factor 2 (ARF1-binding protein) (ARF1-BP) (Protein MEGAINTEGUMENTA) Was originally erroneously termed IAA26 and IAA30 (Ref.5). {ECO:0000305|Ref.5}. reclassified-function Q0WTI8 ATJ72 Arabidopsis thaliana (Mouse-ear cress) 3702 Chaperone protein dnaJ 72 (AtDjC72) (AtJ72) Was originally erroneously termed LCR51 before the split of the gene model. {ECO:0000305}. reclassified-function Q8LBA0 ATL24 Arabidopsis thaliana (Mouse-ear cress) 3702 NEP1-interacting protein-like 2 (RING-H2 finger protein ATL24) Was originally (PubMed:16557337) assigned as a member of the E3 ubiquitin-protein ligase ATL subfamily but does not display E3 catalytic activity (PubMed:16339806). {ECO:0000305|PubMed:16339806, ECO:0000305|PubMed:16557337}. reclassified-function Q9FKX5 ATL27 Arabidopsis thaliana (Mouse-ear cress) 3702 NEP1-interacting protein-like 1 (RING-H2 finger protein ATL27) Was originally assigned as a member of the E3 ubiquitin-protein ligase ATL subfamily. {ECO:0000305|PubMed:16557337}. reclassified-function O22866 ATTI2 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 193 (Trypsin inhibitor ATTI-2) Was initially thought to be a protease inhibitor. {ECO:0000305|PubMed:15082560}. reclassified-function O22867 ATTI3 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 194 (Trypsin inhibitor ATTI-3) Was initially thought to be a protease inhibitor. {ECO:0000305|PubMed:15082560}. reclassified-function Q8RYE7 ATTI4 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 196 (Trypsin inhibitor ATTI-4) Was initially thought to be a protease inhibitor. {ECO:0000305|PubMed:15082560}. reclassified-function O22869 ATTI6 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 197 (Trypsin inhibitor ATTI-6) Was initially thought to be a protease inhibitor. {ECO:0000305|PubMed:15082560}. reclassified-function Q42330 ATTI7 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 192 (Trypsin inhibitor ATTI-7) Was initially thought to be a protease inhibitor. {ECO:0000305|PubMed:15082560}. reclassified-function Q9SUR6 CORI3 Arabidopsis thaliana (Mouse-ear cress) 3702 Cystine lyase CORI3 (EC 4.4.1.35) (Protein CORONATINE INDUCED 3) (Protein JASMONATE RESPONSIVE 2) CORI3 was initially isolated by Lopukhina et al (PMID:11500565) as tyrosine aminotransferase (TAT). The authors also measured a TAT activity in vitro, even though relatively weak. Jones et al (PMID:12525491) showed that CORI3 possesses cystine lyase (CL) activity, but lacks TAT activity in vitro. In addition, CL activity is not inhibited by saturation of L-tyrosine in the medium. As CORI3 should bind L-tyrosine to catalyze TAT activity, this excludes a TAT activity for CORI3. Jones et al. made the statment that TAT activity resulted probably from residual native TAT-catalyzing proteins present in the purified preparations employed by Loupokhina et al. {ECO:0000305|PubMed:11500565, ECO:0000305|PubMed:12525491}. reclassified-function P27450 CST Arabidopsis thaliana (Mouse-ear cress) 3702 Probable serine/threonine-protein kinase CST (EC 2.7.11.1) (Protein CAST AWAY) Was originally (PubMed:1851993) reported to be a connexin and to contain transmembrane domains. PubMed:8400879 authors have assigned that this is not a connexin, but rather a protein kinase. {ECO:0000305|PubMed:1851993}. reclassified-function Q8LCA1 CURT1B Arabidopsis thaliana (Mouse-ear cress) 3702 Protein CURVATURE THYLAKOID 1B, chloroplastic (Photosystem I protein P) (Thylakoid membrane phosphoprotein 14 kDa) Was previously thought to be part of the photosystem I complex. {ECO:0000305|PubMed:16109415}. reclassified-function O80574 DAPB1 Arabidopsis thaliana (Mouse-ear cress) 3702 4-hydroxy-tetrahydrodipicolinate reductase 1, chloroplastic (HTPA reductase 1) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8LB01 DAPB2 Arabidopsis thaliana (Mouse-ear cress) 3702 4-hydroxy-tetrahydrodipicolinate reductase 2, chloroplastic (HTPA reductase 2) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9LZX6 DHDPS1 Arabidopsis thaliana (Mouse-ear cress) 3702 4-hydroxy-tetrahydrodipicolinate synthase 1, chloroplastic (HTPA synthase 1) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9FVC8 DHDPS2 Arabidopsis thaliana (Mouse-ear cress) 3702 4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic (HTPA synthase 2) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P42699 DRT112 Arabidopsis thaliana (Mouse-ear cress) 3702 Plastocyanin major isoform, chloroplastic (DNA-damage-repair/toleration protein DRT112) Was originally thought to be involved in the resistance to UV light and chemical DNA-damaging agents. {ECO:0000305|PubMed:8479917}. reclassified-function Q9ZVN4 DSP1 Arabidopsis thaliana (Mouse-ear cress) 3702 Inositol diphosphatase DSP1 (EC 3.6.1.52) (Inositol pyrophosphate phosphatase DSP1) (Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 1) (AtPFA-DSP1) Was initially described as a protein tyrosine phosphatase and has phosphotyrosine phosphatase activity in vitro but is now thought to function as an inositol pyrophosphate phosphatase. {ECO:0000269|PubMed:35468885}. reclassified-function Q84MD6 DSP2 Arabidopsis thaliana (Mouse-ear cress) 3702 Inositol diphosphatase DSP2 (EC 3.6.1.52) (Inositol pyrophosphate phosphatase DSP2) (Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 2) (AtPFA-DSP2) Was initially described as a protein tyrosine phosphatase and has phosphotyrosine phosphatase activity in vitro but is now thought to function as an inositol pyrophosphate phosphatase. {ECO:0000305}. reclassified-function Q681Z2 DSP3 Arabidopsis thaliana (Mouse-ear cress) 3702 Inositol diphosphatase DSP3 (EC 3.6.1.52) (Inositol pyrophosphate phosphatase DSP3) (Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 3) (AtPFA-DSP3) Was initially described as a protein tyrosine phosphatase and has phosphotyrosine phosphatase activity in vitro but is now thought to function as an inositol pyrophosphate phosphatase. {ECO:0000305}. reclassified-function Q940L5 DSP4 Arabidopsis thaliana (Mouse-ear cress) 3702 Inositol diphosphatase DSP4 (EC 3.6.1.52) (Inositol pyrophosphate phosphatase DSP4) (Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 4) (AtPFA-DSP4) Was initially described as a protein tyrosine phosphatase and has phosphotyrosine phosphatase activity in vitro but is now thought to function as an inositol pyrophosphate phosphatase. {ECO:0000305}. reclassified-function Q9FFD7 DSP5 Arabidopsis thaliana (Mouse-ear cress) 3702 Inositol diphosphatase DSP5 (EC 3.6.1.52) (Inositol pyrophosphate phosphatase DSP5) (Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 5) (AtPFA-DSP5) Was initially described as a protein tyrosine phosphatase and has phosphotyrosine phosphatase activity in vitro but is now thought to function as an inositol pyrophosphate phosphatase. {ECO:0000305}. reclassified-function Q9FNA4 ELP1 Arabidopsis thaliana (Mouse-ear cress) 3702 Elongator complex protein 1 (AtELP1) (Elongator component 1) (Protein ABA-OVERLY SENSITIVE 1) (Protein ELONGATA 2) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:O95163}. reclassified-function F4I1S7 ELP2 Arabidopsis thaliana (Mouse-ear cress) 3702 Elongator complex protein 2 (AtELP2) (Elongator component 2) (Protein GREEN NPR1 SEEDLING ON SA MEDIUM 1) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q6IA86}. reclassified-function Q9C778 ELP4 Arabidopsis thaliana (Mouse-ear cress) 3702 Elongator complex protein 4 (AtELP4) (Elongator component 4) (Protein ELONGATA 1) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}. reclassified-function F4IQJ2 ELP5 Arabidopsis thaliana (Mouse-ear cress) 3702 Elongator complex protein 5 (AtELP5) (Elongator component 5) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q8TE02}. reclassified-function Q8L9Y2 ELP6 Arabidopsis thaliana (Mouse-ear cress) 3702 Elongator complex protein 6 (AtELP6) (Elongator component 6) (UPF0405 protein ELP6) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q0PNE2}. reclassified-function Q8S8F2 FBL11 Arabidopsis thaliana (Mouse-ear cress) 3702 BTB/POZ domain-containing protein FBL11 Was originally thought to contain a F-box domain. {ECO:0000305|PubMed:11077244}. reclassified-function Q8GW72 FUC1 Arabidopsis thaliana (Mouse-ear cress) 3702 Alpha-L-fucosidase 1 (EC 3.2.1.51) (Alpha-1,3/4-fucosidase) (AtFUC1) (Alpha-L-fucoside fucohydrolase) Was reported by PubMed:11788770 to be an alpha-1,2-fucosidase. {ECO:0000305|PubMed:11788770}. reclassified-function F4IEM5 GCR2 Arabidopsis thaliana (Mouse-ear cress) 3702 LanC-like protein GCR2 (G protein-coupled receptor 2) Was originally described as a plasma membrane G protein coupled receptor (GPCR) that binds ABA. Binding of ABA to GCR2 results in the release of G protein and dissociation of the heterotrimeric complex to activate downstream ABA effectors and to trigger the ABA responses (PubMed:17347412). However, GCR2 has been controversial with respect to the reproducibility of the results (PubMed:17894782, PubMed:18714360, PubMed:19286934). Moreover, GCR2 lacks the prototypical seven transmembrane domains of GPCRs, and is homologous to mammalian lanthionine synthetase C-like (LANCL) proteins (PubMed:17991845). Intriguingly, it was shown that human granulocytes and insulin-producing rat insulinoma cells release ABA, and that LANCL2 is necessary for ABA binding and signaling in these cells (PubMed:19667068). {ECO:0000305|PubMed:17347412, ECO:0000305|PubMed:17991845}. reclassified-function Q8LGN1 GLR1.4 Arabidopsis thaliana (Mouse-ear cress) 3702 Glutamate receptor 1.4 (Ligand-gated ion channel 1.4) AAL61996 is a fragment and was originally reported as a spliced variant of AAL61995. {ECO:0000305|PubMed:12082126}. reclassified-function Q9C8L4 GLY3 Arabidopsis thaliana (Mouse-ear cress) 3702 Persulfide dioxygenase ETHE1 homolog, mitochondrial (EC 1.13.11.18) (Glyoxalase II) (Glx II) (Sulfur dioxygenase ETHE1) Was initially thought to be a glyoxalase II isozyme (PubMed:9349270), but has been shown to lack glyoxalase activity (PubMed:22786886). {ECO:0000305|PubMed:22786886, ECO:0000305|PubMed:9349270}. reclassified-function Q93ZR1 HAG3 Arabidopsis thaliana (Mouse-ear cress) 3702 Elongator complex protein 3 (AtELP3) (EC 2.3.1.311) (Elongator component 3) (Protein ELONGATA 3) (Protein ENHANCER-OF-ASYMMETRIC-LEAVES-TWO1) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function P94063 HAL3B Arabidopsis thaliana (Mouse-ear cress) 3702 Probable phosphopantothenoylcysteine decarboxylase (EC 4.1.1.36) (AtCoaC2) (Halotolerance protein Hal3b) (AtHal3b) Was previously called At1g48610. {ECO:0000305}. reclassified-function Q9LFT6 HNL Arabidopsis thaliana (Mouse-ear cress) 3702 Alpha-hydroxynitrile lyase (AtHNL) (EC 4.1.2.10) ((R)-hydroxynitrile lyase) ((R)-oxynitrilase) (Methylesterase 5) (AtMES5) Was originally thought to belong to the methylesterase (MES) family. {ECO:0000305|PubMed:19433222}. reclassified-function Q1ACB3 HST Arabidopsis thaliana (Mouse-ear cress) 3702 Homogentisate solanesyltransferase, chloroplastic (AtHST) (EC 2.5.1.117) (Homogentisate phytyltransferase 2) (AtHPT2) (Vitamin E pathway gene 2-2 protein) (AtVTE2-2) Was initially thought to have a homogentisate phytyltransferase activity and to be involved in tocopherol biosynthesis. {ECO:0000305|PubMed:16408209}. reclassified-function Q9C966 IAA15 Arabidopsis thaliana (Mouse-ear cress) 3702 Auxin-responsive protein IAA15 (Indoleacetic acid-induced protein 15) Was originally (Ref.1) erroneously named IAA21. {ECO:0000305}. reclassified-function Q8RYC6 IAA32 Arabidopsis thaliana (Mouse-ear cress) 3702 Auxin-responsive protein IAA32 (Indoleacetic acid-induced protein 32) Was originally (Ref.6) erroneously named IAA31. {ECO:0000305}. reclassified-function Q9C5X0 IAA34 Arabidopsis thaliana (Mouse-ear cress) 3702 Auxin-responsive protein IAA34 (Indoleacetic acid-induced protein 34) Was originally (Ref.1) erroneously named IAA29. {ECO:0000305}. reclassified-function Q94A20 LFG5 Arabidopsis thaliana (Mouse-ear cress) 3702 BI1-like protein (Protein LIFEGUARD 5) (AtLFG5) Was originally thought to contain a F-box domain and LRR repeats, but it lacks both types of domains. {ECO:0000305|PubMed:11077244}. reclassified-function Q8GT75 NIP1 Arabidopsis thaliana (Mouse-ear cress) 3702 NEP1-interacting protein 1 (RING-H2 finger protein ATL26) Was originally assigned as a member of the E3 ubiquitin-protein ligase ATL subfamily. {ECO:0000305|PubMed:16557337}. reclassified-function Q8GT74 NIP2 Arabidopsis thaliana (Mouse-ear cress) 3702 NEP1-interacting protein 2 (RING-H2 finger protein ATL25) Was originally assigned as a member of the E3 ubiquitin-protein ligase ATL subfamily. {ECO:0000305|PubMed:16557337}. reclassified-function Q7X9V3 NSI Arabidopsis thaliana (Mouse-ear cress) 3702 GCN5-related N-acetyltransferase 2, chloroplastic (EC 2.3.1.255) (Acetyltransferase NSI) (AtNSI) (EC 2.3.1.48) (Nuclear shuttle protein-interacting protein) (Serotonin N-acetyl transferase 1) (AtSNAT) (AtSNAT1) (EC 2.3.1.87) Was initially described as nuclear. {ECO:0000269|PubMed:12837950}. reclassified-function Q9LU85 PAP4 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable plastid-lipid-associated protein 4, chloroplastic (Fibrillin-3a) (Plastoglobulin 25) (AtPGL25) Was named previously At3g26090. {ECO:0000305}. reclassified-function Q8VYA1 PARG2 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable poly(ADP-ribose) glycohydrolase 2 (EC 3.2.1.143) Was previously assigned to At2g31870. {ECO:0000305}. reclassified-function Q1G3U6 PCO3 Arabidopsis thaliana (Mouse-ear cress) 3702 Plant cysteine oxidase 3 (AtPCO3) (EC 1.13.11.20) (NIFS-like protein 2) (NifS2) Was originally identified as a putative plastidic SufS-like protein and thus called CpNifS2. {ECO:0000303|PubMed:18978034}. reclassified-function Q39182 PDF2.2 Arabidopsis thaliana (Mouse-ear cress) 3702 Defensin-like protein 2 (Low-molecular-weight cysteine-rich protein 69) (Protein LCR69) (Plant defensin 2.2) Was initially thought (Ref.2) to be a protease inhibitor. {ECO:0000305}. reclassified-function Q9FVQ4 PLGG1 Arabidopsis thaliana (Mouse-ear cress) 3702 Plastidal glycolate/glycerate translocator 1, chloroplastic (Bacterial membrane protein LrgB-like protein) (AtLrgB) Was initially thought to be involved in chloroplast development or function against cell death (PubMed:21916894, PubMed:22180599). {ECO:0000305}. reclassified-function Q9CAH5 PPRD1 Arabidopsis thaliana (Mouse-ear cress) 3702 Polyprenal reductase 1 (EC 1.3.1.94) Was initially characterized as a polyprenol reductase, mediating the conversion of polyprenol into dolichol (PubMed:26628744). However, it was later shown to catalyze an intermediate step in this pathway and reduce polyprenal (By similarity). {ECO:0000250|UniProtKB:Q9H8P0, ECO:0000269|PubMed:26628744}. reclassified-function Q9SI62 PPRD2 Arabidopsis thaliana (Mouse-ear cress) 3702 Polyprenal reductase 2 (EC 1.3.1.94) Was initially characterized as a polyprenol reductase, mediating the conversion of polyprenol into dolichol (PubMed:26628744). However, it was later shown to catalyze an intermediate step in this pathway and reduce polyprenal (By similarity). {ECO:0000250|UniProtKB:Q9H8P0, ECO:0000269|PubMed:26628744}. reclassified-function O49347 PSBY Arabidopsis thaliana (Mouse-ear cress) 3702 Photosystem II reaction center proteins PsbY, chloroplastic (L-arginine-metabolizing enzyme) (L-AME) [Cleaved into: Photosystem II reaction center protein PsbY-1, chloroplastic (PsbY-A1); Photosystem II reaction center protein PsbY-2, chloroplastic (PsbY-A2)] Was originally thought to be a manganese-binding polypeptide with L-arginine metabolizing activity, with a possible role in the function of the CaMn4O5-cluster in oxygen-evolving PSII (PubMed:9829828). However it is not essential for PSII activity in cyanobacteria and does not furnish ligands for the CaMn4O5 cluster (By similarity). {ECO:0000250|UniProtKB:P73676, ECO:0000305|PubMed:9829828}. reclassified-function O04200 PXN Arabidopsis thaliana (Mouse-ear cress) 3702 Peroxisomal nicotinamide adenine dinucleotide carrier (Peroxisomal NAD carrier) (Peroxisomal membrane protein 38, (PMP36)) (AtPMP38) (Protein ABERRANT PEROXISOME MORPHOLOGY 3) (Solute carrier family 25 member 17) Was originally thought to be an adenine nucleotide carrier. {ECO:0000305|PubMed:11522909}. reclassified-function O48538 RBOHF Arabidopsis thaliana (Mouse-ear cress) 3702 Respiratory burst oxidase homolog protein F (EC 1.11.1.-) (EC 1.6.3.-) (Cytochrome b245 beta chain homolog RbohAp108) (NADPH oxidase RBOHF) (AtRBOHF) Was originally called RBOHA. {ECO:0000305|PubMed:9490748}. reclassified-function Q08682 RPSaA Arabidopsis thaliana (Mouse-ear cress) 3702 Small ribosomal subunit protein uS2z (40S ribosomal protein Sa-1) (Laminin receptor homolog) (p40) Was originally thought to be a laminin receptor. {ECO:0000305}. reclassified-function Q8LAS8 SFGH Arabidopsis thaliana (Mouse-ear cress) 3702 S-formylglutathione hydrolase (AtSFGH) (EC 3.1.2.12) (Esterase D) Was originally classified as an esterase D due to its apparent insensitivity to serine hydrolase inhibitors. {ECO:0000305|PubMed:11888210}. reclassified-function Q9SJW3 SPR1 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein SPIRAL1 (Protein NAP16kDa) Was originally (Ref.2) erroneously thought to be a nitrilase associated protein NAP16kDa. {ECO:0000305}. reclassified-function Q8VY05 SWI3D Arabidopsis thaliana (Mouse-ear cress) 3702 SWI/SNF complex subunit SWI3D (AtSWI3D) (Transcription regulatory protein SWI3D) Was originally incorrectly assigned as CHB4. {ECO:0000305}. reclassified-function Q9M9V9 TCTP2 Arabidopsis thaliana (Mouse-ear cress) 3702 Translationally controlled tumor protein 2 (AtTCTP2) Was initially thought to be a pseudogene. {ECO:0000269|PubMed:19060111}. reclassified-function Q41951 TIP2-1 Arabidopsis thaliana (Mouse-ear cress) 3702 Aquaporin TIP2-1 (Delta-tonoplast intrinsic protein) (Delta-TIP) (Tonoplast intrinsic protein 2-1) (AtTIP2;1) [Cleaved into: Aquaporin TIP2-1, N-terminally processed] Was originally assigned as At3g16230, which is now a completely different protein not related to aquaporins. {ECO:0000305}. reclassified-function O64511 TLP1 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein TWIN LOV 1 Was originally thought to contain a F-box domain. {ECO:0000305|PubMed:11077244}.; reclassified-function Q8LBL1 TPK1 Arabidopsis thaliana (Mouse-ear cress) 3702 Two-pore potassium channel 1 (AtTPK1) (Calcium-activated outward-rectifying potassium channel 1) (AtKCO1) Was initially described as an outward slow-vacuolar (SV) ion channel (PubMed:11821043, PubMed:9184204). {ECO:0000305}. reclassified-function Q9FZE1 UGD1 Arabidopsis thaliana (Mouse-ear cress) 3702 UDP-glucose 6-dehydrogenase 1 (UDP-Glc dehydrogenase 1) (UDP-GlcDH 1) (UDPGDH 1) (EC 1.1.1.22) (At-UGD1) Was originally assigned as UGD4. {ECO:0000305|PubMed:11554483}. reclassified-function Q9FM01 UGD4 Arabidopsis thaliana (Mouse-ear cress) 3702 UDP-glucose 6-dehydrogenase 4 (At-UGD4) (UDP-Glc dehydrogenase 4) (UDP-GlcDH 4) (UDPGDH 4) (EC 1.1.1.22) Was originally assigned as UGD1. {ECO:0000305|PubMed:11554483}. reclassified-function Q9ZQ95 UGT73C6 Arabidopsis thaliana (Mouse-ear cress) 3702 UDP-glycosyltransferase 73C6 (EC 2.4.1.-) (Flavonol-3-O-glycoside-7-O-glucosyltransferase 1) (Zeatin O-glucosyltransferase 2) Was originally (Ref.1) thought to be a zeatin O-glucosyltransferases and was named ZOG2. {ECO:0000305}. reclassified-function O64758 VSR5 Arabidopsis thaliana (Mouse-ear cress) 3702 Vacuolar-sorting receptor 5 (AtVSR5) (BP80-like protein e) (AtBP80e) (Epidermal growth factor receptor-like protein 5) (AtELP5) Was originally erroneously termed BP80D. {ECO:0000305|PubMed:12493849}. reclassified-function Q9FYH7 VSR6 Arabidopsis thaliana (Mouse-ear cress) 3702 Vacuolar-sorting receptor 6 (AtVSR6) (BP80-like protein d) (AtBP80d) (Epidermal growth factor receptor-like protein 6) (AtELP6) Was originally erroneously termed BP80E. {ECO:0000305|PubMed:12493849}. reclassified-function Q9SZY8 YUC1 Arabidopsis thaliana (Mouse-ear cress) 3702 Probable indole-3-pyruvate monooxygenase YUCCA1 (EC 1.14.13.168) (Flavin-containing monooxygenase YUCCA1) Was initially (PubMed:11209081) thought to be involved in the tryptamine pathway for the biosynthesis of indole-3-acetic acid (IAA), but it has been shown (PubMed:20974893) that this is not the case. It is now admitted (PubMed:22025724, PubMed:22108406) that the YUCCA family is implicated in the conversion of indole-3-pyruvic acid (IPA) to indole-3-acetic acid (IAA). {ECO:0000305|PubMed:11209081, ECO:0000305|PubMed:20974893}. reclassified-function P26288 ndhD Arabidopsis thaliana (Mouse-ear cress) 3702 NAD(P)H-quinone oxidoreductase chain 4, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase, chain 4) (NADH-plastoquinone oxidoreductase chain 4) Was originally thought to originate from Synechocystis PCC6803. {ECO:0000305|PubMed:1907869}. reclassified-function P26289 ndhE Arabidopsis thaliana (Mouse-ear cress) 3702 NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 4L) (NADH-plastoquinone oxidoreductase subunit 4L) Was originally thought to originate from Synechocystis PCC6803. {ECO:0000305|PubMed:1907869}. reclassified-function P56809 ycf15-A; ycf15-B Arabidopsis thaliana (Mouse-ear cress) 3702 Uncharacterized protein ycf15 (ORF77) Was originally thought to be a pseudogene before the proof of transcription of the gene. {ECO:0000305|PubMed:11292076}. reclassified-function O29352 dapA Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16) 224325 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function O29353 dapB Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16) 224325 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5P838 dapA Aromatoleum aromaticum (strain DSM 19018 / LMG 30748 / EbN1) (Azoarcus sp. (strain EbN1)) 76114 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5P1G6 dapB Aromatoleum aromaticum (strain DSM 19018 / LMG 30748 / EbN1) (Azoarcus sp. (strain EbN1)) 76114 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P14661 ASCEC-1 Ascaris suum (Pig roundworm) (Ascaris lumbricoides) 6253 Cecropin-P1 Was originally thought to originate from pig (PubMed:1396696, PubMed:2512577). It was later shown that this protein in fact originates from A.suum which is present in pig intestine (PubMed:12737319). {ECO:0000305|PubMed:12737319}. reclassified-function B8N8Q9 afvA Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) 332952 NADPH dehydrogenase afvA (EC 1.6.99.1) (Aflavarin synthesis protein A) (Old yellow enzyme) (OYE) Was originally proposed to be an NADPH dehydrogenase in the biosynthesis of aflavarin, hydroxylating siderin and 7-demethyl siderin. However, it could not catalyze the hydroxylation of the siderin analogs, such as 6-hydroxy-4-methylcoumarin, 6-methylcoumarin, and 7-methylcoumarin, indicating that the enzyme may not play as a hydroxylase in the biosynthesis of aflavarin. {ECO:0000305|PubMed:26209694, ECO:0000305|PubMed:38229304}. reclassified-function Q4WSD1 macA Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) 330879 Copper-activated transcription factor macA MacA was reported to additionally be involved in the control of iron acquisition (PubMed:28515264). However, neither growth assays on solid and in liquid media, analysis of siderophore production nor expression analysis of genes involved in iron acquisition indicated the involvement of macA in the regulation of iron uptake (PubMed:32812643). The authors of the first papers responded with more evidence tha macA is indeed involved in iron uptake (PubMed:32845274). {ECO:0000269|PubMed:28515264, ECO:0000269|PubMed:32812643, ECO:0000269|PubMed:32845274}. reclassified-function K0E2F6 ecdB Aspergillus pachycristata (strain ATCC 58397 / KCTC 6058 / NRRL 11440 / A42355) (Aspergillus nidulans var. roseus) 590939 Transcription factor ecdB EcdB, ecdC, ecdD, ecdE and ecdF have previously been identified as being part of the echinocandin B biosynthetic cluster, but it was later realized that this was due to a genome misassembly and these 5 proteins are now considered as artifacts and not part of the cluster. {ECO:0000269|PubMed:27502607}. reclassified-function K0DZ95 ecdC Aspergillus pachycristata (strain ATCC 58397 / KCTC 6058 / NRRL 11440 / A42355) (Aspergillus nidulans var. roseus) 590939 Major facilitator-type transporter ecdC EcdB, ecdC, ecdD, ecdE and ecdF have previously been identified as being part of the echinocandin B biosynthetic cluster, but it was later realized that this was due to a genome misassembly and these 5 proteins are now considered as artifacts and not part of the cluster. {ECO:0000269|PubMed:27502607}. reclassified-function K0E3U9 ecdD Aspergillus pachycristata (strain ATCC 58397 / KCTC 6058 / NRRL 11440 / A42355) (Aspergillus nidulans var. roseus) 590939 Major facilitator-type transporter ecdD EcdB, ecdC, ecdD, ecdE and ecdF have previously been identified as being part of the echinocandin B biosynthetic cluster, but it was later realized that this was due to a genome misassembly and these 5 proteins are now considered as artifacts and not part of the cluster. {ECO:0000269|PubMed:27502607}. reclassified-function K0E4E1 ecdE Aspergillus pachycristata (strain ATCC 58397 / KCTC 6058 / NRRL 11440 / A42355) (Aspergillus nidulans var. roseus) 590939 Putative glycosyl hydrolase ecdE (EC 3.2.1.-) EcdB, ecdC, ecdD, ecdE and ecdF have previously been identified as being part of the echinocandin B biosynthetic cluster, but it was later realized that this was due to a genome misassembly and these 5 proteins are now considered as artifacts and not part of the cluster. {ECO:0000269|PubMed:27502607}. reclassified-function K0E681 ecdF Aspergillus pachycristata (strain ATCC 58397 / KCTC 6058 / NRRL 11440 / A42355) (Aspergillus nidulans var. roseus) 590939 Putative glycosyl hydrolase ecdF (EC 3.2.1.-) EcdB, ecdC, ecdD, ecdE and ecdF have previously been identified as being part of the echinocandin B biosynthetic cluster, but it was later realized that this was due to a genome misassembly and these 5 proteins are now considered as artifacts and not part of the cluster. {ECO:0000269|PubMed:27502607}. reclassified-function Q0CJ60 atC Aspergillus terreus (strain NIH 2624 / FGSC A1156) 341663 Glucose methanol choline oxidoreductase atC (EC 1.1.99.-) (Terreic acid biosynthesis cluster protein C) Was originally thought to be a cyclase (PubMed:25265334). However, was later shown to have oxidoreductase activity (PubMed:29391515). {ECO:0000269|PubMed:25265334, ECO:0000269|PubMed:29391515}. reclassified-function Q0CJ54 atG Aspergillus terreus (strain NIH 2624 / FGSC A1156) 341663 Cytochrome P450 monooxygenase atG (EC 1.-.-.-) (Terreic acid biosynthesis cluster protein G) Was originally thought to convert 3-methylcatechol directly to terremutin (PubMed:25265334). However, was later shown that this is not the case and that atG is likely to assist atE in the conversion of 3-methylcatechol to 3-methyl-1,2,4-benzenetriol (PubMed:29391515). {ECO:0000269|PubMed:25265334, ECO:0000269|PubMed:29391515}. reclassified-function A1K4F8 dapA Azoarcus sp. (strain BH72) 418699 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B6YQ20 dapA Azobacteroides pseudotrichonymphae genomovar. CFP2 511995 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C1DFM1 dapB Azotobacter vinelandii (strain DJ / ATCC BAA-1303) 322710 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q81SU0 dapB Bacillus anthracis 1392 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C3P5Q2 dapB Bacillus anthracis (strain A0248) 592021 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C3L8Q7 dapB Bacillus anthracis (strain CDC 684 / NRRL 3495) 568206 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C1EN29 dapB Bacillus cereus (strain 03BB102) 572264 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7HL46 dapB Bacillus cereus (strain AH187) 405534 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7JH17 dapB Bacillus cereus (strain AH820) 405535 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q73AW1 dapB Bacillus cereus (strain ATCC 10987 / NRS 248) 222523 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P32444 mbl Bacillus cereus (strain ATCC 10987 / NRS 248) 222523 Cell shape-determining protein Mbl Was originally thought to be MreB. {ECO:0000305|PubMed:1452027}. reclassified-function Q81FP4 dapB Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) 226900 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7HHT6 dapB Bacillus cereus (strain B4264) 405532 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7IPB0 dapB Bacillus cereus (strain G9842) 405531 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B9IVQ5 dapB Bacillus cereus (strain Q1) 361100 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q63DK0 dapB Bacillus cereus (strain ZK / E33L) 288681 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7GN70 dapB Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98) 315749 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q65I50 dapB Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) 279010 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A9VME3 dapB Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis) 315730 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P03683 5.5 Bacillus phage phi29 (Bacteriophage phi-29) 2884424 Gene product 5.5 (gp5.5) (Gene product 5B) (gp5B) (Protein p5.5) Was originally thought to be GP5. {ECO:0000305|PubMed:6274853}. reclassified-function A8FEI3 dapB Bacillus pumilus (strain SAFR-032) 315750 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P0DTW2 Bacillus safensis 561879 Pumilarin (Circular bacteriocin) (Enterocin AS-48-like) (Head-to-tail cyclized peptide) Strain B4107 was originally classified as being from Bacillus pumilus, hence protein name pumilarin. {ECO:0000305}. reclassified-function P52328 sigA Bacillus sp 1409 RNA polymerase sigma factor SigA (Sigma-A) Was originally (Ref.1) thought to originate from Leptospira interrogans serovar copenhageni, but is most probably from a Bacillus species. {ECO:0000305}. reclassified-function P28622 Bacillus sp. (strain KSM-522) 120046 Endoglucanase 4 (EC 3.2.1.4) (Cellulase 4) (EG-IV) (Endo-1,4-beta-glucanase 4) Was originally thought to originate from Clostridium cellulovorans and was termed endoglucanase C (engC). {ECO:0000305|PubMed:2113383}. reclassified-function P09123 thrC Bacillus sp. (strain ULM1) 231717 Threonine synthase (TS) (EC 4.2.3.1) Was originally thought to originate from B.lactofermentum=C.glutamicum. {ECO:0000305|PubMed:3186450}. reclassified-function P39774 spaB Bacillus subtilis 1423 Subtilin biosynthesis protein SpaB Was originally proposed to code for two separate adjacent ORFs, SpaE and SpaD. {ECO:0000305|PubMed:1400221}. reclassified-function P42977 cca Bacillus subtilis (strain 168) 224308 CCA-adding enzyme (EC 2.7.7.72) (CCA tRNA nucleotidyltransferase) (tRNA CCA-pyrophosphorylase) (tRNA adenylyl-/cytidylyl- transferase) (tRNA nucleotidyltransferase) (tRNA-NT) Was originally predicted to have poly(A) polymerase activity (EC 2.7.7.19), and its gene was named papS. {ECO:0000305|PubMed:9829937}. reclassified-function Q04796 dapA Bacillus subtilis (strain 168) 224308 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P42976 dapB Bacillus subtilis (strain 168) 224308 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P19638 dgkA Bacillus subtilis (strain 168) 224308 Undecaprenol kinase (UdpK) (EC 2.7.1.66) Was originally thought to be a diacylglycerol kinase. {ECO:0000305|PubMed:12923107}. reclassified-function P94398 folE2 Bacillus subtilis (strain 168) 224308 GTP cyclohydrolase FolE2 (EC 3.5.4.16) (GTP cyclohydrolase 1B) Was originally thought to be a zinc uptake system. {ECO:0000305|PubMed:12426338}. reclassified-function O07009 ganS Bacillus subtilis (strain 168) 224308 Galactooligosaccharide-binding protein (Cyclodextrin-binding protein) Was originally described as a cyclodextrin-binding protein, but it was shown later that it has no affinity for cyclodextrin. {ECO:0000305|PubMed:11682178, ECO:0000305|PubMed:27501980}. reclassified-function O34483 hprK Bacillus subtilis (strain 168) 224308 HPr kinase/phosphorylase (HPrK/P) (EC 2.7.11.-) (EC 2.7.4.-) (HPr kinase/phosphatase) (HPr(Ser) kinase/phosphorylase) Was originally called HPr kinase/phosphatase, but P-Ser-HPr dephosphorylation was found to follow a quite unique mechanism (PubMed:12359880), in which Pi instead of H(2)O is used for the nucleophilic attack on the phosphoryl group. P-Ser-HPr dephosphorylation is therefore not a phosphohydrolysis but a phospho-phosphorolysis reaction, and the bifunctional enzyme was dubbed HPr kinase/phosphorylase. {ECO:0000305|PubMed:12359880}. reclassified-function P54512 mntR Bacillus subtilis (strain 168) 224308 HTH-type transcriptional regulator MntR (Manganese transport regulator) (Manganese(II) metalloregulatory protein MntR) Was originally thought to act as an activator for the mntABCD operon. {ECO:0000305|PubMed:10760146, ECO:0000305|PubMed:12950915}. reclassified-function P42956 mtlA Bacillus subtilis (strain 168) 224308 PTS system mannitol-specific EIICB component (EIICB-Mtl) (EII-Mtl) [Includes: Mannitol permease IIC component (PTS system mannitol-specific EIIC component); Mannitol-specific phosphotransferase enzyme IIB component (EC 2.7.1.197) (PTS system mannitol-specific EIIB component)] Was originally thought to be a longer ORF that encodes what is now known to be mtlA and mtlF. {ECO:0000305}. reclassified-function O31662 mtnA Bacillus subtilis (strain 168) 224308 Methylthioribose-1-phosphate isomerase (M1Pi) (MTR-1-P isomerase) (EC 5.3.1.23) (S-methyl-5-thioribose-1-phosphate isomerase) Was originally thought to be a translation initiation factor. {ECO:0000305}. reclassified-function O34798 pdaC Bacillus subtilis (strain 168) 224308 Peptidoglycan-N-acetylmuramic acid deacetylase PdaC (Peptidoglycan MurNAc deacetylase) (EC 3.5.1.-) (Polysaccharide deacetylase PdaC) Was originally described as a deoxyribonuclease (PubMed:17878218), but it was later shown that PdaC has no DNase activity at all (PubMed:22277649). {ECO:0000305|PubMed:17878218, ECO:0000305|PubMed:22277649}. reclassified-function P14203 pdeH Bacillus subtilis (strain 168) 224308 Cyclic di-GMP phosphodiesterase PdeH (EC 3.1.4.52) Was originally thought to be comB, a competence gene. {ECO:0000305|PubMed:2507523}. reclassified-function P39610 pdxK Bacillus subtilis (strain 168) 224308 Pyridoxine kinase (EC 2.7.1.35) (PN/PL/PM kinase) (Pyridoxal kinase) (Pyridoxamine kinase) (Vitamin B6 kinase) Was originally annotated in the complete genome as thiD. {ECO:0000305|PubMed:9384377}. reclassified-function P40806 pksJ Bacillus subtilis (strain 168) 224308 Polyketide synthase PksJ (PKS) Was originally thought to be two separate ORFs named pksJ and pksK. {ECO:0000305}. reclassified-function Q9JMQ2 ppaX Bacillus subtilis (strain 168) 224308 Pyrophosphatase PpaX (EC 3.6.1.1) Was originally (PubMed:9465101) called P-Ser-HPr phosphatase as it has been shown to stimulate P-Ser-HPr dephosphorylation, but actually (PubMed:12359880) it has pyrophosphatase activity. {ECO:0000305|PubMed:12359880, ECO:0000305|PubMed:9465101}. reclassified-function P60495 pxpB Bacillus subtilis (strain 168) 224308 5-oxoprolinase subunit B (5-OPase subunit B) (EC 3.5.2.9) (5-oxoprolinase (ATP-hydrolyzing) subunit B) (Antikinase KipI) (Kinase A inhibitor) (Sporulation inhibitor KipI) Was originally (PubMed:8574415, PubMed:8969502) thought to be a longer ORF that encodes what is now known to be pxpB (kipI) and pxpC (kipA). {ECO:0000305|PubMed:9334321}. reclassified-function Q7WY77 pxpC Bacillus subtilis (strain 168) 224308 5-oxoprolinase subunit C (5-OPase subunit C) (EC 3.5.2.9) (5-oxoprolinase (ATP-hydrolyzing) subunit C) (KipI antagonist) (Protein KipA) Was originally (PubMed:8574415, PubMed:8969502) thought to be a longer ORF that encodes what is now known to be pxpB (kipI) and pxpC (kipA). {ECO:0000305|PubMed:9334321}. reclassified-function P36946 rbsD Bacillus subtilis (strain 168) 224308 D-ribose pyranase (EC 5.4.99.62) Was originally thought (PubMed:7921236, PubMed:9353933) to be a high affinity ribose transport protein. {ECO:0000305}. reclassified-function P37552 ridA Bacillus subtilis (strain 168) 224308 2-iminobutanoate/2-iminopropanoate deaminase (EC 3.5.99.10) (Enamine/imine deaminase) Was originally (PubMed:10368157) thought to have a role in the purine repressor-mediated regulation of purA or the pur operon. The effect of yabJ (now ridA) on regulation of purA was due to the orientation of the marker gene downstream of purR in the yabJ mutant strain used in PubMed:10368157. {ECO:0000269|PubMed:14594850, ECO:0000305|PubMed:10368157}. reclassified-function P37531 sleL Bacillus subtilis (strain 168) 224308 Cortical fragment-lytic enzyme (CFLE) (EC 3.2.1.-) (Spore germination protein) (Spore peptidoglycan N-acetylglucosaminidase) Was originally thought to have epimerase activity. {ECO:0000305|PubMed:12177332}. reclassified-function P21885 speA Bacillus subtilis (strain 168) 224308 Arginine decarboxylase (EC 4.1.1.19) Was originally (Ref.1) thought to be a lysine decarboxylase and was consequently named cad. {ECO:0000305}. reclassified-function P71031 sspO Bacillus subtilis (strain 168) 224308 Small, acid-soluble spore protein O (SASP O) Was originally thought to be a spore coat protein. {ECO:0000305|PubMed:9068633}. reclassified-function P71032 sspP Bacillus subtilis (strain 168) 224308 Small, acid-soluble spore protein P (SASP P) Was originally thought to be a spore coat protein. {ECO:0000305|PubMed:9068633}. reclassified-function O32163 sufU Bacillus subtilis (strain 168) 224308 Zinc-dependent sulfurtransferase SufU (EC 2.-.-.-) (Putative iron-sulfur cluster assembly scaffold protein SufU) (Sulfur acceptor protein SufU) Was originally thought to be an iron-sulfur cluster assembly scaffold protein (PubMed:20097860, PubMed:21236255). It is now thought to be a zinc-dependent sulfur transfer protein (PubMed:24321018). {ECO:0000305|PubMed:20097860, ECO:0000305|PubMed:21236255, ECO:0000305|PubMed:24321018}.; reclassified-function P68577 sunA Bacillus subtilis (strain 168) 224308 SPbeta prophage-derived bacteriocin sublancin-168 Was originally (PubMed:9722542, PubMed:11872755) thought to be a lantibiotic but was later shown to be an S-linked glycopeptide. {ECO:0000305|PubMed:21196935}. reclassified-function Q02115 tagU Bacillus subtilis (strain 168) 224308 Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU (EC 2.7.8.-) (Membrane-bound protein LytR) Was originally thought to be involved in transcriptional regulation. {ECO:0000305|PubMed:1357079}.; reclassified-function P25052 tenA Bacillus subtilis (strain 168) 224308 Aminopyrimidine aminohydrolase (EC 3.5.99.2) (4-amino-5-aminomethyl-2-methylpyrimidine hydrolase) (Thiaminase II) Was originally described as a regulatory protein involved in the regulation of the production of extracellular enzymes. {ECO:0000303|PubMed:1898926, ECO:0000305}. reclassified-function P25053 tenI Bacillus subtilis (strain 168) 224308 Thiazole tautomerase (EC 5.3.99.10) Was originally described as a regulatory protein involved in the regulation of the production of extracellular enzymes. {ECO:0000303|PubMed:1898926, ECO:0000305}. reclassified-function P54423 wprA Bacillus subtilis (strain 168) 224308 Cell wall-associated protease (EC 3.4.21.-) [Cleaved into: Cell wall-associated polypeptide CWBP23 (CWBP23); Cell wall-associated polypeptide CWBP52 (CWBP52)] The CWBP52 polypeptide was originally called CWBP55 based on its apparent molecular weight. {ECO:0000305}. reclassified-function O31489 ydcI Bacillus subtilis (strain 168) 224308 Uncharacterized protein YdcI Was originally (Ref.1) thought to be two genes, ydcI and ydcJ. {ECO:0000305}. reclassified-function O34939 ydiO Bacillus subtilis (strain 168) 224308 Type II methyltransferase M1.BsuMI (M1.BsuMI) (EC 2.1.1.37) (BsuMI modification methylase subunit YdiO) (Cytosine-specific methyltransferase M1.BsuMI) The characterized enzyme was reported to be a monomer of approximately 45 kDa; it is not clear whether this corresponds to YdiO, YdiP or to another activity altogether. {ECO:0000305|PubMed:3150363}. reclassified-function O34680 ydiP Bacillus subtilis (strain 168) 224308 Type II methyltransferase M2.BsuMI (M2.BsuMI) (EC 2.1.1.37) (BsuMI modification methylase subunit YdiP) (Cytosine-specific methyltransferase M2.BsuMI) The characterized enzyme was reported to be a monomer of approximately 45 kDa; it is not clear whether this corresponds to YdiO, YdiP or to another activity altogether. {ECO:0000305|PubMed:3150363}. reclassified-function O31506 yeeF Bacillus subtilis (strain 168) 224308 Toxin YeeF (DNase YeeF) Was originally suggested to be an RNase. {ECO:0000305|PubMed:22200572}. reclassified-function O34400 yfkA Bacillus subtilis (strain 168) 224308 Putative protein YfkA Was originally (PubMed:8969503, PubMed:9384377) predicted to be the product of two different genes yfkA and yfkB. {ECO:0000305|PubMed:8969503, ECO:0000305|PubMed:9384377}. reclassified-function O07518 yhaJ Bacillus subtilis (strain 168) 224308 Uncharacterized membrane protein YhaJ Was initially thought to be two separate ORFs named yhaJ and yhaK. {ECO:0000305|PubMed:9579061}. reclassified-function P54599 yhcO Bacillus subtilis (strain 168) 224308 Uncharacterized protein YhcO Was initially thought to be two separate ORFs named yhcO and yhcP. {ECO:0000305|PubMed:8969498}. reclassified-function O06728 yisP Bacillus subtilis (strain 168) 224308 Farnesyl diphosphate phosphatase YisP (EC 3.1.7.6) Was originally thought to be a squalene synthase (PubMed:20713508). Further characterization suggests it is actually a farnesyl diphosphate phosphatase (PubMed:25308276). {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:25308276}. reclassified-function O06750 yitO Bacillus subtilis (strain 168) 224308 Uncharacterized protein YitO Was initially thought to be two separate ORFs named yitO and yitN. {ECO:0000305|PubMed:9353932}. reclassified-function O34330 yobL Bacillus subtilis (strain 168) 224308 Toxin YobL (DNase YobL) Was originally thought to be an RNase; when the C-terminus (residues 449-600) is expressed in E.coli it has RNase, not DNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate immunity protein YobK, but not by immunity proteins specific to other LXG toxins. Mutation of His-562 to Ala leads to loss of growth inhibition and RNase activity in E.coli. {ECO:0000269|PubMed:22200572}. reclassified-function O31998 yokI Bacillus subtilis (strain 168) 224308 Toxin YokI (DNase YokL) (SPbeta prophage-derived protein YokI) Was originally suggested to be an RNase. {ECO:0000305|PubMed:22200572}. reclassified-function P45942 yqcG Bacillus subtilis (strain 168) 224308 Toxin YqcG (DNase YqcG) Was originally thought to be an RNase; when the C-terminus (residues 379-531) is expressed in E.coli it has RNase, not DNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate immunity protein YobK, but not by immunity proteins specific to other LXG toxins. {ECO:0000269|PubMed:22200572}. reclassified-function O34634 yrrK Bacillus subtilis (strain 168) 224308 Putative pre-16S rRNA nuclease (EC 3.1.-.-) Was originally suggested to be a nuclease that resolves Holliday junction intermediates during genetic recombination. {ECO:0000303|PubMed:16021622}. reclassified-function P06629 ywjG Bacillus subtilis (strain 168) 224308 Uncharacterized protein YwjG Was originally thought to be the spo0F protein. {ECO:0000305|PubMed:6402773}. reclassified-function P39155 ywlE Bacillus subtilis (strain 168) 224308 Protein-arginine-phosphatase (PAP) (EC 3.9.1.2) (Phosphoarginine phosphatase) Was originally thought to be a protein-tyrosine-phosphatase (PubMed:15995210). Was later shown to function as an arginine phosphatase in vivo and in vitro (PubMed:22517742, PubMed:23770242). {ECO:0000305|PubMed:15995210}. reclassified-function P42296 yxiD Bacillus subtilis (strain 168) 224308 Toxin YxiD (DNase YxiD) Was originally thought to be an RNase; when the C-terminus (residues 409-569) is expressed in E.coli it has RNase, not DNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate immunity protein YxxD, but not by immunity proteins specific to other toxins with the LXG domain. Mutation of His-548 to Ala leads to loss of growth inhibition and RNase activity in E.coli. {ECO:0000269|PubMed:22200572}. reclassified-function A0RBY6 dapB Bacillus thuringiensis (strain Al Hakam) 412694 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6HL23 dapB Bacillus thuringiensis subsp. konkukian (strain 97-27) 281309 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7Z4U8 dapA Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum) 326423 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7Z600 dapB Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum) 326423 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5LIC7 lacZ_4 Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / LMG 10263 / NCTC 9343 / Onslow / VPI 2553 / EN-2) 272559 Beta-glucuronidase (GUS) (EC 3.2.1.31) (BfGUS) Was originally thought to be a beta-galactosidase, but in vitro assays confirm that it is a beta-glucuronidase. {ECO:0000269|PubMed:26364932}. reclassified-function A1US27 dapA Bartonella bacilliformis (strain ATCC 35685 / KC583 / Herrer 020/F12,63) 360095 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1UTM3 dapB Bartonella bacilliformis (strain ATCC 35685 / KC583 / Herrer 020/F12,63) 360095 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6G468 dapA Bartonella henselae (strain ATCC 49882 / DSM 28221 / CCUG 30454 / Houston 1) (Rochalimaea henselae) 283166 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6G2G3 dapB Bartonella henselae (strain ATCC 49882 / DSM 28221 / CCUG 30454 / Houston 1) (Rochalimaea henselae) 283166 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6G091 dapA Bartonella quintana (strain Toulouse) (Rochalimaea quintana) 283165 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6FZ13 dapB Bartonella quintana (strain Toulouse) (Rochalimaea quintana) 283165 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A9IRK3 dapA Bartonella tribocorum (strain DSM 28219 / CCUG 45778 / CIP 105476 / IBS 506) 382640 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A9IXE5 dapB Bartonella tribocorum (strain DSM 28219 / CCUG 45778 / CIP 105476 / IBS 506) 382640 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6MRM9 dapA Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100) 264462 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6MRM8 dapB Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100) 264462 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2IBR8 dapB Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB 8712) 395963 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C5BWQ6 dapB Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / CCUG 43141 / JCM 11478 / NBRC 16432 / NCIMB 13614 / HKI 0122) 471853 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8DWI2 dapA Bifidobacterium animalis subsp. lactis (strain AD011) 442563 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8DWI3 dapB Bifidobacterium animalis subsp. lactis (strain AD011) 442563 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B3DTC8 dapA Bifidobacterium longum (strain DJO10A) 205913 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8G527 dapA Bifidobacterium longum (strain NCC 2705) 206672 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8G526 dapB Bifidobacterium longum (strain NCC 2705) 206672 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7GUF6 dapB Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) 391904 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7VRT1 dapA Blochmanniella floridana 203907 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7VQK8 dapB Blochmanniella floridana 203907 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q492F5 dapA Blochmanniella pennsylvanica (strain BPEN) 291272 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q493S0 dapB Blochmanniella pennsylvanica (strain BPEN) 291272 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7ISW2 QPCT Boiga dendrophila (Mangrove snake) (Gold-ringed cat snake) 46286 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (By similarity). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000250|UniProtKB:Q16769}. reclassified-function A7ISW1 QPCT Boiga irregularis (Brown tree snake) (Coluber irregularis) 92519 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (By similarity). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000250|UniProtKB:Q16769}. reclassified-function Q7WGH5 dapB Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) 257310 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7W510 dapB Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253) 257311 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P40415 Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 257313 Probable parvulin-type peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Protein p13) (Rotamase) Was originally (Ref.2) thought to originate from Dictyostelium discoideum. {ECO:0000305}. reclassified-function P16575 bvgS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 257313 Virulence sensor protein BvgS (EC 2.7.13.3) Was originally thought to be two separate ORFs named bvgB and bvgC. {ECO:0000305|PubMed:2549542}. reclassified-function Q7VXZ8 dapA Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 257313 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9X6Y9 dapB Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 257313 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P54281 Bos taurus (Bovine) 9913 Calcium-activated chloride channel regulator 1 (EC 3.4.-.-) (Calcium-activated chloride channel) (Epithelial chloride channel protein) Was initially characterized as chloride channel, but such a function is difficult to reconcile with the single predicted transmembrane region. Other family members have been shown to stimulate channel activity. {ECO:0000269|PubMed:8537359, ECO:0000305}. reclassified-function P02769 ALB Bos taurus (Bovine) 9913 Albumin (BSA) (allergen Bos d 6) A peptide arising from positions 165 to 173 was originally termed neurotensin-related peptide (NRP) and was thought to regulate fat digestion, lipid absorption, and blood flow. {ECO:0000305|PubMed:2437111}. reclassified-function O75601 CASP13 Bos taurus (Bovine) 9913 Caspase-13 (CASP-13) (EC 3.4.22.-) (Evolutionary related interleukin-1-beta-converting enzyme) (ERICE) [Cleaved into: Caspase-13 subunit 1; Caspase-13 subunit 2] Was originally thought to originate from human. {ECO:0000305|PubMed:9624166}. reclassified-function Q01321 COXFA4 Bos taurus (Bovine) 9913 Cytochrome c oxidase subunit FA4 (Complex I-MLRQ) (CI-MLRQ) (Cytochrome c oxidase subunit NDUFA4) (NADH-ubiquinone oxidoreductase MLRQ subunit) Was initially believed to be a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (complex I). However, was not present in all complex I preparations and presence correlated with contamination by COX6B1 (PubMed:12837546). {ECO:0000305|PubMed:12837546}. reclassified-function P25930 CXCR4 Bos taurus (Bovine) 9913 C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (Fusin) (LCR1) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184) Was originally thought to be a receptor for neuropeptide Y type 3 (NPY3R) (NPY3-R). Subsequent studies indicated it does not function as receptor for neuropeptide Y. {ECO:0000305|PubMed:1661837, ECO:0000305|PubMed:8234909}. reclassified-function P56965 DDAH1 Bos taurus (Bovine) 9913 N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (DDAH-1) (Dimethylarginine dimethylaminohydrolase 1) (EC 3.5.3.18) (DDAHI) (Dimethylargininase-1) Was originally thought to be a heme protein, but this was later shown to be an artifact. {ECO:0000305|PubMed:8849684}. reclassified-function Q3SX44 DDAH2 Bos taurus (Bovine) 9913 Putative hydrolase DDAH2 (EC 3.-.-.-) (DDAHII) (Inactive N(G),N(G)-dimethylarginine dimethylaminohydrolase 2) (DDAH-2) (Inactive dimethylarginine dimethylaminohydrolase 2) Was originally thought to be a dimethylarginine dimethylaminohydrolase (with EC:3.5.3.18) able to hydrolyze N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) (By similarity). However, a recent multicentre study has shown that DDAH2 does not have dimethylarginine dimethylaminohydrolase activity by using different approaches (By similarity). {ECO:0000250|UniProtKB:O95865}. reclassified-function Q17QF2 EEF1AKMT1 Bos taurus (Bovine) 9913 EEF1A lysine methyltransferase 1 (EC 2.1.1.-) (N(6)-adenine-specific DNA methyltransferase 2) (Protein-lysine N-methyltransferase N6AMT2) Was originally thought to be an N(6)-adenine-specific DNA methyltransferase based on primary sequence and predicted secondary structure. {ECO:0000255|HAMAP-Rule:MF_03187}. reclassified-function Q2KJ61 ELP3 Bos taurus (Bovine) 9913 Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}.; reclassified-function Q2TBH6 ELP4 Bos taurus (Bovine) 9913 Elongator complex protein 4 The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}. reclassified-function P18203 FKBP1A Bos taurus (Bovine) 9913 Peptidyl-prolyl cis-trans isomerase FKBP1A (PPIase FKBP1A) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FKBP-12) (Calstabin-1) (FK506-binding protein 1A) (FKBP-1A) (Immunophilin FKBP12) (Rotamase) Was originally thought to be protein kinase C inhibitor 2 (PKCI-2 or 12 kDa inhibitor of protein kinase C). Later, was shown experimentally not to inhibit protein kinase C (PubMed:1710782, PubMed:1868545). {ECO:0000269|PubMed:1710782, ECO:0000269|PubMed:1868545, ECO:0000305|PubMed:1915353, ECO:0000305|PubMed:2253615}. reclassified-function P20821 GCSH Bos taurus (Bovine) 9913 Glycine cleavage system H protein, mitochondrial (Lipoic acid-containing protein) Was originally (PubMed:3080335, PubMed:2553401) thought to be a ferredoxin. {ECO:0000305}. reclassified-function P50397 GDI2 Bos taurus (Bovine) 9913 Rab GDP dissociation inhibitor beta (Rab GDI beta) (Guanosine diphosphate dissociation inhibitor 2) (GDI-2) Was originally thought to originate from mouse. {ECO:0000305|PubMed:7513052}. reclassified-function P62958 HINT1 Bos taurus (Bovine) 9913 Adenosine 5'-monophosphoramidase HINT1 (EC 3.9.1.-) (17 kDa inhibitor of protein kinase C) (Desumoylating isopeptidase HINT1) (EC 3.4.22.-) (Histidine triad nucleotide-binding protein 1) (Protein kinase C inhibitor 1) (Protein kinase C-interacting protein 1) (PKCI-1) Was originally thought to be a protein kinase C inhibitor and to bind zinc in solution. Both seem to be incorrect. {ECO:0000305}. reclassified-function Q9MYP6 HSD17B14 Bos taurus (Bovine) 9913 L-fucose dehydrogenase (EC 1.1.1.122) (17-beta-hydroxysteroid dehydrogenase DHRS10) (Dehydrogenase/reductase SDR family member 10) (Retinal short-chain dehydrogenase/reductase retSDR3) Was reported as a 17-beta-hydroxysteroid dehydrogenase that catalyzes estradiol and testosterone oxidation in the C17-hydroxyl group to form estrone and androstenedione, respectively (in vitro). However, HSD17B14 is very inefficient in oxidizing steroids, testosterone, suggesting that steroids cannot be physiological substrates for HSD17B14. {ECO:0000250|UniProtKB:Q9BPX1}. reclassified-function Q3SWY2 ILK Bos taurus (Bovine) 9913 Scaffold protein ILK (ILK-1) (ILK-2) (Inactive integrin-linked kinase) (p59ILK) Was originally thought to act as a serine/threonine-protein kinase. Now thought to be a pseudokinase which does not have kinase activity and which functions solely as a scaffold protein. {ECO:0000250|UniProtKB:Q13418}. reclassified-function P82908 KGD4 Bos taurus (Bovine) 9913 Alpha-ketoglutarate dehydrogenase component 4 (Alpha-ketoglutarate dehydrogenase subunit 4) (Mitochondrial ribosomal protein S36) Was originally identified in the small subunit (28S) of mitochondrial ribosomes that were purified on sucrose gradients (PubMed:11279123, PubMed:22015679). This observation has been challenged by experiments showing KGD4 copurification with the oxoglutarate dehydrogenase complex (OGDHC), also called alpha-ketoglutarate dehydrogenase complex (KGDH). Both mitochondrial ribosome 28S subunit and OGDC have a similar size and OGDC is highly abundant, therefore OGDC has been found to contaminate ribosomal preparations performed by sequential centrifugation steps (By similarity). In addition, KGD4 could not be located in the structure of the human mitochondrial ribosome, supporting the hypothesis that it is not a mitoribosomal protein (By similarity). {ECO:0000250|UniProtKB:P82909, ECO:0000250|UniProtKB:Q9CQX8, ECO:0000269|PubMed:11279123, ECO:0000269|PubMed:22015679}. reclassified-function P83095 LACTB Bos taurus (Bovine) 9913 Serine beta-lactamase-like protein LACTB, mitochondrial (EC 3.4.-.-) Was originally identified as 39S ribosomal protein L56 (MRP-L56). {ECO:0000305|PubMed:11551941}. reclassified-function Q1JQD7 MOCS1 Bos taurus (Bovine) 9913 Molybdenum cofactor biosynthesis protein 1 [Includes: GTP 3',8-cyclase (EC 4.1.99.22) (MOCS1A) (Molybdenum cofactor biosynthesis protein A); Cyclic pyranopterin monophosphate synthase (EC 4.6.1.17) (MOCS1B) (Molybdenum cofactor biosynthesis protein C)] The C-terminus of Mocs1a was previously believed to be thiocarboxylated, but it is now known not to be the case. {ECO:0000250|UniProtKB:Q9NZB8}. reclassified-function Q0P570 MVD Bos taurus (Bovine) 9913 Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Mevalonate (diphospho)decarboxylase) (MDDase) (Mevalonate pyrophosphate decarboxylase) Was originally thought to be located in the peroxisome. However, was later shown to be cytosolic. {ECO:0000250|UniProtKB:P53602}. reclassified-function P31836 NCAM1 Bos taurus (Bovine) 9913 Neural cell adhesion molecule 1 (N-CAM-1) (NCAM-1) Was originally thought to be a calmodulin-independent adenylate cyclase. {ECO:0000305|PubMed:2776887}. reclassified-function P52175 NME1 Bos taurus (Bovine) 9913 Nucleoside diphosphate kinase A (NDP kinase A) (NDPK A) (EC 2.7.4.6) (Farnesyl diphosphate kinase NME1) (EC 2.7.4.18) (Histidine protein kinase NDK) (EC 2.7.13.3) (Non-specific serine/threonine protein kinase NME1) (EC 2.7.11.1) (Nucleoside diphoshate kinase 1) (NDK1) (Nucleoside diphosphate kinase NBR-A) (NBR-A) (Nucleoside diphosphate kinase NBR-B) (NBR-B) (Putative 3'-5'-DNA exonuclease NDK1) (EC 3.1.11.-) (Putative granzyme A-activated DNA endonuclease) (GAAD) (EC 3.1.24.-) Originally thought that the two cDNAs found, corresponded to two different genes, the first has been named NBR-A (X92956) and the second NBR-B (X92957) by analogy to NME1/NDPKA and NME2/NDPKB in human, but in fact these two cDNAs correspond to the same gene NME1 in bovin. {ECO:0000305|PubMed:9760230}. reclassified-function Q05927 NT5E Bos taurus (Bovine) 9913 5'-nucleotidase (5'-NT) (EC 3.1.3.35) (EC 3.1.3.5) (EC 3.1.3.89) (EC 3.1.3.91) (EC 3.1.3.99) (5'-deoxynucleotidase) (Ecto-5'-nucleotidase) (IMP-specific 5'-nucleotidase) (Thymidylate 5'-phosphatase) (CD antigen CD73) The homodimer was initially thought to be disulfide bonded; however it is not the case. {ECO:0000305|PubMed:10825541}. reclassified-function P38657 PDIA3 Bos taurus (Bovine) 9913 Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60) Was originally thought to be a phosphatidylinositol 4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha). {ECO:0000305}. reclassified-function Q08DA4 PHTF1 Bos taurus (Bovine) 9913 Protein PHTF1 The PHTF domain was initially defined as an atypical homeodomain, suggesting that this protein could act as a transcription regulator (By similarity). However, the protein is not found in the nucleus and mainly localizes in the endoplasmic reticulum membrane, suggesting that it does not act as a transcription factor (By similarity). {ECO:0000250|UniProtKB:F1M8G0, ECO:0000250|UniProtKB:Q9UMS5}. reclassified-function P21671 PLCD4 Bos taurus (Bovine) 9913 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (EC 3.1.4.11) (PLC-85) (Phosphoinositide phospholipase C-delta-4) (Phospholipase C-delta-2) (PLC-delta-2) (Phospholipase C-delta-4) (PLC-delta-4) Was initially (PubMed:2753038) named PLCD2 and was thought to be a new member of the PLC-delta family. It was later shown that it corresponds to PLCD4 (PubMed:15219862). {ECO:0000305|PubMed:15219862, ECO:0000305|PubMed:2753038}. reclassified-function Q2KIU2 PMVK Bos taurus (Bovine) 9913 Phosphomevalonate kinase (PMKase) (EC 2.7.4.2) Was originally thought to be located in the peroxisome. However, was later shown to be cytosolic. {ECO:0000250|UniProtKB:Q15126}. reclassified-function Q28120 QPCT Bos taurus (Bovine) 9913 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (By similarity). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000250|UniProtKB:Q16769}. reclassified-function Q0V8G3 QPCTL Bos taurus (Bovine) 9913 Glutaminyl-peptide cyclotransferase-like protein (EC 2.3.2.5) (Golgi-resident glutaminyl-peptide cyclotransferase) (isoQC) (gQC) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (By similarity). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000250|UniProtKB:Q16769}. reclassified-function Q29RM1 SLC25A19 Bos taurus (Bovine) 9913 Mitochondrial thiamine pyrophosphate carrier (Solute carrier family 25 member 19) Previously identified as the mitochondrial deoxyribonucleotide carrier. However other experiments later demonstrated that SLC25A19 is a thiamine diphosphate transporter and not a mitochondrial deoxyribonucleotide carrier. {ECO:0000250|UniProtKB:Q9HC21}. reclassified-function P32007 SLC25A6 Bos taurus (Bovine) 9913 ADP/ATP translocase 3 (ADP,ATP carrier protein 3) (ADP,ATP carrier protein, isoform T2) (ANT 2) (Adenine nucleotide translocator 3) (ANT 3) (Solute carrier family 25 member 6) [Cleaved into: ADP/ATP translocase 3, N-terminally processed] Was reported as a homodimer (PubMed:11809823). However, 3D structure data show that it forms a monomer (By similarity). {ECO:0000250|UniProtKB:G2QNH0, ECO:0000250|UniProtKB:P02722, ECO:0000269|PubMed:11809823}. reclassified-function O97594 SMC3 Bos taurus (Bovine) 9913 Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) (Chondroitin sulfate proteoglycan 6) Was originally isolated as a proteoglycan protein (explaining its name). Although not excluded, such secreted function is not clear. {ECO:0000305}. reclassified-function Q9NZ50 SNCG Bos taurus (Bovine) 9913 Gamma-synuclein (Synoretin) (SR) Was originally (PubMed:10192768) thought to correspond to a new class of synuclein. In fact, it is ortholog of the human gamma-synuclein. {ECO:0000305|PubMed:10192768}. reclassified-function Q3MHW7 TMEM97 Bos taurus (Bovine) 9913 Sigma intracellular receptor 2 (Sigma-2 receptor) (Sigma2 receptor) (Transmembrane protein 97) The molecular identity of the sigma-2 receptor has been unclear for a long time. It is now identified as TMEM97 (PubMed:28559337). Previously identified as PGRMC1. {ECO:0000250|UniProtKB:Q5BJF2, ECO:0000269|PubMed:28559337}. reclassified-function Q3SZI5 UCP2 Bos taurus (Bovine) 9913 Dicarboxylate carrier UCP2 (Mitochondrial uncoupling protein 2) (UCP 2) (Solute carrier family 25 member 8) The role of UCP2/SLC25A8 in mitochondrial proton conductance is a matter of debate. It was initially suggested that it mediates proton leak that increases net proton conductance in response to ROS such as reactive alkenals generated during fatty acid oxidation in mitochondria. By lowering the proton motive force, it would provide for feedback control of mitochondrial ROS metabolism limiting extensive ROS production and protecting cells against oxidative stress. This activity and its potential regulation by ubiquinones and nucleotides was disputed by later studies, which failed to reproduce the effect on proton conductance under physiological conditions. Rather than 'uncoupling' the link between electron transfer and ATP synthesis, it may couple metabolite transport to proton flux to allow for optimal ATP turnover. {ECO:0000250|UniProtKB:P55851, ECO:0000250|UniProtKB:P70406}. reclassified-function P00129 UQCRB Bos taurus (Bovine) 9913 Cytochrome b-c1 complex subunit 7 (Complex III subunit 7) (Complex III subunit VII) (QP-C) (Ubiquinol-cytochrome c reductase complex 14 kDa protein) Was originally thought to be the ubiquinone-binding protein (QP-C). {ECO:0000305|PubMed:2981208}. reclassified-function Q9YIB5 QPCT Bothrops jararaca (Jararaca) (Bothrops jajaraca) 8724 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (By similarity). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000250|UniProtKB:Q16769}. reclassified-function P93052 Botryococcus braunii (Green alga) 38881 L-lactate dehydrogenase (LDH) (EC 1.1.1.27) Was originally (Ref.1) thought to be a malate dehydrogenase or an NADH-dependent acyl-CoA reductase. {ECO:0000305|PubMed:7649295}. reclassified-function P26020 N Bovine coronavirus (strain OK-0514) (BCoV) (BCV) 231432 Nucleoprotein (Nucleocapsid protein) (NC) (Protein N) Was originally thought to originate from Turkey coronavirus. {ECO:0000305|PubMed:1856695}. reclassified-function C0R176 dapA Brachyspira hyodysenteriae (strain ATCC 49526 / WA1) 565034 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C0R175 dapB Brachyspira hyodysenteriae (strain ATCC 49526 / WA1) 565034 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9RH76 dapA Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) 224911 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q89WK2 dapB Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) 224911 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P31907 hoxX Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) 224911 Hydrogenase maturation factor HoxX Was originally thought to be a sensor protein involved in the regulation of hydrogenase activity. {ECO:0000305|PubMed:8510650}. reclassified-function A5E8K0 dapB Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) 288000 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A4YJP9 dapB Bradyrhizobium sp. (strain ORS 278) 114615 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P04573 Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum) 7740 Calcium vector protein (CAVP) Was originally thought to have an internal disulfide bond. {ECO:0000305|PubMed:3818612}. reclassified-function A9LIW2 ERD4 Brassica juncea (Indian mustard) (Sinapis juncea) 3707 CSC1-like protein ERD4 (Protein EARLY-RESPONSIVE TO DEHYDRATION STRESS 4) Was originally thought to possess 2 RRM (RNA recognition motif) domains and to bind RNA (PubMed:22431979). It seems to be in disagreement with the supposed ion transporter function. {ECO:0000305|PubMed:22431979}. reclassified-function P80301 Brassica napus (Rape) 3708 Defensin-like protein 4 (RTI) (Trypsin inhibitor) Was initially thought to be a protease inhibitor. {ECO:0000305|PubMed:8143882}. reclassified-function Q45296 enc Brevibacterium linens 1703 Type 1 encapsulin shell protein (Linocin M18) (M18 encapsulin) Was originally thought to be a bacteriocin (PubMed:7986050); it has since been shown this is not the case (PubMed:19172747). {ECO:0000269|PubMed:19172747, ECO:0000269|PubMed:7986050}. reclassified-function Q2YJN7 dapB Brucella abortus (strain 2308) 359391 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q57E96 dapA Brucella abortus biovar 1 (strain 9-941) 262698 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q576R4 dapB Brucella abortus biovar 1 (strain 9-941) 262698 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8YG60 dapA Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M) 224914 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8YDC8 dapB Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M) 224914 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5VPI5 dapA Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) 444178 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8G1R0 dapA Brucella suis biovar 1 (strain 1330) 204722 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8FV07 dapB Brucella suis biovar 1 (strain 1330) 204722 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8D8P8 dapA Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A) 563178 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8D8U7 dapB Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A) 563178 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P57197 dapA Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) 107806 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P57246 dapB Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) 107806 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8D702 dapA Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7) 561501 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8D751 dapB Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7) 561501 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q89AY0 dapA Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) 224915 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P59474 dapB Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) 224915 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q058B1 dapA Buchnera aphidicola subsp. Cinara cedri (strain Cc) 372461 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q057Y0 dapB Buchnera aphidicola subsp. Cinara cedri (strain Cc) 372461 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8KA24 dapA Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) 198804 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8K9Z5 dapB Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) 198804 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0BIB8 dapB Burkholderia ambifaria (strain ATCC BAA-244 / DSM 16087 / CCUG 44356 / LMG 19182 / AMMD) (Burkholderia cepacia (strain AMMD)) 339670 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1YT08 dapB Burkholderia ambifaria (strain MC40-6) 398577 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B4EEW4 dapB Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)) 216591 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A0K4H7 dapB Burkholderia cenocepacia (strain HI2424) 331272 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q39BA7 Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383) 482957 Putative hydrolase Bcep18194_B0137 (EC 3.-.-.-) (UGL) Was originally thought to be a ureidoglycolate lyase (UGL) but several lines of evidence argue against a physiological role of this gene in ureidoglycolate metabolism: (i) experimentally characterized homologs have an established role in the metabolism of 4-hydroxyphenylacetate; (ii) the gene and its homologs are never observed in purine degradation clusters; (iii) in Burkholderia, genes encoding bona fide ureidoglycolate lyase (allA) are present immediately downstream allantoicase, the gene involved in the formation of ureidoglycolate from allantoate. {ECO:0000305|PubMed:24107613}. reclassified-function Q39JM8 dapB Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383) 482957 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q62H17 dapB Burkholderia mallei (strain ATCC 23344) 243160 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A2S5J7 dapB Burkholderia mallei (strain NCTC 10229) 412022 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3MPI2 dapB Burkholderia mallei (strain NCTC 10247) 320389 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1V0H0 dapB Burkholderia mallei (strain SAVP1) 320388 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A9AHB2 dapB Burkholderia multivorans (strain ATCC 17616 / 249) 395019 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1BZ73 dapB Burkholderia orbicola (strain AU 1054) 331271 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1JVG6 dapB Burkholderia orbicola (strain MC0-3) 406425 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3NZB9 dapB Burkholderia pseudomallei (strain 1106a) 357348 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3JNM7 dapB Burkholderia pseudomallei (strain 1710b) 320372 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3NDK8 dapB Burkholderia pseudomallei (strain 668) 320373 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q63QT3 dapB Burkholderia pseudomallei (strain K96243) 272560 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2SZ94 dapB Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264) 271848 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A4JBH8 dapB Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia (strain R1808)) 269482 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q60LW7 elpc-3 Caenorhabditis briggsae 6238 Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function Q60ZM2 elpc-4 Caenorhabditis briggsae 6238 Elongator complex protein 4 (ELP4) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}. reclassified-function Q23651 elpc-3 Caenorhabditis elegans 6239 Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function Q18195 elpc-4 Caenorhabditis elegans 6239 Elongator complex protein 4 (ELP4) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}. reclassified-function P34405 flp-23 Caenorhabditis elegans 6239 FMRFamide-like neuropeptide 23 [Cleaved into: VVGQQDFLRF-amide] The protein was originally predicted to include a TKFQDFLRF-amide peptide, although TKFQDFLRF-amide has no effect on the activity of dissected pharyngeal myogenic muscle system. {ECO:0000305|PubMed:16187307}. reclassified-function P90953 hlh-34 Caenorhabditis elegans 6239 Helix-loop-helix 34 Was reported to probably be expressed in the AVJL and AVJR neurons (PubMed:22768843). However, this has been claimed to be an anatomical error and that expression is restricted to the AVH neurons (PubMed:34604715). {ECO:0000269|PubMed:22768843, ECO:0000269|PubMed:34604715}. reclassified-function Q17990 lite-1 Caenorhabditis elegans 6239 High-energy light unresponsive protein 1 Was initially thought to play a role in the gustatory response (PubMed:18687026). However, it was later shown that it acts as a photoreceptor for short wavelength (UV) light (PubMed:27863243). {ECO:0000269|PubMed:18687026, ECO:0000269|PubMed:27863243}. reclassified-function P34692 phaf-1 Caenorhabditis elegans 6239 Phagosome assembly factor phaf-1 Was originally thought to be lin-10. {ECO:0000305|PubMed:2159938}. reclassified-function Q9GYI4 psr-1 Caenorhabditis elegans 6239 Bifunctional arginine demethylase and lysyl-hydroxylase psr-1 (EC 1.14.11.-) (Phosphatidylserine receptor 1) Was initially thought to constitute the phosphatidylserine receptor, a receptor that mediates recognition of phosphatidylserine, a specific marker only present at the surface of apoptotic cells, and participates in apoptotic cell phagocytosis. However, some results strongly suggest that it does not constitute the receptor for phosphatidylserine and is not involved in apoptotic cell removal. {ECO:0000305}. reclassified-function G5EF68 taf-5 Caenorhabditis elegans 6239 Transcription initiation factor TFIID subunit 5 (TBP-associated transcription factor family member taf-5) The gene name for this protein was previously taf-4 (PubMed:11963920). The nomenclature was changed in PMID:11963920 and so readers should take care to avoid confusion (PubMed:11963920). {ECO:0000303|PubMed:11963920}. reclassified-function Q17361 usp-14 Caenorhabditis elegans 6239 Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) (Deubiquitinating enzyme 14) (Ubiquitin thioesterase 14) (Ubiquitin-specific-processing protease 14) Was originally (Ref.1) thought to be a queuine tRNA-ribosyltransferase. {ECO:0000305}. reclassified-function Q8RBI5 dapA Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis) 273068 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8RBI6 dapB Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis) 273068 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B9MRD1 dapA Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / KCTC 15123 / Z-1320) (Anaerocellum thermophilum) 521460 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4XJU0 dapA Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T 6331) 351627 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0A1C9CX56 CYC1 Camptotheca acuminata (Happy tree) 16922 (S)-8-oxocitronellyl enol synthase CYC1 (EC 1.3.1.122) (Cyclase 1) (Iridoid synthase) (ISY) Was originally thought to catalyze the entire reaction from (6E)-8-oxogeranial to nepetalactol including a cyclase step, but new results have shown that the cyclase is a different enzyme and this enzyme exclusively catalyzes a reduction step. {ECO:0000250|UniProtKB:K7WDL7}. reclassified-function A0A1C9CX66 CYC2 Camptotheca acuminata (Happy tree) 16922 (S)-8-oxocitronellyl enol synthase CYC2 (EC 1.3.1.122) (Cyclase 2) (Iridoid synthase) (ISY) Was originally thought to catalyze the entire reaction from (6E)-8-oxogeranial to nepetalactol including a cyclase step, but new results have shown that the cyclase is a different enzyme and this enzyme exclusively catalyzes a reduction step. {ECO:0000250|UniProtKB:K7WDL7}. reclassified-function A7ZDQ5 dapA Campylobacter concisus (strain 13826) 360104 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7ZB70 dapB Campylobacter concisus (strain 13826) 360104 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7GYB0 dapA Campylobacter curvus (strain 525.92) 360105 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7GWC2 dapB Campylobacter curvus (strain 525.92) 360105 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A0RP26 dapA Campylobacter fetus subsp. fetus (strain 82-40) 360106 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0RMR7 dapB Campylobacter fetus subsp. fetus (strain 82-40) 360106 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7I0Y0 dapA Campylobacter hominis (strain ATCC BAA-381 / DSM 21671 / CCUG 45161 / LMG 19568 / NCTC 13146 / CH001A) 360107 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7I316 dapB Campylobacter hominis (strain ATCC BAA-381 / DSM 21671 / CCUG 45161 / LMG 19568 / NCTC 13146 / CH001A) 360107 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5HUY6 dapA Campylobacter jejuni (strain RM1221) 195099 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5HWX1 dapB Campylobacter jejuni (strain RM1221) 195099 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5HUT1 dsbI Campylobacter jejuni (strain RM1221) 195099 Putative protein-disulfide oxidoreductase DsbI Was originally given the gene name dsbB; however this seems to belong to a different DsbB subfamily. {ECO:0000305}. reclassified-function Q5DNA5 pseC Campylobacter jejuni subsp. doylei (strain ATCC 49349 / DSM 104768 / CCUG 24567 / LMG 8803 / NCTC 11951 / IMVS 1141) 1408360 UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase (EC 2.6.1.92) Was originally thought to catalyze the transfer of the primary amino group of L-glutamate to C-4'' of UDP-4-keto-6-deoxy-GlcNAc (UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose) to form UDP-4-amino-4,6-dideoxy-GalNAc (UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-galactose) (PubMed:15790564). But the substrate and reaction product were misidentified, and it was later shown in another strain of C.jejuni (AC Q0P8W3) that this enzyme in fact forms UDP-4-amino-4,6-dideoxy-beta-L-AltNAc from UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose. {ECO:0000269|PubMed:15790564, ECO:0000305}. reclassified-function A7H443 dapA Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97) 360109 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7H1R4 dapB Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97) 360109 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9PPB4 dapA Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) 192222 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9PIT2 dapB Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) 192222 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0PA25 dsbI Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) 192222 Putative protein-disulfide oxidoreductase DsbI Was originally given the gene name dsbB; however this seems to belong to a different DsbB subfamily. {ECO:0000305}. reclassified-function A1VZF4 dapA Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) 354242 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1VXS5 dapB Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) 354242 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1VZK8 dsbI Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) 354242 Putative protein-disulfide oxidoreductase DsbI Was originally given the gene name dsbB; however this seems to belong to a different DsbB subfamily. {ECO:0000305}. reclassified-function A8FLL9 dapA Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) 407148 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8FJZ8 dapB Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) 407148 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B9KFX0 dapA Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060) 306263 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B9KDT6 dapB Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060) 306263 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P35521 CLNS1A Canis lupus familiaris (Dog) (Canis familiaris) 9615 Methylosome subunit pICln (Chloride channel, nucleotide sensitive 1A) (Chloride conductance regulatory protein ICln) (I(Cln)) Was originally thought to be a chloride channel. {ECO:0000305|PubMed:1313151}. reclassified-function P06857 PNLIPRP1 Canis lupus familiaris (Dog) (Canis familiaris) 9615 Inactive pancreatic lipase-related protein 1 (PL-RP1) Was originally thought to be the pancreatic lipase, but has been shown to have very low or undetectable lipase activity in vitro. {ECO:0000305|PubMed:9610393, ECO:0000305|PubMed:9726421}. reclassified-function Q9N2J1 UCP2 Canis lupus familiaris (Dog) (Canis familiaris) 9615 Dicarboxylate carrier UCP2 (Mitochondrial uncoupling protein 2) (UCP 2) (Solute carrier family 25 member 8) The role of UCP2/SLC25A8 in mitochondrial proton conductance is a matter of debate. It was initially suggested that it mediates proton leak that increases net proton conductance in response to ROS such as reactive alkenals generated during fatty acid oxidation in mitochondria. By lowering the proton motive force, it would provide for feedback control of mitochondrial ROS metabolism limiting extensive ROS production and protecting cells against oxidative stress. This activity and its potential regulation by ubiquinones and nucleotides was disputed by later studies, which failed to reproduce the effect on proton conductance under physiological conditions. Rather than 'uncoupling' the link between electron transfer and ATP synthesis, it may couple metabolite transport to proton flux to allow for optimal ATP turnover. {ECO:0000250|UniProtKB:P55851, ECO:0000250|UniProtKB:P70406}. reclassified-function Q01988 USP11 Canis lupus familiaris (Dog) (Canis familiaris) 9615 Ubiquitin carboxyl-terminal hydrolase 11 (EC 3.4.19.12) (Deubiquitinating enzyme 11) (Ubiquitin thioesterase 11) (Ubiquitin-specific-processing protease 11) Was originally thought to be apomucin (also known as mucin core protein; CTM-A). {ECO:0000305|PubMed:1282002}. reclassified-function Q3ACY8 dapB Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901) 246194 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function K7WDL7 Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) 4058 (S)-8-oxocitronellyl enol synthase (EC 1.3.1.122) (Iridoid synthase) (ISY) Was originally thought to catalyze the entire reaction from (6E)-8-oxogeranial to nepetalactol including a cyclase step (PubMed:23172143). New results have shown that the cyclase is a different enzyme and this enzyme exclusively catalyzes a reduction step (PubMed:30531909). {ECO:0000269|PubMed:30531909, ECO:0000305|PubMed:23172143}. reclassified-function Q9ZTK5 DAT Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) 4058 Deacetylvindoline O-acetyltransferase (EC 2.3.1.107) (Acetyl-coenzyme A:deacetylvindoline 4-O-acetyltransferase) Was originally purified as a heterodimer of the N- and C-terminal end of the DAT gene product, but the cleavage of DAT protein appears to be a purification artifact. {ECO:0000305|PubMed:2350183}. reclassified-function Q9A900 dapA Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus) 190650 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9A2L1 dapB Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus) 190650 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P15345 flaEY Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus) 190650 Regulatory protein FlaEY Was originally proposed to code for two separate adjacent ORFs, flaE and flaY. {ECO:0000305|PubMed:2648000}. reclassified-function P57044 ILK Cavia porcellus (Guinea pig) 10141 Scaffold protein ILK (ILK-1) (ILK-2) (Inactive integrin-linked kinase) (p59ILK) Was originally thought to act as a serine/threonine-protein kinase. Now thought to be a pseudokinase which does not have kinase activity and which functions solely as a scaffold protein. {ECO:0000250|UniProtKB:Q13418}. reclassified-function P37039 Por Cavia porcellus (Guinea pig) 10141 NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4) Was originally thought to originate from mouse. {ECO:0000305|PubMed:1420354}. reclassified-function P30098 TACR3 Cavia porcellus (Guinea pig) 10141 Neuromedin-K receptor (NKR) (NK-3 receptor) (NK-3R) (Neurokinin B receptor) (Tachykinin receptor 3) Was originally (PubMed:1315051) thought to be a kappa-type opioid receptor and to originate from human. PubMed:8947459 showed that it is a tachikinin receptor and was termed NK-4R. PubMed:11864635 shows that it is from guinea pig and is NK-3R. {ECO:0000305|PubMed:1315051}. reclassified-function B3PC19 dapA Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) 498211 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3IYU4 dapB Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides) 272943 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3J1R2 takP Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides) 272943 Alpha-keto acid-binding periplasmic protein TakP (Extracytoplasmic solute receptor protein TakP) (TRAP transporter alpha-keto acid-binding subunit P) (TRAP-T family sorbitol/mannitol transporter, periplasmic binding protein, SmoM) Was originally (Ref.1) annotated as coding for a sorbitol/mannitol-binding protein based solely on its position in the genome close to the smo operon encoding known sorbitol/mannitol catabolic genes. {ECO:0000305}. reclassified-function A4WNS1 dapA Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter sphaeroides) 349102 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4WWP7 dapB Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter sphaeroides) 349102 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3PNF3 dapB Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter sphaeroides) 349101 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B9KP40 dapB Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter sphaeroides) 557760 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q11JT7 dapA Chelativorans sp. (strain BNC1) 266779 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q11CB4 dapB Chelativorans sp. (strain BNC1) 266779 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5L5G7 dapA Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus) 218497 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5L5G4 dapB Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus) 218497 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q822H0 dapA Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC) (Chlamydophila caviae) 227941 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q822G7 dapB Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC) (Chlamydophila caviae) 227941 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q255G0 dapA Chlamydia felis (strain Fe/C-56) (Chlamydophila felis) 264202 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q255G3 dapB Chlamydia felis (strain Fe/C-56) (Chlamydophila felis) 264202 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q46407 ompA Chlamydia muridarum 83560 Major outer membrane porin (MOMP) Was originally thought to originate from Chlamydia trachomatis. {ECO:0000305|PubMed:8277858}. reclassified-function Q9PK33 dapA Chlamydia muridarum (strain MoPn / Nigg) 243161 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9PK30 dapB Chlamydia muridarum (strain MoPn / Nigg) 243161 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P75024 ompA Chlamydia muridarum (strain MoPn / Nigg) 243161 Major outer membrane porin (MOMP) Was originally (PubMed:1937036, PubMed:1718870) thought to originate from Chlamydia trachomatis. {ECO:0000305}. reclassified-function Q9Z6K9 dapA Chlamydia pneumoniae (Chlamydophila pneumoniae) 83558 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9Z6L2 dapB Chlamydia pneumoniae (Chlamydophila pneumoniae) 83558 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9XBF4 ompA Chlamydia pneumoniae (Chlamydophila pneumoniae) 83558 Major outer membrane porin (MOMP) Was originally thought to originate from Chlamydia psittaci. {ECO:0000305|PubMed:8125292}. reclassified-function Q3KLZ5 dapA Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13) 315277 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3KLZ2 dapB Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13) 315277 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O84366 dapA Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx) 272561 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function O84369 dapB Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx) 272561 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0B888 rplF Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu) 471472 Large ribosomal subunit protein uL6 (50S ribosomal protein L6) Was originally (PubMed:3312167) thought to be an outer membrane binding protein (chlanectin). The sequence was incorrect due to a cloning artifact. {ECO:0000305|PubMed:3312167}. reclassified-function B8LIX8 IFT25 Chlamydomonas reinhardtii (Chlamydomonas smithii) 3055 Intraflagellar transport protein 25 (Flagellar-associated protein 232) Was initially classified as a member of the small heat shock family protein. However, it was later shown that it is not the case (PubMed:21505417). {ECO:0000305|PubMed:21505417}. reclassified-function B3QM33 dapA Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum) 517417 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B3QKY9 dapB Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum) 517417 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8KC06 dapA Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum) 194439 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8KBD8 dapB Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum) 194439 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3APU0 dapA Chlorobium chlorochromatii (strain CaD3) 340177 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3APL9 dapB Chlorobium chlorochromatii (strain CaD3) 340177 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B3EH29 dapA Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330) 290315 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B3EG74 dapB Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330) 290315 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3B2G4 dapA Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon luteolum) 319225 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3B619 dapB Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon luteolum) 319225 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B3EMS4 dapA Chlorobium phaeobacteroides (strain BS1) 331678 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B3EN04 dapB Chlorobium phaeobacteroides (strain BS1) 331678 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1BE04 dapA Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430) 290317 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1BI80 dapB Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430) 290317 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A4SG05 dapA Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris vibrioformis (strain DSM 265)) 290318 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4SD53 dapB Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris vibrioformis (strain DSM 265)) 290318 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B3QUT2 dapA Chloroherpeton thalassium (strain ATCC 35110 / GB-78) 517418 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B3QYM8 dapB Chloroherpeton thalassium (strain ATCC 35110 / GB-78) 517418 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P93762 HOX Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa) 2769 Hexose oxidase (HOx) (EC 1.1.3.5) [Cleaved into: Hexose oxidase, 40 kDa form; Hexose oxidase, 29 kDa form] Was initially reported to use Cu(2+) as a cofactor (PubMed:4708670). However, cofactor composition could not be confirmed later (PubMed:9108257), and the discrepancies in the reported characteristics of the enzyme were suggested to originate from the characterization of a contaminating protein in PubMed:4708670. {ECO:0000305|PubMed:4708670, ECO:0000305|PubMed:9108257}. reclassified-function P23061 SPH Choristoneura biennis entomopoxvirus (CbEPV) 10288 Spindolin (Spheroidin) (p50) Was originally thought to be a spheroidin. {ECO:0000305|PubMed:2327073}. reclassified-function A0LZ30 dapA Christiangramia forsetii (strain DSM 17595 / CGMCC 1.15422 / KT0803) (Gramella forsetii) 411154 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0LZI4 dapB Christiangramia forsetii (strain DSM 17595 / CGMCC 1.15422 / KT0803) (Gramella forsetii) 411154 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7NX34 dapB Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / CCUG 213 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / MK) 243365 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1QTP6 dapA Chromohalobacter israelensis (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11) (Chromohalobacter salexigens) 290398 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q1QSX7 dapB Chromohalobacter israelensis (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11) (Chromohalobacter salexigens) 290398 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B5EGX4 dapA Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem) (Geobacter bemidjiensis) 404380 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B5EGX3 dapB Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem) (Geobacter bemidjiensis) 404380 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8ALS4 dapB Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) 290338 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5CSN2 dapB Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382) 443906 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0RGX5 dapB Clavibacter sepedonicus (Clavibacter michiganensis subsp. sepedonicus) 31964 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P16154 tcdA Clostridioides difficile (Peptoclostridium difficile) 1496 Toxin A (EC 3.4.22.-) [Cleaved into: Glucosyltransferase TcdA (EC 2.4.1.-)] Host HSP90B1/gp96 was initially identified as a possible receptor for TcdA (PubMed:18411291). However, as HSP90B1/gp96 localizes in the endoplasmic reticulum and not at the cell membrane, it probably does not act as a receptor for TcdA. {ECO:0000269|PubMed:18411291, ECO:0000305}. reclassified-function Q97GI9 dapA1 Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) 272562 4-hydroxy-tetrahydrodipicolinate synthase 1 (HTPA synthase 1) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q97D80 dapA2 Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) 272562 4-hydroxy-tetrahydrodipicolinate synthase 2 (HTPA synthase 2) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q97GI8 dapB Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) 272562 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2V5A9 dapB Clostridium botulinum (strain Alaska E43 / Type E3) 508767 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2TS69 dapB Clostridium botulinum (strain Eklund 17B / Type B) 935198 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C1FUH3 orfX3 Clostridium botulinum (strain Kyoto / Type A2) 536232 Protein OrfX3 Was originally thought to be a membrane protein. Crystallography of an ortholog in complex with OrfX1 shows this is not the case (By similarity). {ECO:0000250|UniProtKB:A0A5P3XKL3, ECO:0000305|PubMed:29067689}. reclassified-function A0PZM3 dapA Clostridium novyi (strain NT) 386415 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0PZM2 dapB Clostridium novyi (strain NT) 386415 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8XJ56 dapA Clostridium perfringens (strain 13 / Type A) 195102 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8XJ55 dapB Clostridium perfringens (strain 13 / Type A) 195102 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0TP55 dapA Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) 195103 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q0TP54 dapB Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) 195103 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0SRS5 dapA Clostridium perfringens (strain SM101 / Type A) 289380 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q0SRS4 dapB Clostridium perfringens (strain SM101 / Type A) 289380 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P13604 adh1 Clostridium saccharobutylicum 169679 NADPH-dependent butanol dehydrogenase (BDH) (EC 1.1.1.-) Was originally thought to originate from C.acetobutylicum. {ECO:0000305|PubMed:2673928}. reclassified-function P15704 eglA Clostridium saccharobutylicum 169679 Endoglucanase (EC 3.2.1.4) (Cellulase) (Endo-1,4-beta-glucanase) Was originally thought to originate from C.acetobutylicum. {ECO:0000305|PubMed:3389820}. reclassified-function P53578 fixB Clostridium saccharobutylicum 169679 Protein FixB Was originally thought to originate from C.acetobutylicum. {ECO:0000305}. reclassified-function P18855 floX Clostridium saccharobutylicum 169679 Flavodoxin Was originally thought to originate from C.acetobutylicum. {ECO:0000305}. reclassified-function P10656 glnA Clostridium saccharobutylicum 169679 Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Glutamine synthetase I alpha) (GSI alpha) Was originally thought to originate from C.acetobutylicum. {ECO:0000303|PubMed:1981087, ECO:0000303|PubMed:2891680}.; reclassified-function Q45831 regA Clostridium saccharobutylicum 169679 HTH-type transcriptional regulator RegA Was originally thought to originate from C.acetobutylicum. {ECO:0000305}. reclassified-function P17137 xynB Clostridium saccharobutylicum 169679 Endo-1,4-beta-xylanase (Xylanase) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase) Was originally thought to originate from C.acetobutylicum. {ECO:0000305|PubMed:2336398}. reclassified-function P07914 baiA1; baiA3 Clostridium scindens (strain JCM 10418 / VPI 12708) 29347 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase 1/3 (EC 1.1.1.395) (3alpha-hydroxysteroid dehydrogenase 1/3) (3alpha-HSDH 1/3) (Bile acid-inducible protein BaiA1) (Bile acid-inducible protein BaiA3) Was originally named bile acid 7-dehydroxylase (PubMed:3549693). In fact, the 7-dehydroxylation process is catalyzed by multiple enzymes. {ECO:0000305}. reclassified-function P19410 baiCD Clostridium scindens (strain JCM 10418 / VPI 12708) 29347 3-oxocholoyl-CoA 4-desaturase (EC 1.3.1.115) (Bile acid-inducible operon protein C) (Bile acid-inducible operon protein CD) (Bile acid-inducible operon protein D) Was originally thought to be the product of two separate ORFs, baiC and baiD. {ECO:0000305|PubMed:2254270}. reclassified-function Q891S3 dapA Clostridium tetani (strain Massachusetts / E88) 212717 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q891S2 dapB Clostridium tetani (strain Massachusetts / E88) 212717 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q39535 DAPA Coix lacryma-jobi (Job's tears) 4505 4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q47YI6 dapB Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) 167879 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P69752 Conus ermineus (Agate cone) (Chelyconus ermineus) 55423 Delta-conotoxin-like EVIB (Delta-EVIB) (Delta-EVIA) This toxin was originally named EVIA. As another delta-conotoxin was named EVIA in 2004 for which structural studies were carried out, the present toxin was renamed here EVIB. {ECO:0000305}. reclassified-function Q06100 Cgl1 Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata) 5346 Galectin-1 (Cgl-I) (Galectin I) Was originally thought to be an endonuclease subunit. {ECO:0000305|PubMed:1452023}. reclassified-function P21820 Coptis japonica (Japanese goldthread) 3442 Triosephosphate isomerase, cytosolic (TIM) (Triose-phosphate isomerase) (EC 5.3.1.1) Was originally thought to be (S)-tetrahydro-berberine oxidase (EC 1.3.3.8). {ECO:0000305|PubMed:2463630}. reclassified-function C3PH04 dapA Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 / CN-1) (Corynebacterium nigricans) 548476 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C3PH06 dapB Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 / CN-1) (Corynebacterium nigricans) 548476 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6NGP4 dapA Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) 257309 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6NGP2 dapB Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) 257309 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8RQM8 dapA Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) 196164 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8RQN0 dapB Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) 196164 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P19808 dapA Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) 196627 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P40110 dapB Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) 196627 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A4QEY0 dapB Corynebacterium glutamicum (strain R) 340322 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q4JV64 dapA Corynebacterium jeikeium (strain K411) 306537 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q4JV62 dapB Corynebacterium jeikeium (strain K411) 306537 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1VDC4 dapA Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109) 504474 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1VDC2 dapB Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109) 504474 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q91365 CEP162 Coturnix coturnix (Common quail) (Tetrao coturnix) 9091 Centrosomal protein of 162 kDa (Cep162) (Protein quail neuroretina 1) Was initially thought to regulate chromosome segregation and mitotic spindle assembly (PubMed:16302001). However, it was later shown that its absence neither affect mitosis nor centriole duplication. {ECO:0000305|PubMed:16302001}. reclassified-function B6J2F3 dapB Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)) 434923 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B6J4U6 dapB Coxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)) 434924 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A9KFS0 dapA Coxiella burnetii (strain Dugway 5J108-111) 434922 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A9KC25 dapB Coxiella burnetii (strain Dugway 5J108-111) 434922 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A9NDT3 dapA Coxiella burnetii (strain RSA 331 / Henzerling II) 360115 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A9NA71 dapB Coxiella burnetii (strain RSA 331 / Henzerling II) 360115 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q83CA6 dapA Coxiella burnetii (strain RSA 493 / Nine Mile phase I) 227377 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P24703 dapB Coxiella burnetii (strain RSA 493 / Nine Mile phase I) 227377 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7MP70 dapA Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) 290339 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7MI96 dapB Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) 290339 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P0CV92 QPCT Crotalus atrox (Western diamondback rattlesnake) 8730 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (By similarity). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000250|UniProtKB:Q16769}. reclassified-function Q1LJ29 dapB Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) 266264 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0K705 dapB Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) 381666 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q46XD7 dapB Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator (strain JMP 134)) 264198 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q46M57 tfdR Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator (strain JMP 134)) 264198 HTH-type transcriptional regulator TdfR The products of the genes tfdR and tfdS were originally thought to be identical but in fact they differ by one residue (amino acid 264 which is Asp in tfdR and Ala in tfdS). {ECO:0000305}. reclassified-function Q46M54 tfdS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator (strain JMP 134)) 264198 HTH-type transcriptional regulator TfdS The products of the genes tfdR and tfdS were originally thought to be identical but in fact they differ by one residue (amino acid 264 which is Asp in tfdR and Ala in tfdS). {ECO:0000305}. reclassified-function B3R6R4 dapB Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)) 977880 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6AA18 dapA Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium acnes) 267747 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6A7P7 dapB Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium acnes) 267747 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P31171 preA Cyanophora paradoxa 2762 Prenyl transferase (EC 2.5.1.-) Was originally called crtE. {ECO:0000305|PubMed:1711042}. reclassified-function B8HYL7 dapA Cyanothece sp. (strain PCC 7425 / ATCC 29141) 395961 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8HRK9 dapB Cyanothece sp. (strain PCC 7425 / ATCC 29141) 395961 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q11VI2 dapA Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465) 269798 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5U3U4 cdadc1 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 dCTP deaminase (EC 3.5.4.13) (Cytidine and dCMP deaminase domain-containing protein 1) (Deoxycytidine triphosphate deaminase) (Testis development protein NYD-SP15) CDADC1 was initially reported to exhibit cytidine deaminase activity (By similarity). However, subsequent studies demonstrated that it specifically deaminates dCTP, with no activity toward cytidine or deoxycytidine. The initial attribution may have been an artifact of using partially purified recombinant protein. While one study reported weak activity on dCMP, another failed to detect any dCMP deamination (By similarity). {ECO:0000250|UniProtKB:Q9BWV3}. reclassified-function Q6NYP8 eef1akmt1 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 EEF1A lysine methyltransferase 1 (EC 2.1.1.-) (N(6)-adenine-specific DNA methyltransferase 2) (Protein-lysine N-methyltransferase n6amt2) Was originally thought to be an N(6)-adenine-specific DNA methyltransferase based on primary sequence and predicted secondary structure. {ECO:0000250|UniProtKB:P53200}. reclassified-function Q05AM5 elp2 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Elongator complex protein 2 (ELP2) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q6IA86}. reclassified-function Q5RIC0 elp3 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function Q566Y1 elp4 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Elongator complex protein 4 (ELP4) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}. reclassified-function A1A5V9 elp5 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Elongator complex protein 5 (Dermal papilla-derived protein 6 homolog) (Retinoic acid-induced protein 12) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q8TE02}. reclassified-function Q0P424 elp6 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Elongator complex protein 6 (Protein TMEM103) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q0PNE2}. reclassified-function F1QCV2 hdac10 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Polyamine deacetylase HDAC10 (EC 3.5.1.48) (EC 3.5.1.62) (Histone deacetylase 10) Originally thought to be a histone deacetylase and shown in vitro to have this activity (By similarity). Has also been shown to be involved in MSH2 deacetylation (By similarity). However, protein deacetylase activity is a matter of debate, as 3D structure analysis shows that a glutamate gatekeeper and a sterically constricted active site confer specificity for N(8)-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Supporting this observation, has been shown to exhibit only very low activity, if any, towards acetyl-lysine peptide substrates (By similarity). {ECO:0000250|UniProtKB:Q969S8}. reclassified-function Q6PFM0 jmjd6 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR) (zfpsr) Was initially thought to constitute the phosphatidylserine receptor, a receptor that mediates recognition of phosphatidylserine, a specific marker only present at the surface of apoptotic cells, and participates in apoptotic cell phagocytosis. However, some results strongly suggest that it does not constitute the receptor for phosphatidylserine and is not involved in apoptotic cell removal. {ECO:0000305}. reclassified-function Q8AXB3 kdrl Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Vascular endothelial growth factor receptor kdr-like (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Kinase insert domain receptor-A) (Kinase insert domain receptor-like) (Protein-tyrosine kinase receptor flk-1) (Vascular endothelial growth factor receptor 4) (VEGFR-4) Was originally thought to be an ortholog of KDR, but PubMed:18516225 has shown that it represents a fourth vertebrate vascular endothelial growth factor receptor (VEGFR) that is not present in eutherian mammals (marsupials and placental mammals). {ECO:0000305}. reclassified-function Q9DGE0 map2k6 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (Mitogen-activated protein kinase kinase 3) (zMKK3) Was originally thought to be a Map2k3 protein but sequence analysis shows closer similarity to the Map2k6 proteins. {ECO:0000305, ECO:0000305|PubMed:10995439}. reclassified-function Q6P0D7 mpp7 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 MAGUK p55 subfamily member 7 (Protein humpback) Was originally thought to be the ortholog of mammalian DLG3. {ECO:0000305|PubMed:10446262}. reclassified-function Q5U403 mvd Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Mevalonate (diphospho)decarboxylase) (MDDase) (Mevalonate pyrophosphate decarboxylase) Was originally thought to be located in the peroxisome. However, was later shown to be cytosolic. {ECO:0000250|UniProtKB:P53602}. reclassified-function C5H5C4 notum1a Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Palmitoleoyl-protein carboxylesterase notum1a (EC 3.1.1.98) The molecular function of NOTUM family protein has remained unclear for many years. It was initially thought to hydrolyze glycosaminoglycan (GAG) chains of glypicans, thereby affecting glypicans ability to interact with Wnt ligands. It was later reported to trigger glypican shedding, by mediating cleavage of their GPI-anchor (PubMed:22669824). It was finally shown that it requires glypicans to suppress Wnt signaling, but does not cleave their GPI-anchor. It acts by mediating depalmitoleoylation of WNT proteins, impairing WNT binding to frizzled receptors. {ECO:0000269|PubMed:22669824, ECO:0000305}. reclassified-function P35359 rho Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Rhodopsin Was originally (PubMed:8327475, PubMed:8924413) thought to be an ultraviolet-sensitive opsin present in short single cones. {ECO:0000305}. reclassified-function Q7SXS7 setd3 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Actin-histidine N-methyltransferase (EC 2.1.1.85) (Protein-L-histidine N-tele-methyltransferase) (SET domain-containing protein 3) Was initially reported to have histone methyltransferase activity and methylate 'Lys-36' of histone H3 (H3K36me) (PubMed:21307598). However, this conclusion was based on mass spectrometry data wherin mass shifts were inconsistent with a bona fide methylation event and the histone methyltransferase activity could not be confirmed (By similarity). {ECO:0000250|UniProtKB:Q86TU7, ECO:0000269|PubMed:21307598}. reclassified-function Q1ECV4 ttll3 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Tubulin monoglycylase TTLL3 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 3) TTLL3 and TTLL8 monoglycylase-mediated glycylation of tubulin was initially reported to play a role in ependymal motile ciliary maintenance (By similarity). However, contradictory results were later observed (By similarity). {ECO:0000250|UniProtKB:A4Q9E5}. reclassified-function B8A5Y1 znf488 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Zinc finger protein 488 (EC 2.1.1.-) Was originally named prdm8 but the gene name was later changed to znf488 in recognition of the fact that it is an ortholog of mammalian ZNF488 as supported by synteny and phylogenetics. In non-mammalian gnathostomes, znf488 has an N-terminal SET domain and C-terminal zinc fingers similar to PRDM8 while mammalian ZNF488 has lost the N-terminal SET domain but retains the C-terminal zinc fingers. {ECO:0000305}. reclassified-function A6H8T7 zte25 Danio rerio (Zebrafish) (Brachydanio rerio) 7955 Cytosolic carboxypeptidase 2 (EC 3.4.17.-) (ATP/GTP-binding protein-like 2) (Protein deglutamylase CCP2) (Testis-expressed protein 25) Was initially shown to catalyze the removal of carboxy-terminus tyrosine from alpha-tubulin (By similarity). However, later studies did not identified any detyrosinase or deglycylase activities from the carboxy-terminus of tubulin (By similarity). {ECO:0000250|UniProtKB:Q5U5Z8, ECO:0000250|UniProtKB:Q8CDK2}.; reclassified-function P37706 RRF Daucus carota (Wild carrot) 4039 Ribosome-recycling factor, chloroplastic (RRF) (Nuclear located protein D2) (Ribosome-releasing factor, chloroplastic) Was originally (Ref.1) submitted as a nuclear protein when it seems to be chloroplastic (By similarity with the spinach sequence). {ECO:0000305}. reclassified-function Q47HS9 dapA Dechloromonas aromatica (strain RCB) 159087 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q47HI9 dapB Dechloromonas aromatica (strain RCB) 159087 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5FQT5 dapA Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1) 216389 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5FQT3 dapB Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1) 216389 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3Z7V3 dapA Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195) (Dehalococcoides ethenogenes (strain 195)) 243164 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3Z7V5 dapB Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195) (Dehalococcoides ethenogenes (strain 195)) 243164 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3ZXV3 dapA Dehalococcoides mccartyi (strain CBDB1) 255470 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3ZXV5 dapB Dehalococcoides mccartyi (strain CBDB1) 255470 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9RRB6 slpA Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) 243230 Outer membrane protein SlpA Was originally thought to be a major constituent of the S-layer. However, structural and deletion mutant studies showed that SlpA is an outer membrane protein and is not an integral part of the S-layer (PubMed:35943982). {ECO:0000269|PubMed:35943982, ECO:0000305|PubMed:16946272, ECO:0000305|PubMed:26074883}. reclassified-function Q46495 dfx Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14) 644282 Desulfoferrodoxin (Dfx) (EC 1.15.1.2) (Superoxide reductase) (SOR) Was originally thought to be a rubredoxin oxidoreductase. {ECO:0000305|PubMed:8955290}. reclassified-function B8FQZ3 dapB Desulfitobacterium hafniense (strain DSM 10664 / DCB-2) 272564 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q24UK0 dapB Desulfitobacterium hafniense (strain Y51) 138119 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q93PS3 xsc Desulfonispora thiosulfatigenes 83661 Sulfoacetaldehyde acetyltransferase (EC 2.3.3.15) Was originally thought to be a sulfo-lyase. {ECO:0000305|PubMed:11439112}. reclassified-function A4J5V5 dapA Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1) (Desulfotomaculum reducens) 349161 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1I383 dapA Desulforudis audaxviator (strain MP104C) 477974 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6AR63 dapA Desulfotalea psychrophila (strain LSv54 / DSM 12343) 177439 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6AR64 dapB Desulfotalea psychrophila (strain LSv54 / DSM 12343) 177439 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8J0P9 dapB Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB) 525146 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P22076 dfx Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB) 525146 Desulfoferrodoxin (Dfx) (EC 1.15.1.2) (Superoxide reductase) (SOR) Was originally thought to be a superoxide dismutase. {ECO:0000305|PubMed:10215854}. reclassified-function Q01770 hcp Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB) 525146 Hydroxylamine reductase (EC 1.7.99.1) (Hybrid-cluster protein) (HCP) (Prismane protein) Was originally thought to contain a 6Fe-6S cluster as indicated. {ECO:0000305|PubMed:1311311}. reclassified-function A5EXM4 dapA Dichelobacter nodosus (strain VCS1703A) 246195 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8KR69 glgX Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi) 556 Glycogen debranching enzyme (EC 3.2.1.196) (Limit dextrin alpha-1,6-maltotetraose-hydrolase) Was originally (PubMed:11554733) identified as an isoamylase despite of its little activity on glycogen, but was renamed as glycogen debranching enzyme due to the characterization of the flanking gene coding for the glycogen branching enzyme (PubMed:12480526). {ECO:0000305|PubMed:11554733, ECO:0000305|PubMed:12480526}. reclassified-function B5YEB2 dapB Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) 309799 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8E2S7 dapB Dictyoglomus turgidum (strain DSM 6724 / Z-1310) 515635 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q54WC0 WHR1 Dictyostelium discoideum (Social amoeba) 44689 Winged helix repair factor 1 (Inactive serine/threonine-protein kinase 19 homolog) Was originally reported to be a serine/threonine-protein kinase. However, later studies have shown that the protein does not have kinase activity and is involved in transcription-coupled nucleotide excision repair. {ECO:0000250|UniProtKB:P49842}. reclassified-function Q556W1 ddo-1; ddo-2 Dictyostelium discoideum (Social amoeba) 44689 D-amino-acid oxidase (DAAO) (DAMOX) (DAO) (EC 1.4.3.3) Was originally annotated as D-aspartate oxidase. {ECO:0000305}.; reclassified-function Q86H45 elp2 Dictyostelium discoideum (Social amoeba) 44689 Elongator complex protein 2 (ELP2) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q6IA86}. reclassified-function Q1ZXC6 elp3 Dictyostelium discoideum (Social amoeba) 44689 Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function Q54XS0 elp4 Dictyostelium discoideum (Social amoeba) 44689 Elongator complex protein 4 (ELP4) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}. reclassified-function Q9GPT6 elp6 Dictyostelium discoideum (Social amoeba) 44689 Elongator complex protein 6 The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q0PNE2}. reclassified-function Q8SSQ0 gefR Dictyostelium discoideum (Social amoeba) 44689 Ras guanine nucleotide exchange factor R (RasGEF domain-containing protein R) Was originally (PubMed:8793298) named RasGEFA, as it was the second RasGEF, after aimless, to be identified there. When aimless, aleA, was renamed gefA to make the nomenclature consistent and systematic, RasGEFA was renamed gefR. {ECO:0000305|PubMed:8793298}. reclassified-function Q54NM6 mocs1 Dictyostelium discoideum (Social amoeba) 44689 Molybdenum cofactor biosynthesis protein 1 [Includes: GTP 3',8-cyclase (EC 4.1.99.22) (MOCS1A) (Molybdenum cofactor biosynthesis protein A); Cyclic pyranopterin monophosphate synthase (EC 4.6.1.17) (MOCS1B) (Molybdenum cofactor biosynthesis protein C)] The C-terminus of mocs1a was previously believed to be thiocarboxylated, but it is now known not to be the case. {ECO:0000250|UniProtKB:Q9NZB8}. reclassified-function Q54YQ9 mvd Dictyostelium discoideum (Social amoeba) 44689 Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Mevalonate (diphospho)decarboxylase) (MDDase) (Mevalonate pyrophosphate decarboxylase) Was originally thought to be located in the peroxisome. However, was later shown to be cytosolic. {ECO:0000250|UniProtKB:P53602}. reclassified-function Q54B14 qpct Dictyostelium discoideum (Social amoeba) 44689 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (By similarity). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000250|UniProtKB:Q16769}. reclassified-function A8LKQ5 dapA Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12) 398580 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8LL24 dapB Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12) 398580 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9W138 Drosophila melanogaster (Fruit fly) 7227 Probable S-adenosyl-L-methionine-dependent methyltransferase (EC 2.1.1.-) (S-adenosylmethionine sensor upstream of mTORC1) (dSamtor) Was originally thought to function as a nutrient sensor for methionine, inhibiting the TORC1 signaling pathway in the absence of S-adenosyl-L-methionine-binding (PubMed:29123071, PubMed:35776786). Subsequent studies showed that this conclusion may have been based on RNAi-mediated experimental artifacts and instead ascribe this function to the methyltransferase unmet (PubMed:38514639). The involvement of Samtor in this process in Diptera, if any, remains unknown. {ECO:0000269|PubMed:29123071, ECO:0000269|PubMed:35776786, ECO:0000269|PubMed:38514639, ECO:0000305|PubMed:38514639}. reclassified-function Q27333 Alg3 Drosophila melanogaster (Fruit fly) 7227 Dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase Alg3 (EC 2.4.1.258) (Alpha-1,3-mannosyltransferase Alg3) (Asparagine-linked glycosylation protein 3 homolog) (Lethal(2)neighbor of tid protein) (Lethal(2)tumorous imaginal discs) (NOT45) (NOT56) Several mutations leading to tumorous growth of imaginal discs were originally thought to affect a neighboring gene encoded within the intron of the Alg3 gene. These mutations were subsequently shown to affect Alg3 (PubMed:29870719). This has led to some confusion in nomenclature. The intronic gene was originally named lethal(2)tumorous imaginal discs (l(2)tid) and Alg3 was named lethal(2)neighbor of tid (l(2)not). Some authors may refer to Alg3 as l(2)tid or l(2)not interchangeably. {ECO:0000269|PubMed:29870719, ECO:0000305, ECO:0000305|PubMed:9373138}. reclassified-function P14599 Appl Drosophila melanogaster (Fruit fly) 7227 Amyloid-beta-like protein Was originally (PubMed:2494667) thought to be vnd but further analysis (PubMed:2127912) has clearly shown that it corresponds to Appl. {ECO:0000305|PubMed:2127912, ECO:0000305|PubMed:2494667}. reclassified-function Q9VGK7 Elp1 Drosophila melanogaster (Fruit fly) 7227 Elongator complex protein 1 The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:O95163}. reclassified-function Q7K4B3 Elp2 Drosophila melanogaster (Fruit fly) 7227 Elongator complex protein 2 (Stat3-interacting protein homolog) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q6IA86}. reclassified-function Q9VQZ6 Elp3 Drosophila melanogaster (Fruit fly) 7227 Elongator complex protein 3 (EC 2.3.1.311) (EC 2.3.1.48) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function Q9VMQ7 Elp4 Drosophila melanogaster (Fruit fly) 7227 Elongator complex protein 4 The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}. reclassified-function Q24050 Elp5 Drosophila melanogaster (Fruit fly) 7227 Elongator complex protein 5 The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q8TE02}. reclassified-function Q9VFW4 Elp6 Drosophila melanogaster (Fruit fly) 7227 Elongator complex protein 6 The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q0PNE2}. reclassified-function Q8SWV6 Fic Drosophila melanogaster (Fruit fly) 7227 Protein adenylyltransferase Fic (dFic) (EC 2.7.7.108) (De-AMPylase Fic) (EC 3.1.4.-) Was initially thought to mediate AMPylation of Hsc70-3/BiP at 'Thr-366' (PubMed:25395623). However, it was later shown that it catalyzes AMPylation of Hsc70-3/BiP at 'Thr-518'. {ECO:0000269|PubMed:25395623, ECO:0000269|PubMed:29089387}. reclassified-function O17468 Hira Drosophila melanogaster (Fruit fly) 7227 Protein HIRA homolog (Protein sesame) (dHIRA) Was originally thought to be involved in protamine removal but this was shown to be incorrect in the subsequent published erratum. {ECO:0000269|Ref.10}. reclassified-function P25722 Hs2st Drosophila melanogaster (Fruit fly) 7227 Heparin sulfate O-sulfotransferase (dmHS-2OST) (EC 2.8.2.-) Was originally thought to be SD. {ECO:0000305|PubMed:1936954}. reclassified-function P29844 Hsc70-3 Drosophila melanogaster (Fruit fly) 7227 Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein homolog) (GRP-78 homolog) (Binding-immunoglobulin protein homolog) (BiP) (Heat shock 70 kDa protein cognate 3) (Heat shock protein cognate 72) Was initially thought to be AMPylated at 'Thr-366' by Fic (PubMed:25395623). However, it was later shown to be AMPylated at 'Thr-518'. {ECO:0000269|PubMed:25395623, ECO:0000269|PubMed:29089387}. reclassified-function Q9VW78 Ir76b Drosophila melanogaster (Fruit fly) 7227 Ionotropic receptor coreceptor Ir76b (Ionotropic receptor 76b) Was initially characterized as a conventional ionotropic receptor with sodium channel activity (PubMed:23766326). However, it was later shown that it rather acts as a coreceptor of conventional ionotropic receptors rather than a ion channel (PubMed:27982028). {ECO:0000269|PubMed:23766326, ECO:0000269|PubMed:27982028}. reclassified-function Q8IQF1 Mocs1 Drosophila melanogaster (Fruit fly) 7227 Molybdenum cofactor biosynthesis protein 1 [Includes: GTP 3',8-cyclase (EC 4.1.99.22) (MOCS1A) (Molybdenum cofactor biosynthesis protein A); Cyclic pyranopterin monophosphate synthase (EC 4.6.1.17) (MOCS1B) (Molybdenum cofactor biosynthesis protein C)] The C-terminus of Mocs1a was previously believed to be thiocarboxylated, but it is now known not to be the case. {ECO:0000250|UniProtKB:Q9NZB8}. reclassified-function Q9VUX3 Notum Drosophila melanogaster (Fruit fly) 7227 Palmitoleoyl-protein carboxylesterase NOTUM (EC 3.1.1.98) (Protein Notum) (Protein wingful) (dNOTUM) The molecular function of NOTUM has remained unclear for many years. It was initially thought to hydrolyze glycosaminoglycan (GAG) chains of glypicans, thereby affecting glypicans ability to interact with Wnt ligands (PubMed:12000788, PubMed:12015973). It was later reported to trigger glypican shedding, by mediating cleavage of their GPI-anchor (PubMed:15469839). However, while NOTUM specifically inhibit the Wnt signaling pathway, more pleiotropic effects would be expected from an enzyme affecting glypicans. It was finally shown that it requires glypicans to suppress Wnt signaling, but does not cleave their GPI-anchor (PubMed:25731175). It acts by mediating depalmitoleoylation of WNT proteins, impairing WNT binding to frizzled receptors (PubMed:25731175). {ECO:0000269|PubMed:25731175, ECO:0000305|PubMed:12000788, ECO:0000305|PubMed:12015973, ECO:0000305|PubMed:15469839}. reclassified-function Q9V7W1 PIG-V Drosophila melanogaster (Fruit fly) 7227 GPI mannosyltransferase 2 (EC 2.4.1.-) (GPI mannosyltransferase II) (GPI-MT-II) Was originally (PubMed:11102367) named veg. However, more thorough studies (PubMed:22575127) found that the veg phenotype does not map to this protein. It is still not known which gene corresponds to the veg phenotype. {ECO:0000305|PubMed:11102367, ECO:0000305|PubMed:22575127}. reclassified-function Q9NB04 Patj Drosophila melanogaster (Fruit fly) 7227 Patj homolog Was originally thought to be the Disks lost (Dlt) protein. However, PubMed:14667407 showed that it is not the case and renamed it Patj. This drastically changes the first conclusions drawn about its essential function, since the mutant used contained defects for another protein, which is now called Dlt. If its association with proteins involved in cell polarization complexes is clear, Patj is not essential since its absence apparently does not lead to important defects. {ECO:0000305}. reclassified-function P52295 Pen Drosophila melanogaster (Fruit fly) 7227 Importin subunit alpha (Karyopherin subunit alpha) (Pendulin) Was originally thought to be the overgrown hematopoietic organs-31 protein (OHO-31). {ECO:0000305|PubMed:7790349}. reclassified-function Q9VRQ9 QC Drosophila melanogaster (Fruit fly) 7227 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry. However, a recent study suggests a Zn(2+)-independent catalytic mechanism. {ECO:0000250|UniProtKB:B7QK46}. reclassified-function P25161 Rpn3 Drosophila melanogaster (Fruit fly) 7227 Probable 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome subunit S3) (Diphenol oxidase A2 component) (DOX-A2) (Regulatory particle non-ATPase 3) Was originally thought to be the diphenol oxidase A2 component involved in catecholamine metabolism, melanin formation, and sclerotization of the cuticle. {ECO:0000305|PubMed:1909680}. reclassified-function P91938 Trxr1 Drosophila melanogaster (Fruit fly) 7227 Thioredoxin reductase 1, mitochondrial (EC 1.8.1.9) Was originally thought to be a glutathione reductase. {ECO:0000305|PubMed:9056265}. reclassified-function P24350 acj6 Drosophila melanogaster (Fruit fly) 7227 Inhibitory POU protein (I-POU) (Abnormal chemosensory jump 6 protein) Was originally thought that the I-POU homeobox is unable to bind DNA because it lacks two N-terminal basic residues. {ECO:0000305|PubMed:1673230}.; reclassified-function Q86PD7 isoQC Drosophila melanogaster (Fruit fly) 7227 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Iso glutaminyl cyclase) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry. However, a recent study suggests a Zn(2+)-independent catalytic mechanism. {ECO:0000250|UniProtKB:B7QK46}. reclassified-function Q27237 l(2)tid Drosophila melanogaster (Fruit fly) 7227 DnaJ homolog l(2)tid, mitochondrial (Protein lethal(2)tumorous imaginal discs) (TID50) (TID56) Was originally thought to be the target of mutations leading to tumorous growth of imaginal discs, resulting in the name lethal(2)tumorous imaginal discs (l(2)tid). Encoded within the intron of the neighboring gene Alg3/lethal(2)neighbor of tid (l(2)not) (PubMed:7758246). The mutations leading to tumorous growth of imaginal discs were subsequently shown to affect the neighboring Alg3 gene (PubMed:29870719). Some authors may refer to Alg3 as l(2)tid or l(2)not interchangeably. {ECO:0000269|PubMed:29870719, ECO:0000269|PubMed:7758246, ECO:0000305, ECO:0000305|PubMed:7758246, ECO:0000305|PubMed:9373138}. reclassified-function P14083 lov Drosophila melanogaster (Fruit fly) 7227 Protein jim lovell (Protein TKR) (Tyrosine kinase-related) (dTKR) Was originally thought to be a kinase on the basis of weak and non-significant similarities. {ECO:0000305|PubMed:3428600}. reclassified-function B7Z0L8 moi Drosophila melanogaster (Fruit fly) 7227 Protein modigliani The naming of this protein has been complicated due to being expressed from a bicistronic mRNA. The upstream ORF (uORF) encodes moi/modigliani while the downstream ORF (dORF) encodes Tgs1 (PubMed:15684427). The gene was originally named Drosophila tat-like (DTL) for the RNA-binding activity of Tgs1, and the respective ORF products have been referred to as DTLu and DTLd. The ORF identifier CG31241 was originally assigned to the gene encompassing both products, which have since been given separate ORF identifiers (CG42350 for moi/modigliani and CG44890 for Tgs1). {ECO:0000269|PubMed:15684427, ECO:0000305, ECO:0000305|PubMed:15684427}. reclassified-function Q9VWV9 por Drosophila melanogaster (Fruit fly) 7227 Protein-serine O-palmitoleoyltransferase porcupine (EC 2.3.1.250) Was initially thought to mediate palmitoylation of Wnt proteins. It was later shown that instead it acts as a serine O-palmitoleoyltransferase that mediates the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins. {ECO:0000305}. reclassified-function P38979 sta Drosophila melanogaster (Fruit fly) 7227 Small ribosomal subunit protein uS2 (40S ribosomal protein SA) (K14) (Laminin receptor homolog) (Protein stubarista) Was originally thought to be a laminin receptor. {ECO:0000305}. reclassified-function P16241 vvl Drosophila melanogaster (Fruit fly) 7227 POU domain protein CF1A (Chorion factor 1A) (CF1-A) (Protein drifter) (Ventral veins lacking protein) Was originally thought to interact with acj6. {ECO:0000305|PubMed:1673230}. reclassified-function Q9V4M2 wech Drosophila melanogaster (Fruit fly) 7227 Protein wech (Protein dappled) Was originally termed dappled. {ECO:0000305|PubMed:8725239}. reclassified-function P09615 wg Drosophila melanogaster (Fruit fly) 7227 Protein wingless (Protein Wnt-1) (Protein int-1) (dInt-1) (dWnt-1) Was initially thought to be palmitoylated at Ser-239. It was later shown that it is palmitoleoylated. {ECO:0000305}. reclassified-function Q9U3V9 xmas Drosophila melanogaster (Fruit fly) 7227 Protein xmas Isoform A (xmas-2) and isoform B (xmas-1) were originally thought to be separate genes until a third longer transcript, isoform C, was identified that encompasses both ORFs and supports their existence as three alternatively spliced isoforms (PubMed:29779104). Although most of the functional information for this protein is attributed to isoform A/xmas-2 in the literature, it might also be relevant for isoform C and isoform B/xmas-1. {ECO:0000269|PubMed:29779104, ECO:0000305|PubMed:29779104}. reclassified-function Q290J8 Drosophila pseudoobscura pseudoobscura (Fruit fly) 46245 GPI mannosyltransferase 2 (EC 2.4.1.-) (GPI mannosyltransferase II) (GPI-MT-II) Was originally named veg by similarity to the D.melanogaster ortholog. However, it was later shown that the veg phenotype does not map to this protein. It is still not known which gene corresponds to the veg phenotype. {ECO:0000305}. reclassified-function A4XSW1 dapA Ectopseudomonas mendocina (strain ymp) (Pseudomonas mendocina) 399739 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4XYF4 dapB Ectopseudomonas mendocina (strain ymp) (Pseudomonas mendocina) 399739 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C5B7A2 dapA Edwardsiella ictaluri (strain 93-146) 634503 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C5B7N2 dapB Edwardsiella ictaluri (strain 93-146) 634503 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3YSK1 dapA Ehrlichia canis (strain Jake) 269484 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3YRP2 dapB Ehrlichia canis (strain Jake) 269484 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2GG09 dapA Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas) 205920 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2GH22 dapB Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas) 205920 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5FFT0 dapB Ehrlichia ruminantium (strain Gardel) 302409 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5HAV4 dapB Ehrlichia ruminantium (strain Welgevonden) 254945 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P23802 Eleusine coracana (Indian finger millet) (Ragi) 4511 Non-specific lipid-transfer protein (LTP) (Alpha-amylase inhibitor I-2) Was originally (Ref.1) thought to be an inhibitor of alpha-amylase. {ECO:0000305}. reclassified-function Q05534 pacG Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) 227321 Protein pacG (Nonrepressible acid phosphatase regulator pacG) Was originally thought to be a phosphatase. {ECO:0000305|PubMed:7916713}. reclassified-function B1GYN1 dapA Endomicrobium trichonymphae 1408204 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q27651 PPi-PFK Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM) 294381 ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) Was originally thought to be a PPi-dependent phosphofructokinase (PubMed:8645233), but it has later been shown that the enzyme does not possess PPi-dependent activity and instead is an ATP-dependent phosphofructokinase (PubMed:11262402). {ECO:0000305|PubMed:11262402, ECO:0000305|PubMed:8645233}. reclassified-function A4W6E7 dapB Enterobacter sp. (strain 638) 399742 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P0DXF2 uvsW1 Enterobacteria phage T4 (Bacteriophage T4) 10665 Protein UvsW.1 Originally thought to be encoded as part of the preceding uvsW gene (PubMed:17092935). {ECO:0000269|PubMed:17092935}. reclassified-function Q836D1 dapA Enterococcus faecalis (strain ATCC 700802 / V583) 226185 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q834S6 dapB Enterococcus faecalis (strain ATCC 700802 / V583) 226185 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3Y316 Enterococcus faecium (strain ATCC BAA-472 / TX0016 / DO) 333849 D-mandelate dehydrogenase (D-ManDH2) (EC 1.1.1.379) ((R)-mandelate dehydrogenase) (2-keto acid reductase) (EC 1.1.1.-) Was originally thought to be a 2-ketopantoate reductase. However, in vitro studies have revealed a high rate of benzoylformate reduction, while showing the least activity with 2-ketopantoate. {ECO:0000269|PubMed:28327357}. reclassified-function P43440 ntpJ Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R) 768486 Potassium/sodium uptake protein NtpJ (K(+):Na(+) symporter) Was originally thought to be part of the V-type sodium ATP synthase. {ECO:0000305|PubMed:8157629}. reclassified-function P03184 Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) 10377 Packaging protein UL32 homolog Was originally thought to be an envelope glycoprotein. {ECO:0000305}. reclassified-function P68338 Equine herpesvirus 1 (strain AB1) (EHV-1) (Equine abortion virus) 10328 Packaging protein UL32 homolog (Glycoprotein 300) (GP300) Was originally [PubMed:1331295] thought to be an envelope glycoprotein. {ECO:0000305}. reclassified-function P69329 Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus) 31520 Packaging protein UL32 homolog Was originally thought to be an envelope glycoprotein. {ECO:0000305}. reclassified-function B2VE56 dapA Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99) 465817 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B2VH06 dapB Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99) 465817 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2N9J7 dapA Erythrobacter litoralis (strain HTCC2594) 314225 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P21312 Escherichia coli 562 Probable replication endonuclease from retron Ec67 (EC 3.1.-.-) (Protein ORF2 in retron Ec67) Was originally (PubMed:1701261) proposed to code for three separate adjacent ORFs, ORF2, ORF3 and ORFE. This has been reconstructed to match proteins in other enterobacteria. {ECO:0000305|PubMed:1701261}. reclassified-function Q9X2V7 mcjA Escherichia coli 562 Microcin J25 (MccJ25) (Class II lasso peptide) (Ribosomally synthesized and post-translationally modified peptide) (RiPP) Was originally thought to have a head-to-tail cyclic structure, but actually has a threaded side chain-to-backbone ring structure that is penetrated by the C-terminal tail in a noose-like motif. {ECO:0000305|PubMed:10092860}. reclassified-function B7LCL6 dapA Escherichia coli (strain 55989 / EAEC) 585055 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B7L4F3 dapB Escherichia coli (strain 55989 / EAEC) 585055 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1IWI1 dapA Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks) 481805 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1IRE5 dapB Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks) 481805 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1XBF6 dapB Escherichia coli (strain K12 / DH10B) 316385 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C4ZPV7 dapB Escherichia coli (strain K12 / MC4100 / BW2952) 595496 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P42912 agaI Escherichia coli (strain K12) 83333 Putative deaminase AgaI (EC 3.5.99.-) Was originally thought to be involved in the deamination and isomerization of D-galactosamine 6-phosphate to D-tagatofuranose 6-phosphate. {ECO:0000305|PubMed:23634833}. reclassified-function P26458 appB Escherichia coli (strain K12) 83333 Cytochrome bd-II ubiquinol oxidase subunit 2 (EC 7.1.1.3) (Cytochrome bd-II oxidase subunit II) Was originally thought not to translocate protons. {ECO:0000305|PubMed:19542282}. reclassified-function P26459 appC Escherichia coli (strain K12) 83333 Cytochrome bd-II ubiquinol oxidase subunit 1 (EC 7.1.1.3) (Cytochrome bd-II oxidase subunit I) Was originally thought not to translocate protons. {ECO:0000305|PubMed:19542282}. reclassified-function P27254 argK Escherichia coli (strain K12) 83333 GTPase ArgK (EC 3.6.5.-) (G protein chaperone) Was originally thought to be a membrane protein kinase involved in phosphorylation of the AO and LAO periplasmic-binding proteins (PubMed:9733684). However, its role needs to be reexamined. {ECO:0000305|PubMed:9733684}. reclassified-function P0AB98 atpB Escherichia coli (strain K12) 83333 ATP synthase subunit a (ATP synthase F0 sector subunit a) (F-ATPase subunit 6) Was originally proposed to be encoded from either Met-1 or Val-71 (PID CAA23521); it is now thought to start of Met-1. {ECO:0000305|PubMed:6278247}. reclassified-function P41407 azoR Escherichia coli (strain K12) 83333 FMN-dependent NADH:quinone oxidoreductase (EC 1.6.5.-) (Azo-dye reductase) (FMN-dependent NADH-azo compound oxidoreductase) (FMN-dependent NADH-azoreductase) (EC 1.7.1.17) Was originally thought to be an ACP phosphodiesterase, but ACP phosphodiesterase activity was not detected in vivo or in vitro in further analysis. {ECO:0000269|PubMed:11583992, ECO:0000305|PubMed:2168383}. reclassified-function P06610 btuE Escherichia coli (strain K12) 83333 Thioredoxin/glutathione peroxidase BtuE (EC 1.11.1.24) (EC 1.11.1.9) Part of the btuCED operon, and was originally thought to participate in the transport of vitamin B12, but it was shown later that it plays no essential role in vitamin B12 transport. {ECO:0000305|PubMed:2671656, ECO:0000305|PubMed:3528129}. reclassified-function P31572 caiB Escherichia coli (strain K12) 83333 L-carnitine CoA-transferase (EC 2.8.3.21) (Crotonobetainyl-CoA:carnitine CoA-transferase) Was originally thought to be an L-carnitine dehydratase. {ECO:0000305|PubMed:8188598}. reclassified-function P69791 chbA Escherichia coli (strain K12) 83333 PTS system N,N'-diacetylchitobiose-specific EIIA component (EIIA-Chb) (EIII-Chb) (IIIcel) (N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIA component) Was originally (PubMed:2179047) characterized as part of a cryptic cel operon for a cellobiose degradation system. The Cel+ phenotype is due to mutations making expression chitobiose-independent and altering the substrate specificity. {ECO:0000305|PubMed:2179047}. reclassified-function P69795 chbB Escherichia coli (strain K12) 83333 PTS system N,N'-diacetylchitobiose-specific EIIB component (EIIB-Chb) (IVcel) (N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIB component) (EC 2.7.1.196) Was originally (PubMed:2092358) characterized as part of a cryptic cel operon for a cellobiose degradation system. The Cel+ phenotype is due to mutations making expression chitobiose-independent and altering the substrate specificity. {ECO:0000305|PubMed:2092358}. reclassified-function P17334 chbC Escherichia coli (strain K12) 83333 PTS system N,N'-diacetylchitobiose-specific EIIC component (EIIC-Chb) (IIcel) (N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIC component) Was originally (PubMed:2179047) characterized as part of a cryptic cel operon for a cellobiose degradation system. The Cel+ phenotype is due to mutations making expression chitobiose-independent and altering the substrate specificity. {ECO:0000305|PubMed:2179047}. reclassified-function P17411 chbF Escherichia coli (strain K12) 83333 6-phospho-beta-glucosidase (EC 3.2.1.86) (Cellobiose-6-phosphate hydrolase) (Phospho-chitobiase) Was originally (PubMed:2179047) characterized as part of a cryptic cel operon for a cellobiose degradation system. The Cel+ phenotype is due to mutations making expression chitobiose-independent and altering the substrate specificity. {ECO:0000305|PubMed:2179047}. reclassified-function P37794 chbG Escherichia coli (strain K12) 83333 Chitooligosaccharide deacetylase ChbG (COD) (EC 3.5.1.105) (Chitin disaccharide deacetylase) (Chitobiose deacetylase) (Chitobiose-6P deacetylase) (Chitotriose deacetylase) (Chitotriose-6P deacetylase) Was originally characterized as part of a cryptic cel operon for a cellobiose degradation system (PubMed:2179047, PubMed:8121401). The Cel+ phenotype is due to mutations making expression chitobiose-independent and altering the substrate specificity. {ECO:0000305}. reclassified-function P37019 clcA Escherichia coli (strain K12) 83333 H(+)/Cl(-) exchange transporter ClcA (ClC-ec1) Was originally thought to be a voltage-gated ClC-type chloride channel. {ECO:0000305}. reclassified-function P0A6I6 coaD Escherichia coli (strain K12) 83333 Phosphopantetheine adenylyltransferase (EC 2.7.7.3) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (PPAT) Was originally thought to have an essential function in lipopolysaccharide biosynthesis. {ECO:0000305|PubMed:1577693}. reclassified-function P75960 cobB Escherichia coli (strain K12) 83333 NAD-dependent protein deacylase (EC 2.3.1.286) (Lysine delactylase) (Delactylase) (EC 2.3.1.-) (Regulatory protein SIR2 homolog) Was originally thought to be involved in cobalamin biosynthesis. {ECO:0000305}.; reclassified-function P67826 cutC Escherichia coli (strain K12) 83333 PF03932 family protein CutC (Putative copper homeostasis protein CutC) Was originally thought to be involved in copper homeostasis (PubMed:7635807), however, the copper sensitivity phenotype of the mutant was later shown to be due to the loss of MicL sRNA which leads to elevated Lpp levels (PubMed:25030700). Silent mutations in this protein that disrupt the promoter of micL are copper sensitive. {ECO:0000269|PubMed:25030700, ECO:0000269|PubMed:7635807}. reclassified-function P22255 cysQ Escherichia coli (strain K12) 83333 3'(2'),5'-bisphosphate nucleotidase CysQ (EC 3.1.3.7) (3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase) (3'-phosphoadenosine 5'-phosphate phosphatase) (PAP phosphatase) (DPNPase) Was originally thought to be an ammonium transport protein. {ECO:0000305|PubMed:1856684}. reclassified-function P0A6J5 dadA Escherichia coli (strain K12) 83333 D-amino acid dehydrogenase (EC 1.4.99.-) (D-alanine dehydrogenase) Was originally thought to be a heterodimer based on the purification of the enzyme first reported from E.coli B, but results of enzyme assays in PubMed:21378189 have indicated that DadA is solely responsible for the observed dehydrogenase activity. {ECO:0000305}. reclassified-function P0A6L2 dapA Escherichia coli (strain K12) 83333 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB (PubMed:20503968, PubMed:8993314). {ECO:0000305|PubMed:20503968, ECO:0000305|PubMed:8993314}. reclassified-function P04036 dapB Escherichia coli (strain K12) 83333 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction (PubMed:20503968). {ECO:0000305|PubMed:20503968}. reclassified-function P37349 dhaM Escherichia coli (strain K12) 83333 PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM (EC 2.7.1.121) (Dihydroxyacetone kinase subunit M) Was reported to be a protein deacetylase that removes acetyl groups on specific lysine residues in target proteins (PubMed:26716769). However, later experiments demonstrate that this protein does not have any protein deacetylase activity; the discrepancy observed seems to be due to contaminants having proteolytic activity (PubMed:29939131). {ECO:0000269|PubMed:26716769, ECO:0000269|PubMed:29939131}. reclassified-function P08555 dsdX Escherichia coli (strain K12) 83333 D-serine transporter DsdX An ORF called dsdC was originally assigned to the wrong DNA strand and thought to be a D-serine deaminase activator (PubMed:3275618). It was then resequenced and still thought to be 'dsdC', but this time to function as a D-serine permease (Ref.2). Another report showed that dsdC is another gene and that this sequence should be called dsdX (PubMed:7592420). It should also be noted that the C-terminal part of dsdX (from 338 onward) was also sequenced and was thought to be a separate ORF (don't worry, we also had difficulties understanding what happened!) (PubMed:1659648, PubMed:3029015). {ECO:0000305|PubMed:1659648, ECO:0000305|PubMed:3029015, ECO:0000305|PubMed:3275618, ECO:0000305|PubMed:7592420, ECO:0000305|Ref.2}. reclassified-function P0A6N4 efp Escherichia coli (strain K12) 83333 Elongation factor P (EF-P) The modification on Lys-34 was initially suggested to be a spermidine residue. {ECO:0000305|PubMed:18201202}. reclassified-function P0ABU5 elbB Escherichia coli (strain K12) 83333 Glyoxalase ElbB (EC 4.2.1.-) (Sigma cross-reacting protein 27A) (SCRP-27A) Was originally thought (PubMed:9603997) to be involved in the early steps of isoprenoid biosynthesis. {ECO:0000305}. reclassified-function P37690 envC Escherichia coli (strain K12) 83333 Murein hydrolase activator EnvC (Septal ring factor) Was originally thought to have murein hydrolase activity. {ECO:0000305|PubMed:15165230}.; reclassified-function P0A9B6 epd Escherichia coli (strain K12) 83333 D-erythrose-4-phosphate dehydrogenase (E4PDH) (EC 1.2.1.72) Was originally (PubMed:2546007, PubMed:2124629) thought to be a glyceraldehyde 3-phosphate dehydrogenase, but glyceraldehyde 3-phosphate is not an efficient substrate (PubMed:7751290, PubMed:9182530). {ECO:0000305}. reclassified-function P0A8N7 epmA Escherichia coli (strain K12) 83333 Elongation factor P--(R)-beta-lysine ligase (EF-P--(R)-beta-lysine ligase) (EC 6.3.2.-) (EF-P post-translational modification enzyme A) (EF-P-lysine lysyltransferase) (GX) Was originally suggested to be a tRNA synthase, however its lack of an anticodon-binding domain made this highly unlikely. {ECO:0000305|PubMed:1761227}. reclassified-function Q47146 fadE Escherichia coli (strain K12) 83333 Acyl-coenzyme A dehydrogenase (ACDH) (Acyl-CoA dehydrogenase) (EC 1.3.8.7) (EC 1.3.8.8) Was originally named fadF. {ECO:0000305}. reclassified-function P0A991 fbaB Escherichia coli (strain K12) 83333 Fructose-bisphosphate aldolase class 1 (EC 4.1.2.13) (Fructose-bisphosphate aldolase class I) (FBP aldolase) Was originally (Ref.1) thought to be a dehydrin. {ECO:0000305}. reclassified-function P0AEN1 fre Escherichia coli (strain K12) 83333 NAD(P)H-flavin reductase (EC 1.5.1.41) (FMN reductase) (Ferrisiderophore reductase C) (NAD(P)H:flavin oxidoreductase) (Riboflavin reductase [NAD(P)H]) Was originally assigned to be ubiB. {ECO:0000305|PubMed:1379743}. reclassified-function P0ABG4 ftsW Escherichia coli (strain K12) 83333 Probable peptidoglycan glycosyltransferase FtsW (PGT) (EC 2.4.99.28) (Cell division protein FtsW) (Cell wall polymerase) (Lipid II flippase FtsW) (Peptidoglycan polymerase) (PG polymerase) Has previously been proposed to be a lipid II flippase that transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane (PubMed:21386816, PubMed:24711460), but recent evidence suggests that FtsW may function as a peptidoglycan polymerase (PubMed:27643381). The identity of the lipid II flippase is still controversial with conflicting in vivo and in vitro results, but MurJ (AC P0AF16) is probably the lipid II flippase. {ECO:0000305}. reclassified-function P69937 gdx Escherichia coli (strain K12) 83333 Guanidinium exporter (Quaternary ammonium compound-resistance protein SugE) Was originally (PubMed:8096175) thought to suppress a groEL mutation and mimic the effect of groE overexpression. This was later shown (PubMed:11948170) to be probably due to an artifact. {ECO:0000305|PubMed:11948170, ECO:0000305|PubMed:8096175}. reclassified-function P26649 glgS Escherichia coli (strain K12) 83333 Surface composition regulator Was originally thought to be involved in glycogen synthesis, but it was shown later that its effect on glycogen metabolism is probably indirect. {ECO:0000305|PubMed:1324388, ECO:0000305|PubMed:23537328}. reclassified-function P09391 glpG Escherichia coli (strain K12) 83333 Rhomboid protease GlpG (EC 3.4.21.105) (Intramembrane serine protease) Was originally identified as a repressor of the glycerol-3-phosphate regulon. {ECO:0000305|PubMed:8955387}. reclassified-function P03825 gspB Escherichia coli (strain K12) 83333 Putative general secretion pathway protein B Was originally identified as the 11.3 kDa PinO protein, a calcium-binding protein synthesized in the absence of isoleucine in relA stains, which may be required for the initiation of chromosome replication (PubMed:1925011, PubMed:1938934). But GspB is predicted to be 15.9 kDa and has isoleucine residues, and there is no evidence that gspB encodes the PinO peptide or that it binds calcium. {ECO:0000305, ECO:0000305|PubMed:1925011, ECO:0000305|PubMed:1938934}. reclassified-function P0A8R9 hdfR Escherichia coli (strain K12) 83333 HTH-type transcriptional regulator HdfR (H-NS-dependent flhDC regulator) Was originally thought to be involved in the expression of the phosphatidylserine synthetase pssA. {ECO:0000305|PubMed:6309791}. reclassified-function P0ABC3 hflC Escherichia coli (strain K12) 83333 Modulator of FtsH protease HflC Was originally (PubMed:2973057) thought to be a protease. However, removal of residues 165-200 (a ClpP-protease-like motif) does not alter the lysogenization process, and in vitro studies show no evidence of a protease activity for the isolated HflKC complex. {ECO:0000305|PubMed:2973057}. reclassified-function P0ABC7 hflK Escherichia coli (strain K12) 83333 Modulator of FtsH protease HflK Was originally (PubMed:2973057) thought to be a protease. However, removal of residues '165-200' of complex member HflC (a ClpP-protease-like motif) does not alter the lysogenization process, and in vitro studies show no evidence of a protease activity for the isolated HflKC complex. {ECO:0000305|PubMed:2973057}. reclassified-function P67910 hldD Escherichia coli (strain K12) 83333 ADP-L-glycero-D-manno-heptose-6-epimerase (EC 5.1.3.20) (ADP-L-glycero-beta-D-manno-heptose-6-epimerase) (ADP-glyceromanno-heptose 6-epimerase) (ADP-hep 6-epimerase) (AGME) Was originally thought to be a homohexamer. {ECO:0000305|PubMed:7929099}. reclassified-function P0AAJ8 hybA Escherichia coli (strain K12) 83333 Hydrogenase-2 operon protein HybA Was originally thought to be the small subunit of hydrogenase 2. {ECO:0000305|PubMed:8021226}. reclassified-function P05791 ilvD Escherichia coli (strain K12) 83333 Dihydroxy-acid dehydratase (DAD) (EC 4.2.1.9) Was originally thought to contain a [4Fe-4S] cluster (PubMed:7771772, PubMed:8325851). However, a more recent study in M.tuberculosis has shown that this enzyme contains a [2Fe-2S] cluster, which is unstable and subject to degradation. {ECO:0000269|PubMed:7771772, ECO:0000269|PubMed:8325851, ECO:0000305}. reclassified-function P0A707 infC Escherichia coli (strain K12) 83333 Translation initiation factor IF-3 [Cleaved into: Translation initiation factor IF-3, N-terminally processed; Translation initiation factor IF-3S] Was originally (PubMed:2954162) thought to control the translation of its own gene by binding to its mRNA; it now seems that discrimination against the AUU start codon is a kinetic effect (PubMed:16857585). {ECO:0000305|PubMed:16857585, ECO:0000305|PubMed:2954162}. reclassified-function P62615 ispE Escherichia coli (strain K12) 83333 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (CMK) (EC 2.7.1.148) (4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase) Was originally thought to be an isopentenyl monophosphate kinase. {ECO:0000305|PubMed:1427085}. reclassified-function P0C8K0 kbaZ Escherichia coli (strain K12) 83333 D-tagatose-1,6-bisphosphate aldolase subunit KbaZ Was originally thought to be a tagatose 6-phosphate kinase. {ECO:0000305|PubMed:8932697}. reclassified-function P37339 lhgD Escherichia coli (strain K12) 83333 L-2-hydroxyglutarate dehydrogenase (L2HG dehydrogenase) (EC 1.1.5.13) (L2HG:quinone oxidoreductase) Was originally thought to be an oxidase, i.e. using molecular oxygen for oxidation of L-2-hydroxyglutarate and producing hydrogen peroxide. However, no O2 consumption could be detected with L2HG using the purified recombinant and active enzyme (PubMed:30498244). {ECO:0000269|PubMed:30498244, ECO:0000305|PubMed:18390652}. reclassified-function P61320 lolB Escherichia coli (strain K12) 83333 Outer-membrane lipoprotein LolB Was originally thought to be involved in delta-aminolevulinic acid biosynthesis. {ECO:0000305|PubMed:1427085}. reclassified-function P21645 lpxD Escherichia coli (strain K12) 83333 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (UDP-3-O-(3-OHC14)-GlcN N-acyltransferase) (EC 2.3.1.191) (Protein FirA) (Rifampicin resistance protein) (UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase) Was originally thought to be involved in transcription. {ECO:0000305}. reclassified-function P24205 lpxM Escherichia coli (strain K12) 83333 Lipid A biosynthesis myristoyltransferase (EC 2.3.1.243) (Kdo(2)-lauroyl-lipid IV(A) myristoyltransferase) Was originally thought to be the membrane-bound lytic murein transglycosylase (MLT). {ECO:0000305|PubMed:1356966}. reclassified-function P77432 lsrK Escherichia coli (strain K12) 83333 Autoinducer-2 kinase (AI-2 kinase) (EC 2.7.1.189) Was originally thought to originate from human and was called BRAG1 (brain-related apoptosis gene 1) with a proposed role in apoptosis (PubMed:8649811). The DNA sequence of the region sequenced is more than 99% identical to that of this E.coli gene. Furthermore the claim of an 'extensive similarity to the Bcl-2 family of genes' is not correct. {ECO:0000305|PubMed:8649811}. reclassified-function P0AEY1 marC Escherichia coli (strain K12) 83333 UPF0056 inner membrane protein MarC Was originally thought to be involved in multiple antibiotic resistance. {ECO:0000305|PubMed:8383113}. reclassified-function P0AAG5 mdlB Escherichia coli (strain K12) 83333 Multidrug resistance-like ATP-binding protein MdlB (EC 7.6.2.2) Was originally proposed to be fused with MdlA. {ECO:0000305|PubMed:7904973}. reclassified-function P17109 menD Escherichia coli (strain K12) 83333 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (SEPHCHC synthase) (EC 2.2.1.9) (Menaquinone biosynthesis protein MenD) Was originally thought (PubMed:1459959, PubMed:14621995, PubMed:16511076) to be a 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase but further protein analysis clearly suggests that it is a 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) synthase. {ECO:0000305|PubMed:17760421}. reclassified-function P0A817 metK Escherichia coli (strain K12) 83333 S-adenosylmethionine synthase (AdoMet synthase) (EC 2.5.1.6) (MAT) (Methionine adenosyltransferase) Was originally thought to differ from MetX, which was assigned as a second AdoMet synthase before being shown to be identical to MetK. {ECO:0000305|PubMed:8231813}. reclassified-function P0AEZ7 mltD Escherichia coli (strain K12) 83333 Membrane-bound lytic murein transglycosylase D (EC 4.2.2.n1) (Murein hydrolase D) (Regulatory protein DniR) Was originally thought to be involved in hexaheme nitrite reductase (cytochrome c552) expression. {ECO:0000305|PubMed:1663890}. reclassified-function P25745 mnmA Escherichia coli (strain K12) 83333 tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) Was originally thought to be a 5-methylaminomethyl-2-methyltransferase involved in tRNA modification. {ECO:0000305}. reclassified-function P0DKB3 mntS Escherichia coli (strain K12) 83333 Small protein MntS MntS mRNA was originally thought to be an sRNA. {ECO:0000305|PubMed:21908668}. reclassified-function P0AF01 modB Escherichia coli (strain K12) 83333 Molybdenum transport system permease protein ModB The molybdate transport operon was originally thought to be composed of four genes: modA, modB, modC and modD (modABCD operon) (PubMed:7665460, PubMed:8564363). The annotation of modD as a fourth gene in the mod operon was later adjusted and an open reading frame in the reverse direction, ybhA, is now annotated at this location. {ECO:0000269|PubMed:7665460, ECO:0000269|PubMed:8564363, ECO:0000305}. reclassified-function P09833 modC Escherichia coli (strain K12) 83333 Molybdenum import ATP-binding protein ModC (EC 7.3.2.5) The molybdate transport operon was originally thought to be composed of four genes: modA, modB, modC and modD (modABCD operon) (PubMed:7665460, PubMed:8564363). The annotation of modD as a fourth gene in the mod operon was later adjusted and an open reading frame in the reverse direction, ybhA, is now annotated at this location. {ECO:0000269|PubMed:7665460, ECO:0000269|PubMed:8564363, ECO:0000305}. reclassified-function P31060 modF Escherichia coli (strain K12) 83333 ABC transporter ATP-binding protein ModF (Photorepair protein PhrA) Was originally thought to be PhrA, involved in photoreactivation. The protein was thought to be the C-terminus of what is now accepted to be a longer reading frame called ModF; overexpression from a plasmid yields an approximately 50 kDa protein, which is too long to be PhrA (PubMed:8564363). {ECO:0000269|PubMed:8564363, ECO:0000305|PubMed:8310005, ECO:0000305|PubMed:8550508}. reclassified-function P33236 mokC Escherichia coli (strain K12) 83333 Regulatory protein MokC Was originally described as a gef leader peptide. {ECO:0000305|PubMed:1943701}. reclassified-function P60293 mukF Escherichia coli (strain K12) 83333 Chromosome partition protein MukF (Protein KicB) Was originally thought to be a killing factor. PubMed:8602138 showed that it is not involved in killing system. {ECO:0000305}. reclassified-function P63020 nfuA Escherichia coli (strain K12) 83333 Fe/S biogenesis protein NfuA Was originally thought to be involved in gluconate metabolism and was referred to as GntY. {ECO:0000305|PubMed:9871335}. reclassified-function P28903 nrdD Escherichia coli (strain K12) 83333 Anaerobic ribonucleoside-triphosphate reductase (EC 1.1.98.6) (Class III ribonucleoside-triphosphate reductase) Was originally thought to contain an iron sulfur cluster (PubMed:8381402). It was shown later that only NrdG contains an iron sulfur center (PubMed:8621608). {ECO:0000269|PubMed:8621608, ECO:0000303|PubMed:8381402}. reclassified-function P76446 pdeN Escherichia coli (strain K12) 83333 Probable cyclic di-GMP phosphodiesterase PdeN (EC 3.1.4.52) Was originally (Ref.4) thought to originate from Proteus vulgaris, but was shown to originate from E.coli. {ECO:0000305|PubMed:9079933}. reclassified-function P0A9K7 phoU Escherichia coli (strain K12) 83333 Phosphate-specific transport system accessory protein PhoU (Pst system accessory protein PhoU) (Negative regulator of Pho regulon) Was originally thought to be involved in phosphate transport. {ECO:0000305|PubMed:1459954}. reclassified-function P0ADY1 ppiD Escherichia coli (strain K12) 83333 Periplasmic chaperone PpiD (Periplasmic folding chaperone) Was originally thought to be a peptidyl-prolyl isomerase (PPIase). It was shown later that even if PpiD shows sequence similarity to PPIases, it is in fact devoid of PPIase activity (PubMed:19866485). {ECO:0000269|PubMed:19866485, ECO:0000305|PubMed:9670013}. reclassified-function P0ACC1 prmC Escherichia coli (strain K12) 83333 Release factor glutamine methyltransferase (RF MTase) (EC 2.1.1.297) (M.EcoKHemKP) (N5-glutamine methyltransferase PrmC) (Protein release factor methylation C) (Protein-(glutamine-N5) MTase PrmC) (Protein-glutamine N-methyltransferase PrmC) Was originally thought to be involved in the oxidation of protoporphyrinogen into protoporphyrin IX. {ECO:0000305|PubMed:7883187}. reclassified-function P0AG18 purE Escherichia coli (strain K12) 83333 N5-carboxyaminoimidazole ribonucleotide mutase (N5-CAIR mutase) (EC 5.4.99.18) (5-(carboxyamino)imidazole ribonucleotide mutase) Was originally thought to be the catalytic subunit of phosphoribosylaminoimidazole carboxylase, with ATPase subunit PurK. {ECO:0000305|PubMed:2464576}. reclassified-function P09029 purK Escherichia coli (strain K12) 83333 N5-carboxyaminoimidazole ribonucleotide synthase (N5-CAIR synthase) (EC 6.3.4.18) (5-(carboxyamino)imidazole ribonucleotide synthetase) Was originally thought to be the ATPase subunit of phosphoribosylaminoimidazole carboxylase, with catalytic subunit PurE. {ECO:0000305|PubMed:2464576}. reclassified-function P0A8V0 rbn Escherichia coli (strain K12) 83333 Ribonuclease BN (RNase BN) (EC 3.1.-.-) (Ribonuclease Z homolog) (RNase Z homolog) Was initially thought to be an arylsulfatase, given its similarity with the AtsA family. PubMed:12029081 however showed that it is a zinc phosphodiesterase. {ECO:0000305}. reclassified-function P27830 rffG Escherichia coli (strain K12) 83333 dTDP-glucose 4,6-dehydratase 2 (EC 4.2.1.46) Was originally thought to be rffE, the UDP-N-acetylglucosamine epimerase. {ECO:0000305|PubMed:1379743}. reclassified-function P0A8R0 rraA Escherichia coli (strain K12) 83333 Regulator of ribonuclease activity A Although it was initially thought to be a methyltransferase of the menaquinone pathway, PubMed:13678585 showed that it has no SAM-dependent methyltransferase activity and is not involved in the menaquinone pathway. {ECO:0000305}. reclassified-function P46187 rseC Escherichia coli (strain K12) 83333 Protein RseC Was originally suggested to positively regulate sigma-E activity in vitro. {ECO:0000305|PubMed:9159522}. reclassified-function P0AEH1 rseP Escherichia coli (strain K12) 83333 Regulator of sigma-E protease RseP (EC 3.4.24.-) (S2P endopeptidase) (Site-2 protease RseP) (S2P protease RseP) (Site-2-type intramembrane protease) Was originally thought to be a negative regulator of sigma-E function and to act directly on sigma-E and RpoH; this may not be physiologically relevant. {ECO:0000305|PubMed:11689431}. reclassified-function P39286 rsgA Escherichia coli (strain K12) 83333 Small ribosomal subunit biogenesis GTPase RsgA (EC 3.6.1.-) Was initially characterized with a propeptide of 20 residues; this is now thought to be the result of in vitro proteolysis when the protein is overexpressed (PubMed:12220175, PubMed:14973029). {ECO:0000305|PubMed:12220175, ECO:0000305|PubMed:14973029}. reclassified-function P64559 sdhE Escherichia coli (strain K12) 83333 FAD assembly factor SdhE (Antitoxin CptB) Was originally thought to be the antitoxin component of a type II toxin-antitoxin (TA) system (PubMed:22239607). When coexpressed with cognate toxin CptA (now ygfX), the antitoxin neutralizes toxicity of CptA (PubMed:22239607). Has been suggested to be a transcriptional regulator (PubMed:22239607). The putative toxin, CptA (ygfX) has since been shown not to be toxic in E.coli or Serratia species (PubMed:23657679). {ECO:0000269|PubMed:22239607, ECO:0000269|PubMed:23657679}. reclassified-function P68191 sra Escherichia coli (strain K12) 83333 Stationary-phase-induced ribosome-associated protein (Protein D) (SRA) (30S ribosomal protein S22) Was originally thought to be a ribosomal protein. {ECO:0000305|PubMed:3553168}. reclassified-function P0A840 surE Escherichia coli (strain K12) 83333 5'/3'-nucleotidase SurE (EC 3.1.3.5) (EC 3.1.3.6) (Exopolyphosphatase) (EC 3.6.1.11) (Nucleoside monophosphate phosphohydrolase) (Stationary-phase survival protein SurE) Was originally annotated as an acid phosphatase (EC 3.1.3.2). {ECO:0000305}. reclassified-function P25396 tehA Escherichia coli (strain K12) 83333 Tellurite resistance protein TehA Was originally thought to be plasmid encoded. {ECO:0000305|PubMed:2060788}. reclassified-function P25397 tehB Escherichia coli (strain K12) 83333 Tellurite methyltransferase (EC 2.1.1.265) (Chalcogen-detoxifying protein TehB) (Selenite methyltransferase) (Tellurite resistance protein TehB) Was originally thought to be plasmid encoded. {ECO:0000305|PubMed:2060788}. reclassified-function P37025 thpR Escherichia coli (strain K12) 83333 RNA 2',3'-cyclic phosphodiesterase (RNA 2',3'-CPDase) (EC 3.1.4.58) (Two-histidine 2',3'-cyclic phosphodiesterase acting on RNA) Was originally thought to be a 2',5'-RNA ligase. {ECO:0000305|PubMed:6347395, ECO:0000305|PubMed:8940112}. reclassified-function P46923 torZ Escherichia coli (strain K12) 83333 Trimethylamine-N-oxide reductase 2 (TMAO reductase 2) (Trimethylamine oxidase 2) (EC 1.7.2.3) Was originally thought to be a biotin sulfoxide reductase. {ECO:0000305|PubMed:8919859}. reclassified-function P0A881 trpR Escherichia coli (strain K12) 83333 Trp operon repressor PubMed:7841459 sequence was originally thought to originate from S.typhimurium, but seems to come from an unknown E.coli strain. {ECO:0000305}. reclassified-function P60932 uppP Escherichia coli (strain K12) 83333 Undecaprenyl-diphosphatase (EC 3.6.1.27) (Bacitracin resistance protein) (Undecaprenyl pyrophosphate phosphatase) Was originally thought to be an undecaprenol kinase. {ECO:0000305|PubMed:8389741}. reclassified-function P0A8G6 wrbA Escherichia coli (strain K12) 83333 NAD(P)H dehydrogenase (quinone) (EC 1.6.5.2) (Flavoprotein WrbA) (NAD(P)H:quinone oxidoreductase) (NQO) Was originally (PubMed:9694845) thought to enhance the formation and/or stability of non-covalent complexes between the trp repressor protein and operator-bearing DNA. However, WrbA does not specifically influence the affinity or mode of binding of TrpR to its operator. {ECO:0000305|PubMed:9694845}. reclassified-function P27835 wzyE Escherichia coli (strain K12) 83333 Probable ECA polymerase Was originally thought to be WecF, the 4-alpha-L-fucosyltransferase. {ECO:0000305|PubMed:11673418}. reclassified-function P33128 yadV Escherichia coli (strain K12) 83333 Probable fimbrial chaperone YadV Was originally called ecpD, but ecp is now used for the ecpABCDE operon involved in E.coli common pilus (ECP) synthesis. {ECO:0000305|PubMed:8102362}. reclassified-function Q46948 yajL Escherichia coli (strain K12) 83333 Protein/nucleic acid deglycase 3 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Chaperone protein YajL) (Maillard deglycase) Was originally (Ref.1) thought to be involved in thiamine biosynthesis. However, this phenotype was probably due to an artifactual recombination event involving a portion of the adjacent thiI gene. {ECO:0000305}.; reclassified-function P0AAT4 ybdG Escherichia coli (strain K12) 83333 Mechanosensing system component YbdG (Mechanosensitive channel homolog YbdG) Was originally thought to be the miniconductance mechanosensitive channel MscM. However, the YbdG channel was not found to gate in patch clamp experiments unless a mutation has been introduced and YbdG alone cannot account for the MscM activity since null mutations do not eliminate the MscM channel activity from patches (PubMed:20616037). It was shown later that yjeP does encode the principal component of the MscM channel (PubMed:22874652). {ECO:0000269|PubMed:20616037, ECO:0000269|PubMed:22874652, ECO:0000305|PubMed:20616037}. reclassified-function P76318 yedK Escherichia coli (strain K12) 83333 Abasic site processing protein YedK (EC 4.-.-.-) (Peptidase YedK) (EC 3.4.-.-) Was reported to act as an endonuclease that specifically cleaves 5-hydroxymethylcytosine (5hmC)-containing DNA in vitro (PubMed:29020633). Additional experiments are however required to confirm this activity as this protein is present in many organisms that do not utilize methylcytosine for epigenetic control. {ECO:0000269|PubMed:29020633, ECO:0000305|PubMed:30554877}. reclassified-function P33345 yehF Escherichia coli (strain K12) 83333 Protein YehF Was originally thought to be involved in the regulation of molybdate metabolism, which gave rise to the name molR, however the locus in PubMed:2156810 was mapped at 65 centisomes (minutes) on the E.coli chromosome, while this locus maps to 47.3 centisomes (PubMed:2156810). This locus gives rise to a transcript that could encode the 'interrupted' N-terminal 274 amino acid gene product of yehF. The protein it encodes (shown here) is missing the C-terminus compared to orthologs. {ECO:0000269|PubMed:2156810, ECO:0000305}. reclassified-function P33359 yehW Escherichia coli (strain K12) 83333 Glycine betaine uptake system permease protein YehW Was originally thought to be part of an osmoprotectant uptake system (PubMed:15251200). However, it was shown later that the complex does not mediate osmotic stress protection (PubMed:26325238). {ECO:0000305|PubMed:15251200, ECO:0000305|PubMed:26325238}. reclassified-function P33360 yehX Escherichia coli (strain K12) 83333 Glycine betaine uptake system ATP-binding protein YehX (EC 7.4.2.-) Was originally thought to be part of an osmoprotectant uptake system (PubMed:15251200). However, it was shown later that the complex does not mediate osmotic stress protection (PubMed:26325238). {ECO:0000305|PubMed:15251200, ECO:0000305|PubMed:26325238}. reclassified-function P33361 yehY Escherichia coli (strain K12) 83333 Glycine betaine uptake system permease protein YehY Was originally thought to be part of an osmoprotectant uptake system (PubMed:15251200). However, it was shown later that the complex does not mediate osmotic stress protection (PubMed:26325238). {ECO:0000305|PubMed:15251200, ECO:0000305|PubMed:26325238}. reclassified-function P33362 yehZ Escherichia coli (strain K12) 83333 Glycine betaine-binding protein YehZ Was originally thought to be part of an osmoprotectant uptake system (PubMed:15251200). However, it was shown later that the complex does not mediate osmotic stress protection (PubMed:26325238). {ECO:0000305|PubMed:15251200, ECO:0000305|PubMed:26325238}. reclassified-function P76536 yfeX Escherichia coli (strain K12) 83333 Dye-decolorizing peroxidase YfeX (EC 1.11.1.-) (Porphyrinogen oxidase) Was originally thought to be a deferrochelatase, which promotes iron extraction from exogenous heme source, preserving the tetrapyrrol ring intact (PubMed:19564607). However, Dailey et al. were unable to reproduce the in vitro dechelation reaction (PubMed:22068980). They suggest that YfeX is a typical dye-decolorizing peroxidase and not a dechelatase, and that the protoporphyrin reported by Letoffe et al. to accumulate when YfeX is overexpressed likely arises from the intracellular oxidation of endogenously synthesized protoporphyrinogen and not from dechelation of exogenously supplied heme (PubMed:22068980). {ECO:0000269|PubMed:22068980, ECO:0000305|PubMed:19564607}. reclassified-function P38506 ygdG Escherichia coli (strain K12) 83333 Flap endonuclease Xni (FEN) (EC 3.1.-.-) (Exonuclease IX) (ExoIX) Was initially reported (PubMed:9592142) as a 3'-5' exonuclease due to contamination of samples. This protein possesses no such activity (PubMed:17567612, PubMed:19000038). {ECO:0000305|PubMed:9592142}. reclassified-function Q46824 ygfX Escherichia coli (strain K12) 83333 Inner membrane protein YgfX (Toxin CptA) Was originally thought to be the toxic component of a type II toxin-antitoxin (TA) system; overexpression was shown to lead to growth arrest after 5 hours, with initial elongation of cells, followed by swelling (PubMed:22239607). The toxic effects were abrogated by coexpression with antitoxin CptB (now sdhE) (PubMed:22239607). However subsequent studies have been unable to show the toxic effect upon overexpression, nor is the Serratia ortholog a toxin (PubMed:23657679). {ECO:0000269|PubMed:22239607, ECO:0000269|PubMed:23657679}. reclassified-function P37674 yiaM Escherichia coli (strain K12) 83333 2,3-diketo-L-gulonate TRAP transporter small permease protein YiaM Was originally proposed to be a subunit from an L-xylulose uptake system, but PubMed:16385129 shows that it does not bind L- or D-xylulose. {ECO:0000305|PubMed:14668138}. reclassified-function P37675 yiaN Escherichia coli (strain K12) 83333 2,3-diketo-L-gulonate TRAP transporter large permease protein YiaN Was originally proposed to be a subunit from an L-xylulose uptake system, but PubMed:16385129 shows that it does not bind L- or D-xylulose. {ECO:0000305|PubMed:14668138}. reclassified-function P37676 yiaO Escherichia coli (strain K12) 83333 2,3-diketo-L-gulonate-binding periplasmic protein YiaO (2,3-DKG-binding protein) (Extracytoplasmic solute receptor protein YiaO) Was originally proposed to be a subunit from an L-xylulose uptake system, but PubMed:16385129 shows that YiaO does not bind L- or D-xylulose. {ECO:0000305|PubMed:14668138}. reclassified-function P25531 yicR Escherichia coli (strain K12) 83333 UPF0758 protein YicR Was originally thought to be the site of the radC102 mutation, but it was subsequently shown that radC102 is an allele of RecG. {ECO:0000305|PubMed:11053371}. reclassified-function P32129 yihG Escherichia coli (strain K12) 83333 1-acylglycerol-3-phosphate O-acyltransferase YihG (EC 2.3.1.51) (Lysophosphatidic acid acyltransferase) (LPAAT) Was originally thought to be a second poly(A) polymerase. However, it was shown later that this protein does not function as a poly(A) polymerase (PubMed:10594834). {ECO:0000269|PubMed:10594834, ECO:0000305|PubMed:8876178}. reclassified-function P0A8K8 yihY Escherichia coli (strain K12) 83333 UPF0761 membrane protein YihY Was originally (PubMed:8955422) thought to be the tRNA-processing ribonuclease BN (rbn). This was later proven not to be the case (PubMed:15764599). {ECO:0000305|PubMed:15764599, ECO:0000305|PubMed:8955422}. reclassified-function P27375 yjaZ Escherichia coli (strain K12) 83333 Protein YjaZ (Heat shock protein C) Was originally thought to be a heat shock protein. However upon further examination the original mutants do not have a deletion in this gene (PubMed:16980444). {ECO:0000269|PubMed:16980444, ECO:0000305|PubMed:2160943}. reclassified-function P16681 yjdN Escherichia coli (strain K12) 83333 Protein YjdN Was originally thought to be involved in phosphonate metabolism. {ECO:0000305|PubMed:2155230}. reclassified-function P39393 yjiV Escherichia coli (strain K12) 83333 Putative uncharacterized protein YjiV A portion of this ORF was originally annotated as mcrD, and reported to inhibit mcrE restriction. {ECO:0000305}.; reclassified-function P39411 yjjX Escherichia coli (strain K12) 83333 Inosine/xanthosine triphosphatase (ITPase/XTPase) (EC 3.6.1.73) (Non-canonical purine NTP phosphatase) (Non-standard purine NTP phosphatase) (Nucleoside-triphosphate phosphatase) (NTPase) PubMed:7841459 sequence was originally thought to originate from S.typhimurium, but seems to come from an unknown E.coli strain. {ECO:0000305}. reclassified-function P0AAA5 ymcE Escherichia coli (strain K12) 83333 Uncharacterized protein YmcE Was originally thought to suppress the temperature-sensitive growth phenotype of fabA6(Ts) mutants. {ECO:0000305|PubMed:8808925}. reclassified-function P0A8I1 yqgF Escherichia coli (strain K12) 83333 Putative pre-16S rRNA nuclease (EC 3.1.-.-) Was originally suggested to be a nuclease that resolves Holliday junction intermediates during genetic recombination. {ECO:0000303|PubMed:10982859}. reclassified-function P0ADW3 zapG Escherichia coli (strain K12) 83333 Z-ring associated protein G (Cell division protein ZapG) (LPS assembly protein LapD) Was originally thought to be a member of the cytochrome bd-I complex (PubMed:16079137). Subsequent work suggests this is not the case (PubMed:16863643). {ECO:0000305|PubMed:16079137, ECO:0000305|PubMed:16863643}. reclassified-function P14375 zraR Escherichia coli (strain K12) 83333 Transcriptional regulatory protein ZraR Was originally thought to be involved in the regulation of the labile hydrogenase activity (PubMed:2666400). It was shown later that this activity results from the non-specific action of overproduced ZraR on hydrogenase 3 formation (PubMed:11243806). {ECO:0000269|PubMed:11243806, ECO:0000269|PubMed:2666400}. reclassified-function P14377 zraS Escherichia coli (strain K12) 83333 Sensor histidine kinase ZraS (EC 2.7.13.3) Was originally thought to be involved in the regulation of the labile hydrogenase activity (PubMed:2666400). It was shown later that this activity results from the non-specific action of overproduced ZraR on hydrogenase 3 formation (PubMed:11243806). {ECO:0000269|PubMed:11243806, ECO:0000269|PubMed:2666400}. reclassified-function B6I548 dapA Escherichia coli (strain SE11) 409438 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B6HYX9 dapB Escherichia coli (strain SE11) 409438 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1LNC8 dapA Escherichia coli (strain SMS-3-5 / SECEC) 439855 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1LFW1 dapB Escherichia coli (strain SMS-3-5 / SECEC) 439855 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1RGH0 dapB Escherichia coli (strain UTI89 / UPEC) 364106 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7UI76 dapB Escherichia coli O127:H6 (strain E2348/69 / EPEC) 574521 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P94777 modD Escherichia coli O127:H6 (strain E2348/69 / EPEC) 574521 Putative pyrophosphorylase ModD (EC 2.4.2.-) Was originally (Ref.1) thought to be involved in molybdate transport. {ECO:0000305}. reclassified-function A7ZPS4 dapA Escherichia coli O139:H28 (strain E24377A / ETEC) 331111 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7ZHC0 dapB Escherichia coli O139:H28 (strain E24377A / ETEC) 331111 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P63944 dapA Escherichia coli O157:H7 83334 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P58209 dapB Escherichia coli O157:H7 83334 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B5Z015 dapA Escherichia coli O157:H7 (strain EC4115 / EHEC) 444450 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B5YYC3 dapB Escherichia coli O157:H7 (strain EC4115 / EHEC) 444450 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7N7Q5 dapB Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC) 585056 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1A780 dapB Escherichia coli O1:K1 / APEC 405955 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7MAF2 dapB Escherichia coli O45:K1 (strain S88 / ExPEC) 585035 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P63943 dapA Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) 199310 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8FLB4 dapB Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) 199310 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0TLW0 dapB Escherichia coli O6:K15:H31 (strain 536 / UPEC) 362663 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7NQL6 dapA Escherichia coli O7:K1 (strain IAI39 / ExPEC) 585057 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B7NHD5 dapB Escherichia coli O7:K1 (strain IAI39 / ExPEC) 585057 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7M7I1 dapA Escherichia coli O8 (strain IAI1) 585034 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B7M0C7 dapB Escherichia coli O8 (strain IAI1) 585034 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7MYB7 dapA Escherichia coli O81 (strain ED1a) 585397 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B7MNN7 dapB Escherichia coli O81 (strain ED1a) 585397 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8A2X1 dapA Escherichia coli O9:H4 (strain HS) 331112 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7ZVX9 dapB Escherichia coli O9:H4 (strain HS) 331112 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7LKG3 dapA Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73) 585054 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B7LWM1 dapB Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73) 585054 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1YJ39 dapA Exiguobacterium sibiricum (strain DSM 17290 / CCUG 55495 / CIP 109462 / JCM 13490 / 255-15) 262543 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1YJ40 dapB Exiguobacterium sibiricum (strain DSM 17290 / CCUG 55495 / CIP 109462 / JCM 13490 / 255-15) 262543 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C4L2D2 dapA Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b) 360911 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C4L2D3 dapB Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b) 360911 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O01369 UBCRBP Fasciola hepatica (Liver fluke) 6192 Cytochrome b-c1 complex subunit 7 (Complex III subunit 7) (Complex III subunit VII) (Ubiquinol-cytochrome c reductase complex 14 kDa protein) Was originally thought to be the ubiquinone-binding protein (QP-C). {ECO:0000305}. reclassified-function A7HJ56 dapA Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1) 381764 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5FE82 dapA Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae) 376686 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6H0M8 dapA Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86) 402612 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9ZRF1 CAD Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana) 3747 Probable mannitol dehydrogenase (EC 1.1.1.255) (NAD-dependent mannitol dehydrogenase) Was originally thought to be a cinnamyl-alcohol dehydrogenase. {ECO:0000305|PubMed:12147722}. reclassified-function B0TWJ4 dapA Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / CCUG 19701 / FSC 153 / O#319-036) 484022 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0Q8L5 dapA Francisella tularensis subsp. novicida (strain ATCC 15482 / CCUG 33449 / U112) 401614 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P56533 aldh9A1 Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias) 8053 4-trimethylaminobutyraldehyde dehydrogenase (TMABA-DH) (TMABADH) (EC 1.2.1.47) (Aldehyde dehydrogenase family 9 member A1) (EC 1.2.1.3) (Betaine aldehyde dehydrogenase) (BADH) Was originally named betaine aldehyde dehydrogenase (PubMed:9792097). Sequence similarity is higher with aldehyde dehydrogenase family 9 member A1, suggesting it has the same function and catalytic activities as other homologs. {ECO:0000303|PubMed:9792097, ECO:0000305}. reclassified-function P00789 Gallus gallus (Chicken) 9031 Calpain-1 catalytic subunit (EC 3.4.22.52) (Calcium-activated neutral proteinase) (CANP) (Calpain-1 large subunit) (Mu/M-type) This protein was previously thought to be M-calpain but has since been found to be an intermediate form between the M and Mu types. {ECO:0000305}. reclassified-function P33879 ATP1B3 Gallus gallus (Chicken) 9031 Sodium/potassium-transporting ATPase subunit beta-3 (Sodium/potassium-dependent ATPase subunit beta-3) Was originally thought to be the beta-2 subunit. {ECO:0000305|PubMed:8391844}. reclassified-function P13127 CAPZA1 Gallus gallus (Chicken) 9031 F-actin-capping protein subunit alpha-1 (Beta-actinin subunit I) (CapZ 36/32) Was originally thought to have an internal disulfide bond. {ECO:0000305|PubMed:2762296}. reclassified-function P19204 CASQ2 Gallus gallus (Chicken) 9031 Calsequestrin-2 (Laminin-binding protein) Was initially identified as a laminin-binding protein (PubMed:3417768), but later studies indicate that this is highly unlikely (PubMed:1825466, PubMed:2302244). {ECO:0000305}. reclassified-function Q5ZKT6 EEF1AKMT1 Gallus gallus (Chicken) 9031 EEF1A lysine methyltransferase 1 (EC 2.1.1.-) (N(6)-adenine-specific DNA methyltransferase 2) (Protein-lysine N-methyltransferase N6AMT2) Was originally thought to be an N(6)-adenine-specific DNA methyltransferase based on primary sequence and predicted secondary structure. {ECO:0000255|HAMAP-Rule:MF_03187}. reclassified-function Q5ZHS1 ELP3 Gallus gallus (Chicken) 9031 Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function Q9DF58 ILK Gallus gallus (Chicken) 9031 Scaffold protein ILK (ILK-1) (ILK-2) (Inactive integrin-linked kinase) (p59ILK) Was originally thought to act as a serine/threonine-protein kinase. Now thought to be a pseudokinase which does not have kinase activity and which functions solely as a scaffold protein. {ECO:0000250|UniProtKB:Q13418}. reclassified-function P55080 MFAP1 Gallus gallus (Chicken) 9031 Microfibrillar-associated protein 1 (Associated microfibril protein) (AMF) (Spliceosome B complex protein MFAP1) Was initially identified as a component of the elastin-associated microfibrils (PubMed:1374398). More recent results indicate it is instead part of the spliceosome B complex. {ECO:0000250|UniProtKB:P55081, ECO:0000269|PubMed:1374398}. reclassified-function Q8UW59 PARK7 Gallus gallus (Chicken) 9031 Protein/nucleic acid deglycase DJ-1 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) (Parkinson disease protein 7 homolog) (Parkinsonism-associated deglycase) (Protein DJ-1) (DJ-1) Glyoxylase activity previously reported may reflect in fact its deglycase activity. {ECO:0000250|UniProtKB:Q99497}.; reclassified-function P57788 SLC16A3 Gallus gallus (Chicken) 9031 Monocarboxylate transporter 4 (MCT 4) (Solute carrier family 16 member 3) Was initially thought to be considered to be a low affinity lactate transporter with negligible affinity for pyruvate (By similarity). However, it was later shown that SLC16A3 is a high affinity lactate transporter with physiologically relevant affinity for pyruvate (By similarity). {ECO:0000250|UniProtKB:O15427}. reclassified-function P48984 TEAD4 Gallus gallus (Chicken) 9031 Transcriptional enhancer factor TEF-3 (M-CAT-binding factor) (RTEF-1) (TEA domain family member 4) (TEAD-4) (TEF-1) Was originally called TEF-1, but is the ortholog of mammalian TEF-3. {ECO:0000305|PubMed:8106348}. reclassified-function F1NZP5 TLCD1 Gallus gallus (Chicken) 9031 TLC domain-containing protein 1 (Calfacilitin) Was originally proposed to be a calcium channel facilitator (PubMed:23673622). However, a more recent study shows that this protein regulates membrane phospholipid homeostasis (By similarity). Therefore, any effects on calcium flux are most likely a secondary consequence of defects in membrane composition or fluidity (By similarity). {ECO:0000250|UniProtKB:Q96CP7, ECO:0000269|PubMed:23673622}. reclassified-function Q98SN7 WNT2B Gallus gallus (Chicken) 9031 Protein Wnt-2b Was initially thought to be WNT13. {ECO:0000305|PubMed:10398532}. reclassified-function Q5KXW6 dapB Geobacillus kaustophilus (strain HTA426) 235909 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9X4K2 azoR Geobacillus stearothermophilus (Bacillus stearothermophilus) 1422 FMN-dependent NADH:quinone oxidoreductase (EC 1.6.5.-) (Azo-dye reductase) (FMN-dependent NADH-azo compound oxidoreductase) (FMN-dependent NADH-azoreductase) (EC 1.7.1.17) Was originally (Ref.1) thought to be a thermostable diaphorase. {ECO:0000305}. reclassified-function A4IQ67 dapB Geobacillus thermodenitrificans (strain NG80-2) 420246 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q39Z67 dapA Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15) 269799 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q39Z66 dapB Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15) 269799 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C6E9Q9 dapA Geobacter sp. (strain M21) 443144 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C6E9Q8 dapB Geobacter sp. (strain M21) 443144 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q74GT6 dapA Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) 243231 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q74GT5 dapB Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) 243231 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q749L1 omcC Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) 243231 C-type polyheme cytochrome OmcC (Outer membrane c-type cytochrome C) (Polyheme membrane-associated cytochrome c) Was initially thought to act as an electron-transport mediator in the dissimilatory reduction of Fe(3+). {ECO:0000305|PubMed:11563978}. reclassified-function Q74FU6 sfrA Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) 243231 NADPH-Fe(3+) oxidoreductase subunit alpha (EC 1.-.-.-) (Soluble Fe(3+) reductase alpha subunit) PubMed:17906154 suggests that SfrAB is involved in acetate metabolism and does not participate directly in the reduction of Fe(3+) chelates, as was initially proposed in PubMed:11443080. {ECO:0000305}. reclassified-function Q74FU5 sfrB Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) 243231 NADPH-Fe(3+) oxidoreductase subunit beta (EC 1.-.-.-) (Soluble Fe(3+) reductase beta subunit) PubMed:17906154 suggests that SfrAB is involved in acetate metabolism and does not participate directly in the reduction of Fe(3+) chelates, as was initially proposed in PubMed:11443080. {ECO:0000305}. reclassified-function B9M380 dapA Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter daltonii) 316067 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B9M381 dapB Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter daltonii) 316067 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5GD89 dapA Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens) 351605 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5GD90 dapB Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens) 351605 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P0CS93 GAOA Gibberella zeae (Wheat head blight fungus) (Fusarium graminearum) 5518 Galactose oxidase (GAO) (GO) (GOase) (EC 1.1.3.9) Was originally thought to originate from Polyporus circinatus then later from Dactylium dendroides and is now known to be originating from Gibberella (Fusarium). {ECO:0000305}. reclassified-function B8F8Q1 dapB Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis) 557723 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7NLC0 dapB Gloeobacter violaceus (strain ATCC 29082 / PCC 7421) 251221 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7KBV6 dapB Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC 7424)) 65393 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q90YA8 QPCT Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi) 242054 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (By similarity). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000250|UniProtKB:Q16769}. reclassified-function A9HIW2 dapA Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5) 272568 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A9HE99 dapB Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5) 272568 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5FUW9 dapA Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) 290633 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5FSK8 dapB Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) 290633 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q42800 DHPS1 Glycine max (Soybean) (Glycine hispida) 3847 4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P46417 GST3 Glycine max (Soybean) (Glycine hispida) 3847 Glutathione S-transferase 3 (EC 2.5.1.18) Was originally (Ref.1) thought to be a glyoxalase I. {ECO:0000305}. reclassified-function P01070 KTI3 Glycine max (Soybean) (Glycine hispida) 3847 Trypsin inhibitor A (Kunitz-type trypsin inhibitor A) PubMed:8318586 sequence was originally thought to be rat caltrin. A number of peptide fragments were derived from a trypsin digest of caltrin and soybean trypsin inhibitor was used to stop the digestion. It appears that some of the inhibitor was also digested and sequenced. {ECO:0000305}. reclassified-function Q0BPE6 dapB Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) 391165 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7VM87 dapA Haemophilus ducreyi (strain 35000HP / ATCC 700724) 233412 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7VLM6 dapB Haemophilus ducreyi (strain 35000HP / ATCC 700724) 233412 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q4QNT3 dapA Haemophilus influenzae (strain 86-028NP) 281310 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q4QKM7 dapB Haemophilus influenzae (strain 86-028NP) 281310 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P43797 dapA Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) 71421 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P45153 dapB Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) 71421 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P44121 ligA Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) 71421 DNA ligase (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]) Was originally proposed to code for two separate adjacent ORFs, HI_1182 and HI_1183. {ECO:0000305|PubMed:7542800}. reclassified-function P45270 lolB Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) 71421 Outer-membrane lipoprotein LolB Was originally thought to be involved in delta-aminolevulinic acid biosynthesis. {ECO:0000305}. reclassified-function P44798 torZ Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) 71421 Trimethylamine-N-oxide reductase (TMAO reductase) (Trimethylamine oxidase) (EC 1.7.2.3) Was originally assigned to be a biotin sulfoxide reductase hence the original gene designation of bisC. {ECO:0000305|PubMed:7542800}. reclassified-function A5UAN5 dapA Haemophilus influenzae (strain PittEE) 374930 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5UCB3 dapB Haemophilus influenzae (strain PittEE) 374930 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5UG62 dapA Haemophilus influenzae (strain PittGG) 374931 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5UF10 dapB Haemophilus influenzae (strain PittGG) 374931 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P00473 hhaIIM Haemophilus parahaemolyticus 735 Type II methyltransferase M.HhaII (M.HhaII) (EC 2.1.1.72) (Adenine-specific methyltransferase HhaII) (Modification methylase HhaII) Strain ATCC 10014 was originally thought to originate from H.haemolyticus. {ECO:0000305}. reclassified-function P00643 hhaIIR Haemophilus parahaemolyticus 735 Type II restriction enzyme HhaII (R.HhaII) (EC 3.1.21.4) (Endonuclease HhaII) (Type-2 restriction enzyme HhaII) Strain ATCC 10014 was originally thought to originate from H.haemolyticus. {ECO:0000305}. reclassified-function P05102 hhaIM Haemophilus parahaemolyticus 735 Type II methyltransferase M.HhaI (M.HhaI) (EC 2.1.1.37) (Cytosine-specific methyltransferase HhaI) (Modification methylase HhaI) Strain ATCC 10014 was originally thought to originate from H.haemolyticus. {ECO:0000305}. reclassified-function Q2SMM6 dapB Hahella chejuensis (strain KCTC 2396) 349521 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9KC32 dapA1 Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans) 272558 4-hydroxy-tetrahydrodipicolinate synthase 1 (HTPA synthase 1) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9KA91 dapA2 Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans) 272558 4-hydroxy-tetrahydrodipicolinate synthase 2 (HTPA synthase 2) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9KC93 dapB Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans) 272558 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5V5D4 dapA Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) 272569 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5V5D5 dapB Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) 272569 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P29051 gdhX Halobacterium salinarum (Halobacterium halobium) 2242 NAD-specific glutamate dehydrogenase A (NAD-GDH A) (EC 1.4.1.2) Was initially thought to be a NADP-specific glutamate dehydrogenase. {ECO:0000305|PubMed:1766432}. reclassified-function B0R5N7 brp Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) 478009 Probable beta-carotene 15,15'-dioxygenase Brp (EC 1.13.11.63) (Bacteriorhodopsin-related protein) Was originally thought to regulate bop expression (PubMed:6093059). However, this seems to result from a polar effect on the downstream gene bat, which forms a transcription unit with brp. {ECO:0000305|PubMed:6093059}. reclassified-function A1WZ50 dapA Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) 349124 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1WX29 dapB Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) 349124 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O85041 csoS2 Halothiobacillus neapolitanus (strain ATCC 23641 / DSM 15147 / CIP 104769 / NCIMB 8539 / c2) (Thiobacillus neapolitanus) 555778 Carboxysome assembly protein CsoS2B (Carboxysome shell protein CsoS2B) Both Cso2A and Cso2B were originally thought to be glycosylated (PubMed:10525740). Later experiments do not show any evidence of glycosylation (PubMed:26608811). {ECO:0000269|PubMed:10525740, ECO:0000269|PubMed:26608811}. reclassified-function Q17WU7 dapA Helicobacter acinonychis (strain Sheeba) 382638 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q17XF1 dapB Helicobacter acinonychis (strain Sheeba) 382638 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7VFP9 dapA Helicobacter hepaticus (strain ATCC 51449 / 3B1) 235279 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7VIW7 dapB Helicobacter hepaticus (strain ATCC 51449 / 3B1) 235279 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O25657 dapA Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) 85962 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P94844 dapB Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) 85962 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P25178 lspA Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) 85962 Lipoprotein signal peptidase (EC 3.4.23.36) (Prolipoprotein signal peptidase) (Signal peptidase II) (SPase II) Was originally thought to be related to urease function. {ECO:0000305|PubMed:2001995}. reclassified-function Q09068 ureI Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) 85962 Acid-activated urea channel (Urease accessory protein UreI) Was originally (PubMed:1313413) thought to be an accessory protein required for nickel incorporation at the urease active site or for nickel transport. Actually, has been shown (PubMed:9712811) not to be required for the assembly of a catalytically active urease. {ECO:0000305|PubMed:1313413, ECO:0000305|PubMed:9712811}.; reclassified-function B5Z6I0 dapA Helicobacter pylori (strain G27) 563041 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B5Z6N2 dapB Helicobacter pylori (strain G27) 563041 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1CU72 dapA Helicobacter pylori (strain HPAG1) 357544 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q1CU21 dapB Helicobacter pylori (strain HPAG1) 357544 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9ZM13 dapA Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) 85963 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9ZLW6 dapB Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) 85963 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B6JL09 dapA Helicobacter pylori (strain P12) 570508 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B6JL92 dapB Helicobacter pylori (strain P12) 570508 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2USR7 dapA Helicobacter pylori (strain Shi470) 512562 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B2UTX8 dapB Helicobacter pylori (strain Shi470) 512562 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0THT2 dapA Heliobacterium modesticaldum (strain ATCC 51547 / Ice1) 498761 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4G724 dapA Herminiimonas arsenicoxydans 204773 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4G8E2 dapB Herminiimonas arsenicoxydans 204773 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0I260 dapA Histophilus somni (strain 129Pt) (Haemophilus somnus) 205914 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q0I3N1 dapB Histophilus somni (strain 129Pt) (Haemophilus somnus) 205914 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0UVZ8 dapA Histophilus somni (strain 2336) (Haemophilus somnus) 228400 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B0UU27 dapB Histophilus somni (strain 2336) (Haemophilus somnus) 228400 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q06277 ibpA Histophilus somni (strain 2336) (Haemophilus somnus) 228400 Protein adenylyltransferase and cysteine protease IbpA (HMW IgBP) (p120) [Cleaved into: Protein p76 IgBP (76 kDa antigen)] [Includes: Protein adenylyltransferase IbpA (EC 2.7.7.108) (AMPylator IbpA); Cysteine protease IbpA (EC 3.4.22.-)] Was originally [PubMed:8245839] thought to be a 76 kDa immunoglobulin-binding protein; it is now apparent that the gene is much longer but how it is translated and processed is unclear. {ECO:0000305}. reclassified-function Q9UNQ0 ABCG2 Homo sapiens (Human) 9606 Broad substrate specificity ATP-binding cassette transporter ABCG2 (EC 7.6.2.2) (ATP-binding cassette sub-family G member 2) (Breast cancer resistance protein) (CDw338) (Mitoxantrone resistance-associated protein) (Placenta-specific ATP-binding cassette transporter) (Urate exporter) (CD antigen CD338) Was originally proposed to function as a glutathione transporter (PubMed:20332504). However, some evidences suggest it is not the case (PubMed:24312054). {ECO:0000269|PubMed:20332504, ECO:0000269|PubMed:24312054}. reclassified-function Q8N2K0 ABHD12 Homo sapiens (Human) 9606 Lysophosphatidylserine lipase ABHD12 (EC 3.1.1.-) (2-arachidonoylglycerol hydrolase ABHD12) (Abhydrolase domain-containing protein 12) (hABHD12) (Monoacylglycerol lipase ABHD12) (EC 3.1.1.23) (Oxidized phosphatidylserine lipase ABHD12) (EC 3.1.-.-) A family suffering from Polyneuropathy, hearing loss, ataxia, retinitis pigmentosa, and cataract (PHARC) was initially clinically diagnosed with Usher syndrome type 3 (PubMed:22938382). Reexamination of one affected member of this family revealed ataxia but not polyneuropathy, demonstrating the phenotypic heterogeneity in PHARC and the need for careful neurological assessments to distinguish this disease from other neuropathic disorders (PubMed:22938382). {ECO:0000269|PubMed:22938382}. reclassified-function P25106 ACKR3 Homo sapiens (Human) 9606 Atypical chemokine receptor 3 (C-X-C chemokine receptor type 7) (CXC-R7) (CXCR-7) (Chemokine orphan receptor 1) (G protein-coupled receptor 159) (G protein-coupled receptor RDC1 homolog) (RDC-1) Was originally thought to be the receptor for VIP. {ECO:0000305|PubMed:1675791}. reclassified-function O15218 ACKR5 Homo sapiens (Human) 9606 Atypical chemokine receptor 5 (G protein-coupled receptor 182) Was originally thought to be a receptor for adrenomedullin (PubMed:9367907). However, this function was later not confirmed (PubMed:9535752). {ECO:0000269|PubMed:9367907, ECO:0000269|PubMed:9535752}. reclassified-function P49753 ACOT2 Homo sapiens (Human) 9606 Acyl-coenzyme A thioesterase 2, mitochondrial (Acyl-CoA thioesterase 2) (EC 3.1.2.2) (Acyl-coenzyme A thioester hydrolase 2a) (CTE-Ia) (Long-chain acyl-CoA thioesterase 2) (ZAP128) Was originally (PubMed:10944470) thought to be peroxisomal but was later shown (PubMed:16940157) to be mitochondrial. {ECO:0000305|PubMed:10944470, ECO:0000305|PubMed:16940157}. reclassified-function Q5U5Z8 AGBL2 Homo sapiens (Human) 9606 Cytosolic carboxypeptidase 2 (EC 3.4.17.-) (ATP/GTP-binding protein-like 2) (Protein deglutamylase CCP2) Was initially shown to catalyze the removal of carboxy-terminus tyrosine from alpha-tubulin (PubMed:21303978). However, later studies did not identified any detyrosinase or deglycylase activities from the carboxy-terminus of tubulin (By similarity). {ECO:0000250|UniProtKB:Q8CDK2, ECO:0000269|PubMed:21303978}.; reclassified-function Q02040 AKAP17A Homo sapiens (Human) 9606 A-kinase anchor protein 17A (AKAP-17A) (721P) (B-lymphocyte antigen) (Protein XE7) (Protein kinase A-anchoring protein 17A) (PRKA17A) (Splicing factor, arginine/serine-rich 17A) Was originally thought to be a cell surface protein involved in B-cell activation. {ECO:0000305|PubMed:1438229}. reclassified-function P02768 ALB Homo sapiens (Human) 9606 Albumin A peptide arising from positions 166 to 174 was originally (PubMed:3087352, PubMed:2437111) termed neurotensin-related peptide (NRP) or kinetensin and was thought to regulate fat digestion, lipid absorption, and blood flow. {ECO:0000305}. reclassified-function Q9BT30 ALKBH7 Homo sapiens (Human) 9606 RNA demethylase ALKBH7, mitochondrial (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 7) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial) (Spermatogenesis cell proliferation-related protein) (Spermatogenesis-associated protein 11) (pre-tRNA N1-methyl adenine demethylase ALKBH7) (pre-tRNA N2-dimethyl guanosine demethylase ALKBH7) Was initially reported to localize both in cytoplasm and nucleus (PubMed:17979886). However, it was later shown it localizes in mitochondrion (PubMed:23666923). The discrepancy is probably due to the use of a fusion protein with an N-terminal tag in the initial report (PubMed:17979886). {ECO:0000305|PubMed:17979886, ECO:0000305|PubMed:23666923}. reclassified-function Q96QP1 ALPK1 Homo sapiens (Human) 9606 Alpha-protein kinase 1 (EC 2.7.11.1) (Chromosome 4 kinase) (Lymphocyte alpha-protein kinase) D-glycero-beta-D-manno-heptose 1,7-bisphosphate (HBP) was initially thought to constitute the bacterial pathogen-associated molecular pattern metabolite (PAMP) triggering the ALPK1-TIFA innate immunune response (PubMed:28222186, PubMed:28877472). It was however shown that ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose) constitutes the main PAMP that activates the kinase activity of ALPK1 (PubMed:30111836). {ECO:0000269|PubMed:28222186, ECO:0000269|PubMed:28877472, ECO:0000269|PubMed:30111836}. reclassified-function Q06278 AOX1 Homo sapiens (Human) 9606 Aldehyde oxidase (EC 1.2.3.1) (Aldehyde oxidase 1) (Azaheterocycle hydroxylase) (EC 1.17.3.-) Was originally thought to be a xanthine dehydrogenase. {ECO:0000305|PubMed:8248161}. reclassified-function P18085 ARF4 Homo sapiens (Human) 9606 ADP-ribosylation factor 4 Was originally thought to be ARF2. {ECO:0000305}. reclassified-function Q9NP61 ARFGAP3 Homo sapiens (Human) 9606 ADP-ribosylation factor GTPase-activating protein 3 (ARF GAP 3) Was originally termed ARFGAP1. {ECO:0000305|PubMed:10704287}. reclassified-function Q9P2F6 ARHGAP20 Homo sapiens (Human) 9606 Rho GTPase-activating protein 20 (Rho-type GTPase-activating protein 20) The translocation involving this gene was originally published as t(X;11)(q13;23), but BRWD3 is localized to Xq21 and not to Xq13. {ECO:0000305|PubMed:15543602}. reclassified-function A6NK59 ASB14 Homo sapiens (Human) 9606 Ankyrin repeat and SOCS box protein 14 (ASB-14) Was originally derived from a readthrough transcript including ASB14 and DNAH12. {ECO:0000305}. reclassified-function O75882 ATRN Homo sapiens (Human) 9606 Attractin (DPPT-L) (Mahogany homolog) Was originally (PubMed:7539799, PubMed:9736737) thought to have dipeptidase activity but it was shown later to lack that activity. {ECO:0000305|PubMed:17261078}. reclassified-function P0DMR3 ATXN8OS Homo sapiens (Human) 9606 Putative protein ATXN8OS (ATXN8 opposite strand) (Spinocerebellar ataxia 8) (kelch-like 1 antisense) Product of a dubious CDS prediction. Translation must be initiated from a non-canonical GUG codon (PubMed:24040107). Overlaps with the ATXN8 gene but is transcribed in the opposite strand and was originally considered as non-protein coding (PubMed:10192387). {ECO:0000303|PubMed:10192387, ECO:0000303|PubMed:24040107}. reclassified-function Q96A70 AZIN2 Homo sapiens (Human) 9606 Antizyme inhibitor 2 (AzI2) (Arginine decarboxylase) (ADC) (ARGDC) (Ornithine decarboxylase-like protein) (ODC-like protein) (ornithine decarboxylase paralog) (ODC-p) Was initially reported to have ornithine decarboxylase (PubMed:11587527) or arginine decarboxylase (PubMed:14738999) activities, but it was later found that the mouse ortholog does not possess either of them. {ECO:0000305|PubMed:11587527, ECO:0000305|PubMed:14738999}. reclassified-function O43505 B4GAT1 Homo sapiens (Human) 9606 Beta-1,4-glucuronyltransferase 1 (EC 2.4.1.-) (I-beta-1,3-N-acetylglucosaminyltransferase) (iGnT) (N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase) (Poly-N-acetyllactosamine extension enzyme) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1) Was initially characterized as a beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine, able to initiate the synthesis or the elongation of the linear poly-N-acetyllactosaminoglycans (PubMed:9405606). However, it was later shown that it acts as a beta-1,4-glucuronyltransferase (PubMed:25279697, PubMed:25279699). {ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699, ECO:0000305|PubMed:9405606}. reclassified-function Q9H0W9 BKGD Homo sapiens (Human) 9606 Beta-keto L-gulonate decarboxylase (BKGD) (EC 4.1.1.34) Was originally thought to be an ester hydrolase (PubMed:16522806). However, has since been shown to be a 3-dehydro-L-gulonate decarboxylase, thus addressing the knowledge gap in the pentose pathway (PubMed:40737316). {ECO:0000269|PubMed:16522806, ECO:0000269|PubMed:40737316}. reclassified-function Q9H2G9 BLZF1 Homo sapiens (Human) 9606 Golgin-45 (Basic leucine zipper nuclear factor 1) (JEM-1) (p45 basic leucine-zipper nuclear factor) Was originally identified as a potential transcription factor, because of the presence of a potential basic motif and leucine-zipper domain, and because isoform 1 is detected in the nucleus upon heterologous expression. However, homology at several typical position for basic or hydrophobic residues is missing. Besides, another publication showed it is important for normal Golgi apparatus structure and function. {ECO:0000305|PubMed:11056056, ECO:0000305|PubMed:11739401, ECO:0000305|PubMed:9129147}. reclassified-function Q9Y3E2 BOLA1 Homo sapiens (Human) 9606 BolA-like protein 1 (hBolA) Was initially reported to be secreted via a non-classical export pathway (PubMed:18548201). It was however later shown that it localizes to mitochondria, in agreement with other members of the family (PubMed:22746225). {ECO:0000269|PubMed:18548201, ECO:0000269|PubMed:22746225}. reclassified-function Q6RI45 BRWD3 Homo sapiens (Human) 9606 Bromodomain and WD repeat-containing protein 3 The translocation involving this gene was originally published as t(X;11)(q13;23), but BRWD3 is localized to Xq21 and not to Xq13. {ECO:0000305|PubMed:15543602}. reclassified-function Q96EU7 C1GALT1C1 Homo sapiens (Human) 9606 C1GALT1-specific chaperone 1 (C38H2-like protein 1) (C38H2-L1) (Core 1 beta1,3-galactosyltransferase 2) (C1Gal-T2) (C1GalT2) (Core 1 beta3-Gal-T2) (Core 1 beta3-galactosyltransferase-specific molecular chaperone) Was originally (PubMed:12361956) assigned to be a glycosyltransferase. However, it was later shown (Ref.2 and PubMed:12464682) that it has no transferase activity and rather acts as a chaperone. {ECO:0000305|PubMed:12361956}. reclassified-function Q14444 CAPRIN1 Homo sapiens (Human) 9606 Caprin-1 (Cell cycle-associated protein 1) (Cytoplasmic activation- and proliferation-associated protein 1) (GPI-anchored membrane protein 1) (GPI-anchored protein p137) (GPI-p137) (p137GPI) (Membrane component chromosome 11 surface marker 1) (RNA granule protein 105) Was originally thought to be a GPI-anchored membrane protein. {ECO:0000305|PubMed:7657653}. reclassified-function P41180 CASR Homo sapiens (Human) 9606 Extracellular calcium-sensing receptor (CaR) (CaSR) (hCasR) (Parathyroid cell calcium-sensing receptor 1) (PCaR1) The active form of the homodimer was initially thought to display a symmetric configuration (PubMed:34916296). However, it was later shown to adopt an asymmetric configuration (PubMed:34194040, PubMed:37919470). {ECO:0000269|PubMed:34194040, ECO:0000269|PubMed:34916296, ECO:0000269|PubMed:37919470}. reclassified-function O75828 CBR3 Homo sapiens (Human) 9606 Carbonyl reductase [NADPH] 3 (EC 1.1.1.184) (NADPH-dependent carbonyl reductase 3) (Quinone reductase CBR3) (EC 1.6.5.10) (Short chain dehydrogenase/reductase family 21C member 2) There are conflicting results on the ability of CBR3 to metabolize menadione. Although menadione was originally reported as a good substrate of CBR3 (PubMed:15537833), results of later studies showed that CBR3 possesses very low or no activity toward menadione (PubMed:18493841, PubMed:19841672). {ECO:0000269|PubMed:15537833, ECO:0000269|PubMed:18493841, ECO:0000269|PubMed:19841672}. reclassified-function P13236 CCL4 Homo sapiens (Human) 9606 C-C motif chemokine 4 (G-26 T-lymphocyte-secreted protein) (HC21) (Lymphocyte activation gene 1 protein) (LAG-1) (MIP-1-beta(1-69)) (Macrophage inflammatory protein 1-beta) (MIP-1-beta) (PAT 744) (Protein H400) (SIS-gamma) (Small-inducible cytokine A4) (T-cell activation protein 2) (ACT-2) [Cleaved into: MIP-1-beta(3-69)] Was originally thought to be a ligand for CCR8. {ECO:0000305|PubMed:9521068}. reclassified-function P22674 CCNO Homo sapiens (Human) 9606 Cyclin-O Was originally thought to have uracil-DNA glycosylase (UDG) activity and wrongly named UNG2 and UDG2 (PubMed:2001396). It was later shown that it is a member of the cyclin family (PubMed:8419333). UNG2 corresponds to the isoform 2 of UNG gene. {ECO:0000305|PubMed:2001396, ECO:0000305|PubMed:8419333}. reclassified-function P51685 CCR8 Homo sapiens (Human) 9606 C-C chemokine receptor type 8 (C-C CKR-8) (CC-CKR-8) (CCR-8) (CC chemokine receptor CHEMR1) (CMKBRL2) (Chemokine receptor-like 1) (CKR-L1) (GPR-CY6) (GPRCY6) (TER1) (CD antigen CDw198) Was originally thought to be a receptor for SCYA3 and SCYA17. {ECO:0000305|PubMed:9521068}. reclassified-function Q9BWV3 CDADC1 Homo sapiens (Human) 9606 dCTP deaminase (EC 3.5.4.13) (Cytidine and dCMP deaminase domain-containing protein 1) (Deoxycytidine triphosphate deaminase) (Testis development protein NYD-SP15) CDADC1 was initially reported to exhibit cytidine deaminase activity (PubMed:26945630). However, subsequent studies demonstrated that it specifically deaminates dCTP, with no activity toward cytidine or deoxycytidine (PubMed:40324085, PubMed:40504152). The initial attribution may have been an artifact of using partially purified recombinant protein. While one study reported weak activity on dCMP, another failed to detect any dCMP deamination (PubMed:40324085, PubMed:40504152). {ECO:0000269|PubMed:26945630, ECO:0000269|PubMed:40324085, ECO:0000269|PubMed:40504152, ECO:0000305|PubMed:40324085}. reclassified-function Q9Y232 CDYL Homo sapiens (Human) 9606 Chromodomain Y-like protein (CDY-like) (Crotonyl-CoA hydratase) (EC 4.2.1.-) Was initially reported to display histone acetyltransferase activity, with a preference for histone H4 (PubMed:12072557). Such activity is however unsure in vivo. Histone acetyltransferase activity would be in contradiction with the function of the protein in corepressor complexes (PubMed:19061646, PubMed:22009739). Moreover, crystallographic studies demonstrated that it does not share any similarity with other acetyltransferases and instead forms a crotonase-like fold (PubMed:19507244). {ECO:0000269|PubMed:12072557, ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:19507244, ECO:0000269|PubMed:22009739}. reclassified-function P08861 CELA3B Homo sapiens (Human) 9606 Chymotrypsin-like elastase family member 3B (EC 3.4.21.70) (Elastase IIIB) (Elastase-3B) (Protease E) Was originally thought to be elastase 1. {ECO:0000305|PubMed:2737288}. reclassified-function Q5TB80 CEP162 Homo sapiens (Human) 9606 Centrosomal protein of 162 kDa (Cep162) (Protein QN1 homolog) Was initially thought to regulate chromosome segregation and mitotic spindle assembly (PubMed:16302001). However, it was later shown that its absence neither affect mitosis nor centriole duplication (PubMed:23644468). {ECO:0000305|PubMed:16302001, ECO:0000305|PubMed:23644468}. reclassified-function Q9Y5P4 CERT1 Homo sapiens (Human) 9606 Ceramide transfer protein (hCERT) (Collagen type IV alpha-3-binding protein) (Goodpasture antigen-binding protein) (GPBP) (START domain-containing protein 11) (StARD11) (StAR-related lipid transfer protein 11) Was originally reported to have a protein kinase activity and to phosphorylate on Ser and Thr residues the Goodpasture autoantigen (in vitro). {ECO:0000305|PubMed:10212244}. reclassified-function O43916 CHST1 Homo sapiens (Human) 9606 Carbohydrate sulfotransferase 1 (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 1) (GST-1) (Keratan sulfate Gal-6 sulfotransferase) (KS6ST) (KSGal6ST) (KSST) (EC 2.8.2.21) Was originally (PubMed:9639683) thought to be the ortholog of chicken CHST3 and therefore named C6ST. However, it has no strong chondroitin 6-sulfotransferase activity. {ECO:0000305|PubMed:9639683}. reclassified-function O75339 CILP Homo sapiens (Human) 9606 Cartilage intermediate layer protein 1 (CILP-1) (Cartilage intermediate-layer protein) [Cleaved into: Cartilage intermediate layer protein 1 C1; Cartilage intermediate layer protein 1 C2] Was originally thought to constitute the ATP pyrophosphatase enzyme (NTPPH). However, it was later shown (PubMed:12746903, PubMed:15864306) that it is not the case. {ECO:0000305}. reclassified-function Q05315 CLC Homo sapiens (Human) 9606 Galectin-10 (Gal-10) (Charcot-Leyden crystal protein) (CLC) (Eosinophil lysophospholipase) (Lysolecithin acylhydrolase) Was originally thought to possess lysophospholipase activity but the absence of this activity has been shown by PubMed:11834744. {ECO:0000305}. reclassified-function Q96KN2 CNDP1 Homo sapiens (Human) 9606 Beta-Ala-His dipeptidase (EC 3.4.13.20) (CNDP dipeptidase 1) (Carnosine dipeptidase 1) (Glutamate carboxypeptidase-like protein 2) (Serum carnosinase) The activity towards anserine which was originally shown with purified serum carnosine could not be confirmed. {ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:1903095}. reclassified-function O75131 CPNE3 Homo sapiens (Human) 9606 Copine-3 (Copine III) Was reported to have a protein kinase activity. {ECO:0000305|PubMed:11041869}. reclassified-function Q6UXB2 CXCL17 Homo sapiens (Human) 9606 C-X-C motif chemokine 17 (6-Cys CXCL17) (Dendritic cell and monocyte chemokine-like protein) (DMC) (VEGF coregulated chemokine 1) [Cleaved into: 4-Cys CXCL17] Was initially thought to activate the C-X-C chemokine receptor GPR35 (PubMed:25411203). However, it was later shown that GPR35 does not act as a receptor for CXCL17 (PubMed:29068046, PubMed:29875152). {ECO:0000269|PubMed:25411203, ECO:0000269|PubMed:29068046, ECO:0000269|PubMed:29875152}. reclassified-function P61073 CXCR4 Homo sapiens (Human) 9606 C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (FB22) (Fusin) (HM89) (LCR1) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Lipopolysaccharide-associated protein 3) (LAP-3) (LPS-associated protein 3) (NPYRL) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184) Was originally thought to be a receptor for neuropeptide Y type 3 (NPY3R) (NPY3-R) (PubMed:8234909, PubMed:8329116). Later reports showed that it acts as a receptor for the C-X-C chemokine CXCL12/SDF-1 (PubMed:10825158, PubMed:12034737, PubMed:9427609). {ECO:0000269|PubMed:10825158, ECO:0000269|PubMed:12034737, ECO:0000269|PubMed:9427609, ECO:0000305|PubMed:8234909, ECO:0000305|PubMed:8329116}. reclassified-function P04839 CYBB Homo sapiens (Human) 9606 NADPH oxidase 2 (EC 1.6.3.-) (CGD91-phox) (Cytochrome b(558) subunit beta) (Cytochrome b558 subunit beta) (Cytochrome b-245 heavy chain) (Heme-binding membrane glycoprotein gp91phox) (Neutrophil cytochrome b 91 kDa polypeptide) (Superoxide-generating NADPH oxidase heavy chain subunit) (gp91-1) (gp91-phox) (p22 phagocyte B-cytochrome) Originally thought to be the voltage-gated proton channel responsible for the proton efflux that compensates for the charge movement across the cell membrane (PubMed:10578014). But recent data do not support this idea (PubMed:11477065, PubMed:12034764). DeCoursey et al, show that the selectivity and gating kinetics of voltage-gated proton channels are identical regardless of whether CYBB is present in human myeloid leukemia cells line lacking or expressing CYBB (PubMed:11477065). In addition, no proton currents is detected in COS-7 cells transfected with CYBB (PubMed:12034764). {ECO:0000269|PubMed:10578014, ECO:0000269|PubMed:11477065, ECO:0000269|PubMed:12034764}. reclassified-function P33261 CYP2C19 Homo sapiens (Human) 9606 Cytochrome P450 2C19 (EC 1.14.14.1) ((R)-limonene 6-monooxygenase) (EC 1.14.14.53) ((S)-limonene 6-monooxygenase) (EC 1.14.14.51) ((S)-limonene 7-monooxygenase) (EC 1.14.14.52) (CYPIIC17) (CYPIIC19) (Cytochrome P450-11A) (Cytochrome P450-254C) (Fenbendazole monooxygenase (4'-hydroxylating)) (EC 1.14.14.75) (Mephenytoin 4-hydroxylase) P450-254C was originally listed as a separate gene (CYP2C17). Resequencing demonstrated that it is not a separate gene, but a chimera. The 5'-portion corresponds to a partial 2C18 clone, and the 3'-portion corresponds to a partial 2C19 clone. {ECO:0000305}. reclassified-function Q5TCH4 CYP4A22 Homo sapiens (Human) 9606 Cytochrome P450 4A22 (CYPIVA22) (Fatty acid omega-hydroxylase) (Lauric acid omega-hydroxylase) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.14.80) Was originally termed CYP4A11. {ECO:0000305|PubMed:10860550}. reclassified-function O95865 DDAH2 Homo sapiens (Human) 9606 Putative hydrolase DDAH2 (EC 3.-.-.-) (DDAHII) (Inactive N(G),N(G)-dimethylarginine dimethylaminohydrolase 2) (DDAH-2) (Inactive dimethylarginine dimethylaminohydrolase 2) (Protein G6a) (S-phase protein) Was originally thought to be a dimethylarginine dimethylaminohydrolase (with EC:3.5.3.18) able to hydrolyze N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) (PubMed:10493931). However, a recent multicentre study has shown that DDAH2 does not have dimethylarginine dimethylaminohydrolase activity by using different approaches (PubMed:21493890, PubMed:37296100). {ECO:0000269|PubMed:10493931, ECO:0000269|PubMed:21493890, ECO:0000269|PubMed:37296100}. reclassified-function Q5TDH0 DDI2 Homo sapiens (Human) 9606 Protein DDI1 homolog 2 (EC 3.4.23.-) The protein was initially thought to be catalytically inactive (PubMed:27461074). It was later shown that it has aspartyl protease activity and mediates cleavage of NFE2L1/NRF1 (PubMed:27676298). {ECO:0000269|PubMed:27461074, ECO:0000269|PubMed:27676298}. reclassified-function Q9Y394 DHRS7 Homo sapiens (Human) 9606 Dehydrogenase/reductase SDR family member 7 (EC 1.1.1.-) (Retinal short-chain dehydrogenase/reductase 4) (retSDR4) (Short chain dehydrogenase/reductase family 34C member 1) (Protein SDR34C1) DHRS7 was originally reported to be anchored in the endoplasmic reticulum membrane and facing the lumen (PubMed:24246760). However, the catalytic moiety was later shown to be facing the cytosol (PubMed:28457967). {ECO:0000269|PubMed:24246760, ECO:0000269|PubMed:28457967}. reclassified-function Q6ZR08 DNAH12 Homo sapiens (Human) 9606 Dynein axonemal heavy chain 12 (Axonemal beta dynein heavy chain 12) (Axonemal dynein heavy chain 12-like protein) (Axonemal dynein heavy chain 7-like protein) (Ciliary dynein heavy chain 12) (Dynein axonemal heavy chain 7-like) (Dynein heavy chain domain-containing protein 2) Was originally derived from a readthrough transcript including ASB14 and DNAH12. DNHD2 was thought to be a distinct gene. {ECO:0000305}. reclassified-function Q9BVJ7 DUSP23 Homo sapiens (Human) 9606 Dual specificity protein phosphatase 23 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular mass dual specificity phosphatase 3) (LDP-3) (VH1-like phosphatase Z) Was originally erroneously termed DUSP25. {ECO:0000305}. reclassified-function P51808 DYNLT3 Homo sapiens (Human) 9606 Dynein light chain Tctex-type 3 (Protein 91/23) (T-complex-associated testis-expressed 1-like) Was originally thought to be a candidate for RP3. {ECO:0000305|PubMed:8004092}. reclassified-function O00559 EBAG9 Homo sapiens (Human) 9606 Receptor-binding cancer antigen expressed on SiSo cells (Cancer-associated surface antigen RCAS1) (Estrogen receptor-binding fragment-associated gene 9 protein) It was initially reported to be a ligand for some putative receptor present on T-, B-, natural killer (NK) cells and various human cell lines. However, PubMed:12672804 showed that it does not bind any receptor. {ECO:0000305}. reclassified-function Q8WVE0 EEF1AKMT1 Homo sapiens (Human) 9606 EEF1A lysine methyltransferase 1 (EC 2.1.1.-) (N(6)-adenine-specific DNA methyltransferase 2) (Protein-lysine N-methyltransferase N6AMT2) (eEF1A-KMT) Was originally thought to be an N(6)-adenine-specific DNA methyltransferase based on primary sequence and predicted secondary structure. {ECO:0000255|HAMAP-Rule:MF_03187}. reclassified-function Q9GZT9 EGLN1 Homo sapiens (Human) 9606 Egl nine homolog 1 (EC 1.14.11.29) (Hypoxia-inducible factor prolyl hydroxylase 2) (HIF-PH2) (HIF-prolyl hydroxylase 2) (HPH-2) (Prolyl hydroxylase domain-containing protein 2) (PHD2) (SM-20) It was previously reported that this protein was the ortholog of rat SM-20. However, EGLN3 is now considered the true ortholog of rat SM-20 since it shows substantially greater similarity. {ECO:0000305}. reclassified-function Q96KQ7 EHMT2 Homo sapiens (Human) 9606 Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (EC 2.1.1.367) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Lysine N-methyltransferase 1C) (Protein G9a) While NG36 and G9a were originally thought to derive from 2 separate genes, all G9A transcripts also contain the in frame coding sequence of NG36. {ECO:0000305|PubMed:11707778}.; reclassified-function Q9BY44 EIF2A Homo sapiens (Human) 9606 Eukaryotic translation initiation factor 2A (eIF-2A) (65 kDa eukaryotic translation initiation factor 2A) [Cleaved into: Eukaryotic translation initiation factor 2A, N-terminally processed] This gene should not be confused with EIF2S1, frequently called eIF2-alpha in the literature, and with which it shares the alias EIF2A. EIF2S1 is the alpha subunit of the eIF2 translation initiation complex. Although both of these proteins function in binding initiator tRNA to the 40S ribosomal subunit, the EIF2A protein does so in a codon-dependent manner, whereas eIF2 complex requires GTP. Was initially thought to constitute the ortholog of prokaryotic IF-2 (infB) protein. {ECO:0000305}. reclassified-function P06730 EIF4E Homo sapiens (Human) 9606 Eukaryotic translation initiation factor 4E (eIF-4E) (eIF4E) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) Was originally thought to be phosphorylated on Ser-53 (PubMed:3112145). However, it was later shown that the major phosphorylation site is Ser-209 (By similarity). {ECO:0000250|UniProtKB:A0A9J7FAT4, ECO:0000269|PubMed:3112145}. reclassified-function O95163 ELP1 Homo sapiens (Human) 9606 Elongator complex protein 1 (ELP1) (IkappaB kinase complex-associated protein) (IKK complex-associated protein) (p150) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:11714725, ECO:0000305|PubMed:11818576, ECO:0000305|PubMed:29332244}. reclassified-function Q6IA86 ELP2 Homo sapiens (Human) 9606 Elongator complex protein 2 (ELP2) (SHINC-2) (STAT3-interacting protein 1) (StIP1) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:11714725, ECO:0000305|PubMed:11818576, ECO:0000305|PubMed:29332244}. reclassified-function Q9H9T3 ELP3 Homo sapiens (Human) 9606 Elongator complex protein 3 (hELP3) (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:11714725, ECO:0000305|PubMed:11818576, ECO:0000305|PubMed:15902492, ECO:0000305|PubMed:16713582, ECO:0000305|PubMed:29332244}.; reclassified-function Q96EB1 ELP4 Homo sapiens (Human) 9606 Elongator complex protein 4 (hELP4) (PAX6 neighbor gene protein) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:11714725, ECO:0000305|PubMed:11818576, ECO:0000305|PubMed:16713582, ECO:0000305|PubMed:29332244}. reclassified-function Q8TE02 ELP5 Homo sapiens (Human) 9606 Elongator complex protein 5 (Dermal papilla-derived protein 6) (S-phase 2 protein) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:29332244}. reclassified-function Q0PNE2 ELP6 Homo sapiens (Human) 9606 Elongator complex protein 6 (Angiotonin-transactivated protein 1) (Protein TMEM103) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:29332244}. reclassified-function Q8N8Q3 ENDOV Homo sapiens (Human) 9606 Endonuclease V (hEndoV) (EC 3.1.26.-) (Inosine-specific endoribonuclease) Was initially characterized as an endodeoxyribonuclease involved in DNA repair (PubMed:22664237). While it shows some weak endodeoxyribonuclease activity in vitro, such activity probably does not exist in vivo. {ECO:0000305|PubMed:22664237}. reclassified-function Q7L5Y1 ENOSF1 Homo sapiens (Human) 9606 Mitochondrial enolase superfamily member 1 (EC 4.2.1.68) (Antisense RNA to thymidylate synthase) (rTS) (L-fuconate dehydratase) Was originally (PubMed:8493092) identified as a gene coding for an antisense RNA to thymidylate synthase, and was proposed to down-regulate TYMS activity (PubMed:8869746), possibly by promoting the degradation of TYMS mRNA via an antisense RNA-based mechanism (PubMed:12084460). {ECO:0000305|PubMed:12084460, ECO:0000305|PubMed:8493092, ECO:0000305|PubMed:8869746}. reclassified-function Q6ZTU2 EP400P1 Homo sapiens (Human) 9606 Putative chromatin regulator EP400P1 (EP400 N-terminal-like) (EP400 pseudogene 1) (Putative EP400-like protein) Was previously described as a putative pseudogene. {ECO:0000305}. reclassified-function P07814 EPRS1 Homo sapiens (Human) 9606 Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)] Was originally thought to be a glutaminyl-tRNA synthetase. {ECO:0000305}. reclassified-function Q2NKX8 ERCC6L Homo sapiens (Human) 9606 DNA excision repair protein ERCC-6-like (EC 3.6.4.12) (ATP-dependent helicase ERCC6-like) (PLK1-interacting checkpoint helicase) (Tumor antigen BJ-HCC-15) Was initially thought to play a role in the spindle checkpoint. However, it was later shown that phenotypes initially observed are due to off-target effects of the siRNA used which results in MAD2L1 down-regulation and mis-localization. {ECO:0000305|PubMed:17218258, ECO:0000305|PubMed:19904549}. reclassified-function Q96JP0 FEM1C Homo sapiens (Human) 9606 Protein fem-1 homolog C (FEM1c) (FEM1-gamma) Was initially thought to be the ortholog of mouse FEM1A. {ECO:0000305|PubMed:11733146}. reclassified-function Q9BVA6 FICD Homo sapiens (Human) 9606 Protein adenylyltransferase FICD (EC 2.7.7.108) (AMPylator FICD) (De-AMPylase FICD) (EC 3.1.4.-) (FIC domain-containing protein) (Huntingtin yeast partner E) (Huntingtin-interacting protein 13) (HIP-13) (Huntingtin-interacting protein E) Was initially thought to mediate AMPylation of HSPA5/BiP at 'Ser-365' and 'Thr-366' in vitro, leading to activate HSPA5/BiP (PubMed:25601083). However, it was later shown that it mediates AMPylation of HSPA5/BiP at 'Thr-518', leading to inactivate HSPA5/BiP. {ECO:0000250|UniProtKB:A0A061I403, ECO:0000269|PubMed:25601083}. reclassified-function Q8NFG4 FLCN Homo sapiens (Human) 9606 Folliculin (BHD skin lesion fibrofolliculoma protein) (Birt-Hogg-Dube syndrome protein) Based on its structure and in vitro assays, was initially thought to have guanine nucleotide exchange factor (GEF) activity (PubMed:22977732). However, subsequent studies showed that it does not act as GEF in vivo (PubMed:24095279). {ECO:0000269|PubMed:22977732, ECO:0000269|PubMed:24095279}. reclassified-function P31512 FMO4 Homo sapiens (Human) 9606 Dimethylaniline monooxygenase [N-oxide-forming] 4 (EC 1.14.13.8) (Dimethylaniline oxidase 4) (Hepatic flavin-containing monooxygenase 4) (FMO 4) Was originally termed FMO2. {ECO:0000305|PubMed:1417778}. reclassified-function Q01167 FOXK2 Homo sapiens (Human) 9606 Forkhead box protein K2 (G/T-mismatch specific binding protein) (nGTBP) (Interleukin enhancer-binding factor 1) Was initially named FOXK1a by some reports (PubMed:12402362, PubMed:16624804). It should not be confused with FOXK1 (AC P85037) paralog. {ECO:0000303|PubMed:12402362, ECO:0000303|PubMed:16624804, ECO:0000305}. reclassified-function Q14331 FRG1 Homo sapiens (Human) 9606 Protein FRG1 (FSHD region gene 1 protein) Was originally thought to be located in nuclear speckles based on overexpression of the protein (PubMed:15060122). However, the endogenous protein was later shown not be expressed in nuclear speckles (PubMed:21699900). {ECO:0000305|PubMed:15060122, ECO:0000305|PubMed:21699900}. reclassified-function Q8N3T1 GALNT15 Homo sapiens (Human) 9606 Polypeptide N-acetylgalactosaminyltransferase 15 (EC 2.4.1.41) (Polypeptide GalNAc transferase-like protein 2) (GalNAc-T-like protein 2) (pp-GaNTase-like protein 2) (Polypeptide N-acetylgalactosaminyltransferase-like protein 2) (Protein-UDP acetylgalactosaminyltransferase-like protein 2) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2) Was originally termed Galnt15/pp-GaNTase 15. {ECO:0000305|PubMed:15147861}. reclassified-function P16383 GCFC2 Homo sapiens (Human) 9606 Intron Large complex component GCFC2 (GC-rich sequence DNA-binding factor) (GC-rich sequence DNA-binding factor 2) (Transcription factor 9) (TCF-9) Was originally thought to be a DNA-binding transcriptional repressor. However, later work showed that the original sequence was a chimera and that the DNA-binding activity was derived from the incorrect N-terminal sequence. {ECO:0000305|PubMed:10500253, ECO:0000305|PubMed:2556218}. reclassified-function P36959 GMPR Homo sapiens (Human) 9606 GMP reductase 1 (GMPR 1) (EC 1.7.1.7) (Guanosine 5'-monophosphate oxidoreductase 1) (Guanosine monophosphate reductase 1) The N-terminus was initially (PubMed:2758468) thought to be fused with glucose-6-phosphate-dehydrogenase (G6PD) protein in vivo. However, PubMed:2570640 showed that it encodes a GMP reductase, and PubMed:1694726 showed that the chimeric protein is an artifact. {ECO:0000305|PubMed:2758468}. reclassified-function Q8NHS2 GOT1L1 Homo sapiens (Human) 9606 Aspartate aminotransferase, cytoplasmic 2 (EC 2.6.1.1) (Glutamate oxaloacetate transaminase 1-like protein 1) (Transaminase A-like protein 1) Was reported to exhibit Asp racemase activity (By similarity). However, one study in humans did not confirm this activity (PubMed:25287256). Similarly, a study in mice also failed to demonstrate aspartate racemase activity (By similarity). {ECO:0000250|UniProtKB:Q7TSV6, ECO:0000269|PubMed:25287256}.; reclassified-function P47775 GPR12 Homo sapiens (Human) 9606 G protein-coupled receptor 12 Was originally (PubMed:12220620) thought to be a receptor for sphingosine 1-phosphate. It has been demonstrated that it is not the case in human (PubMed:19286662). {ECO:0000305|PubMed:12220620, ECO:0000305|PubMed:19286662}. reclassified-function P46089 GPR3 Homo sapiens (Human) 9606 G protein-coupled receptor 3 (ACCA orphan receptor) Was originally (PubMed:12220620) thought to be a receptor for sphingosine 1-phosphate. PubMed:19286662 demonstrated that it is not the case. {ECO:0000305|PubMed:12220620}. reclassified-function Q9HC97 GPR35 Homo sapiens (Human) 9606 G protein-coupled receptor 35 (Kynurenic acid receptor) (KYNA receptor) Was initially thought to act as a receptor for the C-X-C chemokine receptor CXCL17 (PubMed:25411203). However, it was later shown to not act as a receptor for CXCL17 (PubMed:29068046, PubMed:29875152). {ECO:0000269|PubMed:25411203, ECO:0000269|PubMed:29068046, ECO:0000269|PubMed:29875152}. reclassified-function P46095 GPR6 Homo sapiens (Human) 9606 G protein-coupled receptor 6 (Sphingosine 1-phosphate receptor GPR6) Was originally (PubMed:12220620) thought to be a receptor for sphingosine 1-phosphate. It has been demonstrated that it is not the case (PubMed:19286662). {ECO:0000305|PubMed:12220620, ECO:0000305|PubMed:19286662}. reclassified-function O43424 GRID2 Homo sapiens (Human) 9606 Glutamate receptor ionotropic, delta-2 (GluD2) (GluR delta-2 subunit) The ligand-gated cation channel activity was previously disputed due to a lack of evidence for direct ligand-gated ion channel activity (PubMed:39052831). However, structural studies have shown an asymmetric opening of the ion channel upon D-serine binding, and this would explain the lack of activity in the absence of D-serine (PubMed:40957579). {ECO:0000269|PubMed:39052831, ECO:0000269|PubMed:40957579}. reclassified-function P35269 GTF2F1 Homo sapiens (Human) 9606 General transcription factor IIF subunit 1 (General transcription factor IIF 74 kDa subunit) (Transcription initiation factor IIF subunit alpha) (TFIIF-alpha) (Transcription initiation factor RAP74) Was reported to have a protein kinase activity and to autophosphorylates on Ser-385 and Thr-389. {ECO:0000305|PubMed:10428810}. reclassified-function P20671 H2AC7 Homo sapiens (Human) 9606 Histone H2A type 1-D (Histone H2A.3) (Histone H2A/g) Was originally thought to originate from mouse. {ECO:0000305|PubMed:2587222}. reclassified-function Q9Y5N5 HEMK2 Homo sapiens (Human) 9606 Methyltransferase HEMK2 (HemK methyltransferase family member 2) (M.HsaHemK2P) (Lysine N-methyltransferase 9) (EC 2.1.1.-) (Methylarsonite methyltransferase N6AMT1) (EC 2.1.1.-) (Methyltransferase N6AMT1) (Protein N(5)-glutamine methyltransferase) (EC 2.1.1.-) Was reported to have N(6)-adenine-specific DNA methyltransferase by mediating methylation of DNA on the 6th position of adenine (N(6)-methyladenosine) (PubMed:30017583). The existence of N(6)-methyladenosine on DNA is unclear in mammals (PubMed:32203414). According to a report, the majority of N(6)-methyladenosine in DNA originates from RNA catabolism via a nucleotide salvage pathway and is misincorporated by DNA polymerases, arguing against a role as epigenetic DNA mark in mammalian cells (PubMed:32203414). Moreover, subsequent studies could not confirm the role of HEMK2 as a N(6)-adenine-specific DNA methyltransferase (PubMed:30392959, PubMed:31632689, PubMed:31636962). {ECO:0000269|PubMed:30017583, ECO:0000269|PubMed:30392959, ECO:0000269|PubMed:31632689, ECO:0000269|PubMed:31636962, ECO:0000269|PubMed:32203414}. reclassified-function P49773 HINT1 Homo sapiens (Human) 9606 Adenosine 5'-monophosphoramidase HINT1 (EC 3.9.1.-) (Desumoylating isopeptidase HINT1) (EC 3.4.22.-) (Histidine triad nucleotide-binding protein 1) (Protein kinase C inhibitor 1) (Protein kinase C-interacting protein 1) (PKCI-1) Was originally thought to be a protein kinase C inhibitor and to bind zinc in solution. Both seem to be incorrect. {ECO:0000305}. reclassified-function Q96FZ2 HMCES Homo sapiens (Human) 9606 Abasic site processing protein HMCES (EC 4.-.-.-) (Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein) (ES cell-specific 5hmC-binding protein) (Peptidase HMCES) (EC 3.4.-.-) (SRAP domain-containing protein 1) Was initially reported to specifically bind 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells (By similarity). It was later suggested to act as an endonuclease that specifically cleaves 5hmC-containing DNA (By similarity). However, the endonuclease activity on 5hmC-containing DNA could not be confirmed by another report (PubMed:30554877). {ECO:0000250|UniProtKB:Q8R1M0, ECO:0000269|PubMed:30554877}. reclassified-function Q9BPX1 HSD17B14 Homo sapiens (Human) 9606 L-fucose dehydrogenase (EC 1.1.1.122) (17-beta-hydroxysteroid dehydrogenase DHRS10) (Dehydrogenase/reductase SDR family member 10) (Retinal short-chain dehydrogenase/reductase retSDR3) (Short chain dehydrogenase/reductase family 47C member 1) Was reported as a 17-beta-hydroxysteroid dehydrogenase that catalyzes estradiol and testosterone oxidation in the C17-hydroxyl group to form estrone and androstenedione, respectively (in vitro). However, HSD17B14 is very inefficient in oxidizing steroids, testosterone, suggesting that steroids cannot be physiological substrates for HSD17B14. {ECO:0000269|PubMed:17067289, ECO:0000269|PubMed:38944119}. reclassified-function P14625 HSP90B1 Homo sapiens (Human) 9606 Endoplasmin (EC 3.6.4.-) (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Heat shock protein family C member 4) (Tumor rejection antigen 1) (gp96 homolog) Was originally thought to function in endoplasmic reticulum associated degradation (ERAD) (PubMed:18264092). However, it was later shown that hyperglycosylated form of HSP90B1 is a target of ERAD and is not involved in ERAD itself (PubMed:18264092). {ECO:0000269|PubMed:18264092}. reclassified-function P11021 HSPA5 Homo sapiens (Human) 9606 Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) AMPylation was initially reported to take place at Ser-365 and Thr-366 in vitro, and promote activation of HSPA5/BiP (PubMed:25601083). However, it was later shown that AMPylation takes place at Thr-518 and leads to inactivation of HSPA5/BiP. {ECO:0000250|UniProtKB:G3I8R9, ECO:0000269|PubMed:25601083}. reclassified-function Q9BUP3 HTATIP2 Homo sapiens (Human) 9606 Protein HTATIP2 (30 kDa HIV-1 TAT-interacting protein) (HIV-1 TAT-interactive protein 2) Was originally (PubMed:9482853, PubMed:10698937) thought to be a transcriptional coregulator with protein kinase activity. However, crystal structure reveals a short chain dehydrogenase/reductase fold binding NADPH rather than ATP. {ECO:0000305}. reclassified-function Q9Y547 IFT25 Homo sapiens (Human) 9606 Intraflagellar transport protein 25 homolog (Heat shock protein beta-11) (Hspb11) (Heat shock protein family B member 11) (Placental protein 25) (PP25) Was initially classified as a member of the small heat shock family protein. However, it was later shown that it is not the case (PubMed:19921466). {ECO:0000305|PubMed:19921466}. reclassified-function P01877 IGHA2 Homo sapiens (Human) 9606 Immunoglobulin heavy constant alpha 2 (Ig alpha-2 chain C region) (Ig alpha-2 chain C region BUT) (Ig alpha-2 chain C region LAN) N-glycosylation was reported in milk on the non-canonical Asn-92 site (PubMed:18780401). However, according to Ref.15, N-glycosylation from the same tissue was found to be absent at this site. {ECO:0000305|Ref.15}.; reclassified-function Q13123 IK Homo sapiens (Human) 9606 Protein Red (Cytokine IK) (IK factor) (Protein RER) Was originally thought to be the IK factor, a cytokine involved in the negative regulatory pathway of constitutive MHC class II antigens expression. {ECO:0000305|PubMed:7970704}. reclassified-function Q13418 ILK Homo sapiens (Human) 9606 Scaffold protein ILK (ILK-1) (ILK-2) (Inactive integrin-linked kinase) (p59ILK) Was originally thought to act as a serine/threonine-protein kinase (PubMed:8538749). Now thought to be a pseudokinase which does not have kinase activity and which functions solely as a scaffold protein (PubMed:20005845, PubMed:21524996, PubMed:30367047). {ECO:0000269|PubMed:20005845, ECO:0000269|PubMed:21524996, ECO:0000269|PubMed:30367047, ECO:0000303|PubMed:8538749}. reclassified-function Q96N16 JAKMIP1 Homo sapiens (Human) 9606 Janus kinase and microtubule-interacting protein 1 (GABA-B receptor-binding protein) (Multiple alpha-helices and RNA-linker protein 1) (Marlin-1) Was originally thought to bind single-stranded RNA molecules and regulate GABA-B receptor expression. {ECO:0000305|PubMed:14718537}. reclassified-function Q6NYC1 JMJD6 Homo sapiens (Human) 9606 Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR) Was initially thought to constitute the phosphatidylserine receptor, a receptor that mediates recognition of phosphatidylserine, a specific marker only present at the surface of apoptotic cells. Phosphatidylserine receptor probably participates in apoptotic cell phagocytosis. This protein was identified using phage display expressing mAb 217, an antibody that specifically recognizes phosphatidylserine receptor. However, its nuclear localization and the fact that mAb 217 antibody still recognizes the phosphatidylserine receptor in mice lacking JMJD6, strongly suggest that it does not constitute the receptor for phosphatidylserine and is not involved in apoptotic cell removal. {ECO:0000305}. reclassified-function P82909 KGD4 Homo sapiens (Human) 9606 Alpha-ketoglutarate dehydrogenase component 4 (Alpha-ketoglutarate dehydrogenase subunit 4) Was originally identified in the small subunit (28S) of mitochondrial ribosomes that were purified on sucrose gradients (By similarity). This observation has been challenged by experiments showing KGD4 copurification with the oxoglutarate dehydrogenase complex (OGDHC), also called alpha-ketoglutarate dehydrogenase complex (KGDH). Both mitochondrial ribosome 28S subunit and OGDC have a similar size and OGDC is highly abundant, therefore OGDC has been found to contaminate ribosomal preparations performed by sequential centrifugation steps (By similarity). In addition, KGD4 could not be located in the structure of the human mitochondrial ribosome, supporting the hypothesis that it is not a mitoribosomal protein (PubMed:25838379). {ECO:0000250|UniProtKB:P82908, ECO:0000250|UniProtKB:Q9CQX8, ECO:0000269|PubMed:25838379}. reclassified-function Q96EK5 KIFBP Homo sapiens (Human) 9606 KIF-binding protein (KIF1-binding protein) (Kinesin family binding protein) Was originally shown to localize in the mitochondrion and to play a role in mitochondrial transport (PubMed:16225668). Recent articles, however, have shown that it does not localize to mitochondria, it interacts with the cytoskeleton and does not have a role in mitochondrial function (PubMed:20621975, PubMed:23427148). {ECO:0000305|PubMed:16225668, ECO:0000305|PubMed:20621975, ECO:0000305|PubMed:23427148}. reclassified-function O14901 KLF11 Homo sapiens (Human) 9606 Krueppel-like factor 11 (Transforming growth factor-beta-inducible early growth response protein 2) (TGFB-inducible early growth response protein 2) (TIEG-2) PubMed:11087666 sequence was originally thought to originate from mouse. {ECO:0000305}. reclassified-function Q9UH77 KLHL3 Homo sapiens (Human) 9606 Kelch-like protein 3 The BCR(KLHL3) complex was initially thought to act by mediating ubiquitination of SLC12A3/NCC (PubMed:22406640). However, it was later shown that effects on SLC12A3/NCC are indirect and caused by impaired ubiquitination of WNK4 (PubMed:23387299). {ECO:0000305|PubMed:22406640, ECO:0000305|PubMed:23387299}. reclassified-function P04264 KRT1 Homo sapiens (Human) 9606 Keratin, type II cytoskeletal 1 (67 kDa cytokeratin) (Cytokeratin-1) (CK-1) (Hair alpha protein) (Keratin-1) (K1) (Type-II keratin Kb1) A peptide corresponding to residues 278 to 289 was isolated as part of plant proteomics studies and was originally thought to be of plant origin (PubMed:16529377, PubMed:18602030, PubMed:19412582). However, it was later shown that it is likely to be human type II keratin, a common contaminant in proteomic analyzes (PubMed:23895828). {ECO:0000305|PubMed:23895828}. reclassified-function Q14CN4 KRT72 Homo sapiens (Human) 9606 Keratin, type II cytoskeletal 72 (Cytokeratin-72) (CK-72) (Keratin-72) (K72) (Type II inner root sheath-specific keratin-K6irs2) (Type-II keratin Kb35) Was initially thought to be the ortholog of mouse KRT71. {ECO:0000305|PubMed:11703281}. reclassified-function P35527 KRT9 Homo sapiens (Human) 9606 Keratin, type I cytoskeletal 9 (Cytokeratin-9) (CK-9) (Keratin-9) (K9) Was originally thought to be a 60 kDa chain of placental scatter protein. {ECO:0000305|PubMed:2140676}. reclassified-function P83111 LACTB Homo sapiens (Human) 9606 Serine beta-lactamase-like protein LACTB, mitochondrial (EC 3.4.-.-) Was originally identified as mitochondrial large ribosomal subunit protein mL56 (MRP-L56) (PubMed:11551941), but has since been shown to localize to the mitochondrial intermembrane space where it forms filaments (PubMed:19858488). {ECO:0000305|PubMed:11551941, ECO:0000305|PubMed:19858488}. reclassified-function P50851 LRBA Homo sapiens (Human) 9606 Lipopolysaccharide-responsive and beige-like anchor protein (Beige-like protein) (CDC4-like protein) Was originally said to be similar to yeast CDC4, but that similarity is very limited. {ECO:0000305|PubMed:1505956}. reclassified-function P55145 MANF Homo sapiens (Human) 9606 Mesencephalic astrocyte-derived neurotrophic factor (Arginine-rich protein) (Protein ARMET) Was originally (PubMed:8649854, PubMed:8971156, PubMed:9174057) thought to be much longer and included an arginine-rich region thought to be the target of cancer-causing mutations. All these mutations are in what is now thought to be the 5'-UTR of the mRNA. {ECO:0000305}.; reclassified-function P04201 MAS1 Homo sapiens (Human) 9606 Proto-oncogene Mas Was originally thought to be a receptor for angiotensin II. {ECO:0000305|PubMed:3419518}. reclassified-function Q9UJA3 MCM8 Homo sapiens (Human) 9606 DNA helicase MCM8 (EC 5.6.2.4) (DNA 3'-5' helicase MCM8) (Minichromosome maintenance 8) Was initially thought to play a role in DNA replication (PubMed:15684404). However, it was later shown that it is mainly involved in homologous recombination repair (PubMed:23401855). {ECO:0000305|PubMed:15684404, ECO:0000305|PubMed:23401855}. reclassified-function Q14676 MDC1 Homo sapiens (Human) 9606 Mediator of DNA damage checkpoint protein 1 (Nuclear factor with BRCT domains 1) Phosphorylation at Ser-329 and Thr-331 by CK2 was initially thought to play a major role in the interaction with TOPBP1 (PubMed:23891287). However, it was later shown that phosphorylation at Ser-168 and Ser-196 promote interaction with TOPBP1 (PubMed:30898438). {ECO:0000269|PubMed:23891287, ECO:0000269|PubMed:30898438}. reclassified-function Q16626 MEA1 Homo sapiens (Human) 9606 Male-enhanced antigen 1 (MEA-1) Was originally thought to be the H-Y antigen. {ECO:0000305}.; reclassified-function Q15049 MLC1 Homo sapiens (Human) 9606 Membrane protein MLC1 (Megalencephalic leukoencephalopathy with subcortical cysts protein 1) Was initially predicted to function as cation channel based on marginal amino acid sequence homology with a voltage-gated K+ channel KCNA1. {ECO:0000269|PubMed:11326298}. reclassified-function Q9NZB8 MOCS1 Homo sapiens (Human) 9606 Molybdenum cofactor biosynthesis protein 1 (Cell migration-inducing gene 11 protein) (Molybdenum cofactor synthesis-step 1 protein A-B) [Includes: GTP 3',8-cyclase (EC 4.1.99.22) (MOCS1A) (Molybdenum cofactor biosynthesis protein A); Cyclic pyranopterin monophosphate synthase (EC 4.6.1.17) (MOCS1B) (Molybdenum cofactor biosynthesis protein C)] The C-terminus of MOCS1A was previously believed to be thiocarboxylated, but it is now known not to be the case. {ECO:0000305|PubMed:25697423}. reclassified-function P25325 MPST Homo sapiens (Human) 9606 3-mercaptopyruvate sulfurtransferase (MST) (EC 2.8.1.2) Was originally thought to be rhodanese. {ECO:0000305|PubMed:1953758}. reclassified-function Q96LA9 MRGPRX4 Homo sapiens (Human) 9606 Mas-related G protein-coupled receptor member X4 (Sensory neuron-specific G protein-coupled receptor 5/6) Bilirubin IXalpha was initially reported to act as a ligand (PubMed:30657454). However, it was later shown to act as a positive allosteric modulator that facilites MRGPRX4 activation by nile acids (PubMed:31500698). {ECO:0000269|PubMed:30657454, ECO:0000269|PubMed:31500698}. reclassified-function Q14197 MRPL58 Homo sapiens (Human) 9606 Large ribosomal subunit protein mL62 (39S ribosomal protein L58, mitochondrial) (MRP-L58) (Digestion substraction 1) (DS-1) (Immature colon carcinoma transcript 1 protein) (Peptidyl-tRNA hydrolase ICT1, mitochondrial) (EC 3.1.1.29) Was initially thought to promote the termination of non-canonical termination stop codons AGG and AGA (PubMed:24352605). However, it was later shown that termination of non-canonical termination stop codons is mediated by MTRF1 (PubMed:37141370). {ECO:0000269|PubMed:37141370, ECO:0000305|PubMed:24352605}.; reclassified-function P08118 MSMB Homo sapiens (Human) 9606 Beta-microseminoprotein (Immunoglobulin-binding factor) (IGBF) (PN44) (Prostate secreted seminal plasma protein) (Prostate secretory protein of 94 amino acids) (PSP-94) (PSP94) (Seminal plasma beta-inhibin) Was originally thought to inhibit the secretion of FSH by pituitary cells. {ECO:0000305}. reclassified-function Q86UE4 MTDH Homo sapiens (Human) 9606 Protein LYRIC (3D3/LYRIC) (Astrocyte elevated gene-1 protein) (AEG-1) (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein) Was originally thought to be a type II membrane protein but this is inconsistent with the results of multiple phosphorylation studies because this topology would locate the phosphorylation sites in the lumen or extracellularly rather than in the cytoplasm. {ECO:0000305|PubMed:15093543}. reclassified-function Q6UB35 MTHFD1L Homo sapiens (Human) 9606 Monofunctional C1-tetrahydrofolate synthase, mitochondrial (EC 6.3.4.3) (Formyltetrahydrofolate synthetase) Was originally thought to be a trifunctional enzyme but only a formyltetrahydrofolate synthetase activity was detected and not a dehydrogenase/cyclohydrogenase activity. {ECO:0000305|PubMed:12937168}. reclassified-function O75570 MTRF1 Homo sapiens (Human) 9606 Peptide chain release factor 1, mitochondrial (MRF-1) (MtRF-1) Was initially thought to not act as a peptide chain release factor because of a sequence insertion in the stop codon-recognition domain that would prevent interactions with the mRNA (PubMed:22569235). However, it was later shown to specifically direct the termination of translation in response to non-canonical termination stop codons AGG and AGA (PubMed:36302763, PubMed:36596788, PubMed:37141370). {ECO:0000269|PubMed:36302763, ECO:0000269|PubMed:36596788, ECO:0000269|PubMed:37141370, ECO:0000305|PubMed:22569235}. reclassified-function Q9UGC7 MTRF1L Homo sapiens (Human) 9606 Peptide chain release factor 1-like, mitochondrial (Mitochondrial translational release factor 1-like) (mtRF1a) Was initially thought to promote the termination of non-canonical termination stop codons AGG and AGA in addition to canonical termination codons UAA and UAG (PubMed:20075246). However, it was later shown that termination of non-canonical termination stop codons AGG and AGA is mediated by MTRF1 (PubMed:37141370). {ECO:0000269|PubMed:20075246, ECO:0000269|PubMed:37141370}. reclassified-function P53602 MVD Homo sapiens (Human) 9606 Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Mevalonate (diphospho)decarboxylase) (MDDase) (Mevalonate pyrophosphate decarboxylase) Was originally thought to be located in the peroxisome (PubMed:11108725). However, was later shown to be cytosolic (PubMed:14972328). {ECO:0000269|PubMed:11108725, ECO:0000269|PubMed:14972328}. reclassified-function Q9UQQ1 NAALADL1 Homo sapiens (Human) 9606 Aminopeptidase NAALADL1 (EC 3.4.11.-) (100 kDa ileum brush border membrane protein) (I100) (Ileal dipeptidylpeptidase) (N-acetylated-alpha-linked acidic dipeptidase-like protein) (NAALADase L) Was originally shown to have aminopeptidase IV activity (PubMed:10085079). Later characterization was unable to detect any significant aminopeptidase IV activity (PubMed:25752612). {ECO:0000269|PubMed:10085079, ECO:0000269|PubMed:25752612}. reclassified-function A0A0U1RRE5 NBDY Homo sapiens (Human) 9606 Negative regulator of P-body association (P-body dissociating protein) (Protein NoBody) Was previously thought to be non-coding but has been shown to be translated and functional. {ECO:0000269|PubMed:27918561}. reclassified-function Q9GZM8 NDEL1 Homo sapiens (Human) 9606 Nuclear distribution protein nudE-like 1 (Protein Nudel) (Mitosin-associated protein 1) Was originally thought to function as an oligopeptidase (NUDEL-oligopeptidase or endooligopeptidase A) which could regulate peptide levels relevant to brain function. {ECO:0000305|PubMed:15728732}. reclassified-function Q8TAT5 NEIL3 Homo sapiens (Human) 9606 Endonuclease 8-like 3 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase FPG2) (DNA glycosylase/AP lyase Neil3) (Endonuclease VIII-like 3) (Nei-like protein 3) Was originally thought to be inactive as a glycosylase (PMID:12200441,PMID:19121397), but recent reports (PMID:22569481, PMID:20185759) demonstrate that cleavage of the initiator methionine is essential for catalytic activity. {ECO:0000305}. reclassified-function P0DMW2 NLRP2B Homo sapiens (Human) 9606 NLR family pyrin domain-containing protein 2B (Pyrin domain-containing protein 2-like protein POP4) (Pyrin-only protein 4) Likely derived from retrogene insertion of an NLRP2/NLRP7-like gene, it was originally considered a pseudogene. However, it turns out to be functional and under purifying selection. {ECO:0000305|PubMed:24871464}. reclassified-function Q9UK39 NOCT Homo sapiens (Human) 9606 Nocturnin (EC 3.1.3.108) (Carbon catabolite repression 4-like protein) Was initially shown to have low deadenylase activity that was lost when the metal-binding Glu was mutated (By similarity). Later studies showed that the purified protein lacked deadenylase activity (PubMed:29860338, PubMed:30389976). Was subsequently shown to act as a phosphatase (PubMed:31147539). {ECO:0000250|UniProtKB:O35710, ECO:0000269|PubMed:29860338, ECO:0000269|PubMed:30389976, ECO:0000269|PubMed:31147539}. reclassified-function Q6P988 NOTUM Homo sapiens (Human) 9606 Palmitoleoyl-protein carboxylesterase NOTUM (EC 3.1.1.98) (hNOTUM) The molecular function of NOTUM has remained unclear for many years. It was initially thought to hydrolyze glycosaminoglycan (GAG) chains of glypicans, thereby affecting glypicans ability to interact with Wnt ligands. It was later reported to trigger glypican shedding, by mediating cleavage of their GPI-anchor. However, while NOTUM specifically inhibit the Wnt signaling pathway, more pleiotropic effects would be expected from an enzyme affecting glypicans. It was finally shown that it requires glypicans to suppress Wnt signaling, but does not cleave their GPI-anchor. It acts by mediating depalmitoleoylation of WNT proteins, impairing WNT binding to frizzled receptors (PubMed:25731175). {ECO:0000269|PubMed:25731175}. reclassified-function P36639 NUDT1 Homo sapiens (Human) 9606 Oxidized purine nucleoside triphosphate hydrolase (EC 3.6.1.56) (2-hydroxy-dATP diphosphatase) (7,8-dihydro-8-oxoguanine triphosphatase) (8-oxo-dGTPase) (Methylated purine nucleoside triphosphate hydrolase) (EC 3.6.1.-) (Nucleoside diphosphate-linked moiety X motif 1) (Nudix motif 1) The role in cancer cell survival is under debate. Was originally considered to play a role as a sanitizing enzyme for oxidized nucleotide pools, and thus important for the survival of cancer cells (PubMed:24695224, PubMed:24695225). A later study indicates that NUDT1 plays a redundant role in eliminating oxidized nucleotides and that it is not essential for cancer cell proliferation and survival (PubMed:28679043). {ECO:0000269|PubMed:24695224, ECO:0000269|PubMed:24695225, ECO:0000269|PubMed:28679043}. reclassified-function P53370 NUDT6 Homo sapiens (Human) 9606 Nudix hydrolase 6 (Antisense basic fibroblast growth factor) (FAD diphosphatase NUDT6) (EC 3.6.1.18) (NADH pyrophosphatase NUDT6) (EC 3.6.1.22) (Nucleoside diphosphate-linked moiety X motif 6) (Nudix motif 6) (Protein GFG) The rat protein was reported to play a role in DNA repair, based on its ability to complement E.coli deficient in the DNA repair enzyme mutT that hydrolyzes oxidized guanine nucleotides (By similarity). PubMed:17569023 found no such activity, neither for the human nor the rat protein. {ECO:0000250|UniProtKB:P70563, ECO:0000305}. reclassified-function P00973 OAS1 Homo sapiens (Human) 9606 2'-5'-oligoadenylate synthase 1 ((2-5')oligo(A) synthase 1) (2-5A synthase 1) (EC 2.7.7.84) (E18/E16) (p46/p42 OAS) PubMed:1651324 sequence was originally thought to originate from mouse. {ECO:0000305}. reclassified-function Q8TAD7 OCC1 Homo sapiens (Human) 9606 Overexpressed in colon carcinoma 1 protein (OCC-1) (AGD3) Was reported to be transcribed but not translated (PubMed:11890990). However, it was later shown that it is expressed at protein level (PubMed:19531736). {ECO:0000305|PubMed:11890990, ECO:0000305|PubMed:19531736}. reclassified-function Q96E52 OMA1 Homo sapiens (Human) 9606 Metalloendopeptidase OMA1, mitochondrial (EC 3.4.24.-) (Metalloprotease-related protein 1) (MPRP-1) (Overlapping with the m-AAA protease 1 homolog) Was initially reported to localize in the endoplasmic reticulum (PubMed:12886954). However, it was later shown that it localizes to mitochondrion (PubMed:20038677). {ECO:0000305|PubMed:12886954, ECO:0000305|PubMed:20038677}. reclassified-function Q96P68 OXGR1 Homo sapiens (Human) 9606 2-oxoglutarate receptor 1 (Alpha-ketoglutarate receptor 1) (G protein-coupled receptor 80) (G protein-coupled receptor 99) (P2Y purinoceptor 15) (P2Y15) (P2Y-like GPCR) (P2Y-like nucleotide receptor) Was originally (Ref.5) thought to be a P2Y receptor. {ECO:0000305}. reclassified-function Q92791 P3H4 Homo sapiens (Human) 9606 Endoplasmic reticulum protein SC65 (Leprecan-like protein 4) (Nucleolar autoantigen No55) (Prolyl 3-hydroxylase family member 4) (Synaptonemal complex protein SC65) Was originally identified in the nucleolus (PubMed:8862517). A recent publication found it only in the endoplasmic reticulum, which agrees with its biological function and the predicted signal sequence (PubMed:23959653). {ECO:0000269|PubMed:23959653, ECO:0000269|PubMed:8862517}. reclassified-function Q9UKK3 PARP4 Homo sapiens (Human) 9606 Protein mono-ADP-ribosyltransferase PARP4 (EC 2.4.2.-) (193 kDa vault protein) (ADP-ribosyltransferase diphtheria toxin-like 4) (ARTD4) (PARP-related/IalphaI-related H5/proline-rich) (PH5P) (Poly [ADP-ribose] polymerase 4) (PARP-4) (Vault poly(ADP-ribose) polymerase) (VPARP) Was initially thought to mediate to mediate poly-ADP-ribosylation of proteins (PubMed:10477748). However, it was later shown to act as a mono-ADP-ribosyltransferase (PubMed:25043379). {ECO:0000269|PubMed:10477748, ECO:0000269|PubMed:25043379}. reclassified-function Q9UHG3 PCYOX1 Homo sapiens (Human) 9606 Prenylcysteine oxidase 1 (EC 1.8.3.5) (Prenylcysteine lyase) Was originally thought to be a lyase and was therefore termed prenylcysteine lyase. {ECO:0000305|PubMed:10585463}. reclassified-function Q5VU43 PDE4DIP Homo sapiens (Human) 9606 Myomegalin (Cardiomyopathy-associated protein 2) (Phosphodiesterase 4D-interacting protein) Was initially reported to localize in the cytoplasm and nucleus (PubMed:11374908). However, many reports in different species have shown that it is associated with the Golgi apparatus and the centrosome. {ECO:0000269|PubMed:11374908, ECO:0000269|PubMed:27666745}. reclassified-function O76074 PDE5A Homo sapiens (Human) 9606 cGMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.35) (cGMP-binding cGMP-specific phosphodiesterase) (CGB-PDE) Was initially thought to act as a major regulator of cardiac hypertrophy in myocytes and muscle and investigations have been made on selective PDE5A inhibitors that could protect against cardiovascular disease. However, while PDE5A regulates nitric-oxide-generated cGMP, nitric oxide signaling is often depressed by heart disease, limiting its effect. Moreover, clinical trial using PDE5A inhibitors were disappointing. {ECO:0000269|PubMed:25799991}. reclassified-function P30101 PDIA3 Homo sapiens (Human) 9606 Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60) Was originally thought to be a phosphatidylinositol 4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha). {ECO:0000305}. reclassified-function P13667 PDIA4 Homo sapiens (Human) 9606 Protein disulfide-isomerase A4 (EC 5.3.4.1) (Endoplasmic reticulum resident protein 70) (ER protein 70) (ERp70) (Endoplasmic reticulum resident protein 72) (ER protein 72) (ERp-72) (ERp72) Was originally thought to be a deoxycytidine kinase. {ECO:0000305|PubMed:2549034}. reclassified-function Q8NEN9 PDZD8 Homo sapiens (Human) 9606 PDZ domain-containing protein 8 (Lysosomal vacuolator) (LYVAC) (Sarcoma antigen NY-SAR-84/NY-SAR-104) (Microbial infection) Was initially reported to enhance infectivity of retroviruses, such as HIV-1, by stabilizing the capsid of retroviruses (PubMed:20573829, PubMed:24554657). However, it was later shown that PDZD8 is not absolutely required for HIV-1 infection, suggesting that its role in retroviral infection is probably indirect (PubMed:25771112). {ECO:0000269|PubMed:20573829, ECO:0000269|PubMed:24554657, ECO:0000269|PubMed:25771112}. reclassified-function Q9BSU1 PHAF1 Homo sapiens (Human) 9606 Phagosome assembly factor 1 Was originally (Ref.1) thought to be a lin-10 homolog. {ECO:0000305}. reclassified-function P48426 PIP4K2A Homo sapiens (Human) 9606 Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha) (Diphosphoinositide kinase 2-alpha) (PIP5KIII) (Phosphatidylinositol 5-Phosphate 4-Kinase) (PI5P4Kalpha) (Phosphatidylinositol 5-phosphate 4-kinase type II alpha) (PI(5)P 4-kinase type II alpha) (PIP4KII-alpha) (PtdIns(4)P-5-kinase B isoform) (PtdIns(4)P-5-kinase C isoform) (PtdIns(5)P-4-kinase isoform 2-alpha) This protein was previously thought to be a phosphatidylinositol 4-phosphate 5-kinase. {ECO:0000305}. reclassified-function Q15126 PMVK Homo sapiens (Human) 9606 Phosphomevalonate kinase (PMKase) (hPMK) (EC 2.7.4.2) Was originally thought to be located in the peroxisome (PubMed:10191291). However, was later shown to be cytosolic (PubMed:14729858, PubMed:27052676). {ECO:0000269|PubMed:14729858, ECO:0000269|PubMed:27052676, ECO:0000305|PubMed:10191291}. reclassified-function P54315 PNLIPRP1 Homo sapiens (Human) 9606 Inactive pancreatic lipase-related protein 1 (PL-RP1) Was originally thought to be the pancreatic lipase, but has been shown to have very low or undetectable lipase activity in vitro. {ECO:0000305|PubMed:19824014}. reclassified-function Q9H237 PORCN Homo sapiens (Human) 9606 Protein-serine O-palmitoleoyltransferase porcupine (EC 2.3.1.250) (Protein MG61) Was initially thought to mediate palmitoylation of Wnt proteins (PubMed:24292069). It was later shown that instead it acts as a serine O-palmitoleoyltransferase that mediates the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1), to Wnt proteins. {ECO:0000269|PubMed:24292069}. reclassified-function Q6P2P2 PRMT9 Homo sapiens (Human) 9606 Protein arginine N-methyltransferase 9 (Protein arginine N-methyltransferase 10) (EC 2.1.1.320) This protein should not be confused with FBXO11 (AC Q86XK2) that was initially erroneously named PRMT9. {ECO:0000305}. reclassified-function Q8NCQ7 PROCA1 Homo sapiens (Human) 9606 Protein PROCA1 (Protein interacting with cyclin A1) Was originally thought to interact with CCNA1 and found in a complex with CCNA1 and CDK2 (PubMed:15159402). However the amino acid sequence described in this paper contains several frameshifts and a wrong choice of frame, so results from this paper need to be validated. {ECO:0000305|PubMed:15159402}. reclassified-function O75832 PSMD10 Homo sapiens (Human) 9606 26S proteasome non-ATPase regulatory subunit 10 (26S proteasome regulatory subunit p28) (Gankyrin) (p28(GANK)) Was initially identified as a genuine component of the 26S proteasome. {ECO:0000305}. reclassified-function Q16401 PSMD5 Homo sapiens (Human) 9606 26S proteasome non-ATPase regulatory subunit 5 (26S protease subunit S5 basic) (26S proteasome subunit S5B) Was initially identified as a genuine component of the 26S proteasome. {ECO:0000305}. reclassified-function O00233 PSMD9 Homo sapiens (Human) 9606 26S proteasome non-ATPase regulatory subunit 9 (26S proteasome regulatory subunit p27) Was initially identified as a component of the 26S proteasome. {ECO:0000305}. reclassified-function P35408 PTGER4 Homo sapiens (Human) 9606 Prostaglandin E2 receptor EP4 subtype (PGE receptor EP4 subtype) (PGE2 receptor EP4 subtype) (Prostanoid EP4 receptor) Was originally designated as the EP2 subtype. {ECO:0000305}. reclassified-function Q8WUK0 PTPMT1 Homo sapiens (Human) 9606 Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (EC 3.1.3.27) (PTEN-like phosphatase) (Phosphoinositide lipid phosphatase) (Protein-tyrosine phosphatase mitochondrial 1) (EC 3.1.3.16, EC 3.1.3.48) Was originally erroneously termed DUSP23. {ECO:0000305}. reclassified-function Q16769 QPCT Homo sapiens (Human) 9606 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (sQC) (Glutaminyl-tRNA cyclotransferase) (Glutamyl cyclase) (EC) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (PubMed:18072935, PubMed:21288892). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000269|PubMed:18072935, ECO:0000269|PubMed:21288892, ECO:0000305}. reclassified-function Q9NXS2 QPCTL Homo sapiens (Human) 9606 Glutaminyl-peptide cyclotransferase-like protein (EC 2.3.2.5) (Golgi-resident glutaminyl-peptide cyclotransferase) (isoQC) (gQC) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (PubMed:21288892). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000269|PubMed:21288892}. reclassified-function O75154 RAB11FIP3 Homo sapiens (Human) 9606 Rab11 family-interacting protein 3 (FIP3) (FIP3-Rab11) (Rab11-FIP3) (Arfophilin-1) (EF hands-containing Rab-interacting protein) (Eferin) (MU-MB-17.148) Was initially shown not to interact with ARF5 (PubMed:16148947). Another study later demonstrated the interaction (PubMed:17030804). {ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:17030804}. reclassified-function O60671 RAD1 Homo sapiens (Human) 9606 Cell cycle checkpoint protein RAD1 (hRAD1) (Rad1-like DNA damage checkpoint protein) [Isoform 1]: Was reported to possess 3'->5' double stranded DNA exonuclease activity (PubMed:9660799). However, this activity was not confirmed by other publications (PubMed:9716408). {ECO:0000269|PubMed:9660799, ECO:0000269|PubMed:9716408}. reclassified-function Q9P258 RCC2 Homo sapiens (Human) 9606 Protein RCC2 (RCC1-like protein TD-60) (Telophase disk protein of 60 kDa) Its precise role in the regulation of RAC1 activity is under debate. Was originally proposed to function as a guanine nucleotide exchange factor for RAC1, but later publications indicate it attenuates RAC1 activation by guanine nucleotide exchange factors and prevents accumulation of active, GTP-bound RAC1 (PubMed:12919680, PubMed:25074804, PubMed:28869598). Conflicting results have also been reported regarding its preferential interaction with nucleotide-free RAC1, as opposed to GPD or GTP-bound RAC1 (PubMed:12919680, PubMed:25074804). {ECO:0000269|PubMed:12919680, ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:28869598}. reclassified-function Q8NBN7 RDH13 Homo sapiens (Human) 9606 Retinol dehydrogenase 13 (EC 1.1.1.300) (Short chain dehydrogenase/reductase family 7C member 3) Was originally thought to lack retinol dehydrogenase (RDH) activity. However, a more recent publication demonstrates a retinol dehydrogenase activity for RDH13. {ECO:0000269|PubMed:12226107, ECO:0000269|PubMed:18039331}. reclassified-function Q01201 RELB Homo sapiens (Human) 9606 Transcription factor RelB (I-Rel) Was originally thought to inhibit the transcriptional activity of nuclear factor NF-kappa-B. {ECO:0000305|PubMed:1577270}. reclassified-function Q8IX06 REXO1L1P Homo sapiens (Human) 9606 Putative exonuclease GOR (EC 3.1.-.-) (Antigen GOR homolog) (RNA exonuclease 1 homolog-like 1) Could be the product of a pseudogene. N-terminally truncated compared to the protein-coding REXO1 gene. Originally thought to encode human GOR47-1, an antigenic epitope identified from the serum of virus infected chimpanzee (see AC P48778), which was apparently also expressed in human and used in ELISA tests to detect hepatitis C virus infection in patients. It turns out that the peptide identified in chimpanzee cannot be produced by human REXO1L1/GOR gene, due to a premature stop codon in the gene (PubMed:11472404) and therefore the basis of the tests remains unclear. However, the same authors provide evidence of the expression of a different N-terminal peptide from the human REXO1L1/GOR gene, the GOR1-125 antigen (PubMed:11472404). {ECO:0000305|PubMed:11472404}. reclassified-function Q63HN8 RNF213 Homo sapiens (Human) 9606 E3 ubiquitin-protein ligase RNF213 (EC 2.3.2.27) (EC 3.6.4.-) (ALK lymphoma oligomerization partner on chromosome 17) (E3 ubiquitin-lipopolysaccharide ligase RNF213) (EC 2.3.2.-) (Mysterin) (RING finger protein 213) The stoichiometry is unclear: was initially thought to form homohexamers (PubMed:24658080, PubMed:26126547). However, the electron microscopy structure showed that it is monomeric and is composed of six ATPase modules within a single polypeptide chain (By similarity). {ECO:0000250|UniProtKB:E9Q555, ECO:0000269|PubMed:24658080, ECO:0000269|PubMed:26126547}. reclassified-function P42677 RPS27 Homo sapiens (Human) 9606 Small ribosomal subunit protein eS27 (40S ribosomal protein S27) (Metallopan-stimulin 1) (MPS-1) Was originally (PubMed:8407955) thought to be a protein that could have played a role as a potentially important mediator of cellular proliferative responses to various growth factors and other environmental signals. Capable of specific binding to a cAMP response element in DNA. {ECO:0000305|PubMed:8407955}. reclassified-function Q86TU7 SETD3 Homo sapiens (Human) 9606 Actin-histidine N-methyltransferase (EC 2.1.1.85) (Protein-L-histidine N-tele-methyltransferase) (SET domain-containing protein 3) (hSETD3) Was initially reported to have histone methyltransferase activity and methylate 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me) (By similarity). However, this conclusion was based on mass spectrometry data wherin mass shifts were inconsistent with a bona fide methylation event (PubMed:30626964). In vitro, the protein-lysine methyltransferase activity is weak compared to the protein-histidine methyltransferase activity (PubMed:30526847). {ECO:0000250|UniProtKB:Q91WC0, ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964}. reclassified-function P23246 SFPQ Homo sapiens (Human) 9606 Splicing factor, proline- and glutamine-rich (100 kDa DNA-pairing protein) (hPOMp100) (DNA-binding p52/p100 complex, 100 kDa subunit) (Polypyrimidine tract-binding protein-associated-splicing factor) (PSF) (PTB-associated-splicing factor) Was originally thought to be myoblast cell surface antigen 24.1D5 and a possible membrane-bound protein ectokinase. {ECO:0000305|PubMed:2480877}. reclassified-function A6NMB1 SIGLEC16 Homo sapiens (Human) 9606 Sialic acid-binding Ig-like lectin 16 (Siglec-16) (Siglec-P16) According to PubMed:18629938, the SIGLECP16 sequence, that was initially classified as a pseudogene, has a 4 bp deletion when compared with the sequence shown in this entry. This deletion is a polymorphism with a frequency of around 50% in the UK population. The frameshifted allele is non-functional whereas the sequence displayed here seems to be functional. The functional allele has been named SIGLEC16 in PubMed:18629938. {ECO:0000305}. reclassified-function O15427 SLC16A3 Homo sapiens (Human) 9606 Monocarboxylate transporter 4 (MCT 4) (Solute carrier family 16 member 3) Was initially thought to be considered to be a low affinity lactate transporter with negligible affinity for pyruvate (PubMed:11101640). However, it was later shown that SLC16A3 is a high affinity lactate transporter with physiologically relevant affinity for pyruvate (PubMed:31719150). {ECO:0000269|PubMed:11101640, ECO:0000269|PubMed:31719150}.; reclassified-function Q9NSA0 SLC22A11 Homo sapiens (Human) 9606 Solute carrier family 22 member 11 (Organic anion transporter 4) (OAT4) (Organic anion:dicarboxylate exchanger OAT4) Was originally thought to be involved in both the uptake and efflux of glutarate, thereby acting as a bidirectional organic anion:dicarboxylate exchanger (PubMed:15037815). However, another study did not show any significant uptake of glutarate by SLC22A11/OAT4 (PubMed:17229912). Although initial results showed that SLC22A11/OAT4 drove DHEA-S and E1S uptake in a Na(+)-independent manner (PubMed:10660625), further studies demonstrated that both the uptake of DHEA-S and E1S by SLC22A11/OAT4 was partly Na(+)-dependent (about 50%) (PubMed:10660625, PubMed:18501590). The mechanism of SLC22A11/OAT4-mediated transport of E1S is unclear. Most studies have demonstrated a translocation of E1S through the plasma membrane into the cytosol, which would highlight a role of SLC22A11/OAT4 in placental and renal absorption (PubMed:10660625, PubMed:15037815, PubMed:17229912, PubMed:18501590, PubMed:26277985). Instead, SLC22A11/OAT4 was later proposed to mediate both the insertion into and the extraction from the plasma membrane of E1S without being translocated into the cytosol (PubMed:28027879). {ECO:0000269|PubMed:10660625, ECO:0000269|PubMed:15037815, ECO:0000269|PubMed:17229912, ECO:0000269|PubMed:18501590, ECO:0000269|PubMed:26277985, ECO:0000269|PubMed:28027879}. reclassified-function Q9HC21 SLC25A19 Homo sapiens (Human) 9606 Mitochondrial thiamine pyrophosphate carrier (Mitochondrial thiamine pyrophosphate transporter) (MTPPT) (Mitochondrial uncoupling protein 1) (Solute carrier family 25 member 19) Previously identified as the mitochondrial deoxyribonucleotide carrier (PubMed:11226231). However other experiments later demonstrated that SLC25A19 is a thiamine diphosphate transporter and not a mitochondrial deoxyribonucleotide carrier (PubMed:15539640, PubMed:18280798). {ECO:0000269|PubMed:11226231, ECO:0000269|PubMed:15539640, ECO:0000269|PubMed:18280798}. reclassified-function Q8N8R3 SLC25A29 Homo sapiens (Human) 9606 Mitochondrial basic amino acids transporter (Carnitine/acylcarnitine translocase-like) (CACT-like) (Mitochondrial carnitine/acylcarnitine carrier protein CACL) (Mitochondrial ornithine transporter 3) (Solute carrier family 25 member 29) Was initially proposed to transport palmitoylcarnitine, based on complementation experiments in yeast mutants lacking CRC1 and CIT2 and release of radiolabeled carnitine from mitochondria incubated with radiolabeled palmitoylcarnithine (By similarity). Later experiments done primarily with human indicate the protein functions instead as transporter of basic amino acids (PubMed:24652292). {ECO:0000250|UniProtKB:Q08DK7, ECO:0000269|PubMed:24652292}. reclassified-function Q9UGQ3 SLC2A6 Homo sapiens (Human) 9606 Solute carrier family 2, facilitated glucose transporter member 6 (Glucose transporter type 6) (GLUT-6) Was initially thought to act as a glucose transporter (PubMed:10970791). However, later studies demonstrated that it does not transport glucose (PubMed:30431159). {ECO:0000269|PubMed:10970791, ECO:0000269|PubMed:30431159}.; reclassified-function Q969S0 SLC35B4 Homo sapiens (Human) 9606 Nucleotide sugar transporter SLC35B4 (Solute carrier family 35 member B4) (UDP-xylose and UDP-N-acetylglucosamine transporter) (YEA4 homolog) It was initially reported to localize to the Golgi apparatus, but this was later found to be artifactual mislocalization due to C-terminal tagging interfering with the ER retention signal. {ECO:0000269|PubMed:15911612, ECO:0000269|PubMed:30458018}. reclassified-function Q9NQQ7 SLC35H1 Homo sapiens (Human) 9606 Solute carrier family 35 member H1 (Ovarian cancer-overexpressed gene 1 protein) (Solute carrier family 35 member C2) SLC35H1, a homolog of the GDP-fucose transporter SLC35C1, was initially predicted to mediate GDP-fucose transport. A study indicates that SLC35H1 promotes Notch1 fucosylation and is essential for optimal Notch signaling in cultured mammalian cells (PubMed:20837470). However, Slc35h1 knockout mice are viable and fertile, showing no signs of impaired Notch signaling during skeletal or T cell development (By similarity). Additionally, deleting SLC35H1 in HEK293T cells does not affect Golgi or ER O-fucosylation, arguing against a primary role for SLC35H1 as a GDP-fucose transporter (PubMed:38270391). {ECO:0000250|UniProtKB:Q8VCX2, ECO:0000269|PubMed:20837470, ECO:0000269|PubMed:38270391}. reclassified-function Q9NP94 SLC39A2 Homo sapiens (Human) 9606 Zinc transporter ZIP2 (6A1) (Eti-1) (Solute carrier family 39 member 2) (Zrt- and Irt-like protein 2) (ZIP-2) (hZIP2) It was previously proposed that SLC39A2 operates as a Zn2(+)/HCO3(-) symport mechanism (PubMed:10681536). However in more recent studies, SLC39A2-mediated transport is independent of both HCO3(-) and H(+)-driving forces, but modulated by extracellular pH and voltage (PubMed:29791142, PubMed:30914478). {ECO:0000269|PubMed:10681536, ECO:0000269|PubMed:29791142, ECO:0000269|PubMed:30914478}. reclassified-function Q5BKX6 SLC45A4 Homo sapiens (Human) 9606 Polyamine-transporter SLC45A4 (Solute carrier family 45 member 4) Was initially characterized as a proton-associated sucrose transporter in vitro (By similarity). However, the sucrose transporter activity could not be confirmed by a subsequent article, which showed that it acts as a polyamine-transporter (PubMed:40836097). {ECO:0000250|UniProtKB:Q0P5V9, ECO:0000269|PubMed:40836097}. reclassified-function Q96BI1 SLC67A1 Homo sapiens (Human) 9606 Solute carrier family 67 member A1 (Beckwith-Wiedemann syndrome chromosomal region 1 candidate gene A protein) (Efflux transporter-like protein) (Imprinted multi-membrane-spanning polyspecific transporter-related protein 1) (Organic cation transporter-like protein 2) (ORCTL-2) (Solute carrier family 22 member 1-like) (Solute carrier family 22 member 18) (Tumor-suppressing STF cDNA 5 protein) (Tumor-suppressing subchromosomal transferable fragment candidate gene 5 protein) (p45-Beckwith-Wiedemann region 1 A) (p45-BWR1A) Was initially classified as a member of the SLC22 family. However, an evolutionary and phylogenetic analysis suggested that SLC22A18 is unique and that it is most distantly related to SLC22 family members. {ECO:0000269|PubMed:26536134}.; reclassified-function Q92581 SLC9A6 Homo sapiens (Human) 9606 Sodium/hydrogen exchanger 6 (Na(+)/H(+) exchanger 6) (NHE-6) (Solute carrier family 9 member 6) Was originally (PubMed:9507001) identified as a mitochondrial inner membrane protein, but was later shown to be localized in early and recycling endosomes and not mitochondria (PubMed:11641397, PubMed:11940519). {ECO:0000269|PubMed:11641397, ECO:0000305|PubMed:11940519, ECO:0000305|PubMed:9507001}. reclassified-function Q9UQE7 SMC3 Homo sapiens (Human) 9606 Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) (Basement membrane-associated chondroitin proteoglycan) (Bamacan) (Chondroitin sulfate proteoglycan 6) (Chromosome-associated polypeptide) (hCAP) Was originally isolated as a proteoglycan protein (explaining its name). Although not excluded, such secreted function is not clear. {ECO:0000305}. reclassified-function P49901 SMCP Homo sapiens (Human) 9606 Sperm mitochondrial-associated cysteine-rich protein Was originally thought to be a selenoprotein and was known as sperm mitochondrial capsule selenoprotein. {ECO:0000305|PubMed:8833144}. reclassified-function Q4W5P6 SMIM43 Homo sapiens (Human) 9606 Small integral membrane protein 43 (Nodal enhanced mesendoderm micropeptide) (NEMEP) This was previously named TMEM55 and corresponded to a 130-residue protein. However, recent evidence suggests that the wrong ORF was originally chosen for this protein and supports an upstream ORF coding for a 63-residue protein. {ECO:0000305}. reclassified-function P35713 SOX18 Homo sapiens (Human) 9606 Transcription factor SOX-18 Was originally termed SOX-8. {ECO:0000305|PubMed:1614875}. reclassified-function P41225 SOX3 Homo sapiens (Human) 9606 Transcription factor SOX-3 Was originally termed SOX-9. {ECO:0000305|PubMed:1614875}. reclassified-function W5XKT8 SPACA6 Homo sapiens (Human) 9606 Sperm acrosome membrane-associated protein 6 (BACHELOR-like protein) Was originally thought to be a non protein-coding gene. reclassified-function Q9UQ90 SPG7 Homo sapiens (Human) 9606 Mitochondrial inner membrane m-AAA protease component paraplegin (EC 3.4.24.-) (EC 3.6.-.-) (Cell matrix adhesion regulator) (Paraplegin) (Spastic paraplegia 7 protein) A CDS in the 3'-UTR of SPG7 mRNA had been erroneously identified as a cell matrix adhesion regulator and originally thought to be encoded by the CMAR gene. There is no experimental evidence for the production of endogenous CMAR protein. {ECO:0000305}. reclassified-function Q9BUA3 SPINDOC Homo sapiens (Human) 9606 Spindlin interactor and repressor of chromatin-binding protein (SPIN1-docking protein) (SPIN-DOC) Was initially reported to inhibit the ability of SPIN1 to bind methylated histones (PubMed:29061846). However, it was later shown to play an opposite role and promote SPIN1 association with bivalent H3K4me3K9me3 mark (PubMed:33574238). {ECO:0000269|PubMed:29061846, ECO:0000269|PubMed:33574238}. reclassified-function Q9H8P0 SRD5A3 Homo sapiens (Human) 9606 Polyprenal reductase (EC 1.3.1.94) (3-oxo-5-alpha-steroid 4-dehydrogenase 3) (EC 1.3.1.22) (Steroid 5-alpha-reductase 2-like) (Steroid 5-alpha-reductase 3) (S5AR 3) (SR type 3) Was initially characterized as a polyprenol reductase, mediating the conversion of polyprenol into dolichol (PubMed:20637498). However, it was later shown to catalyze an intermediate step in this pathway and reduce polyprenal (PubMed:38821050). {ECO:0000269|PubMed:20637498, ECO:0000269|PubMed:38821050}. reclassified-function Q14849 STARD3 Homo sapiens (Human) 9606 StAR-related lipid transfer protein 3 (Metastatic lymph node gene 64 protein) (MLN 64) (Protein CAB1) (START domain-containing protein 3) (StARD3) STARD3 was reported to function in cholesterol transport to the mitochondria or to the cell membrane (PubMed:12070139, PubMed:19965586). Other reports however showed that it mediates cholesterol transport from the endoplasmic reticulum to endosomes (PubMed:11053434, PubMed:28377464). Discrepancies may be due to the different cell type used and the cellular physiological state (PubMed:28377464). {ECO:0000269|PubMed:11053434, ECO:0000269|PubMed:12070139, ECO:0000269|PubMed:19965586, ECO:0000269|PubMed:28377464}. reclassified-function Q9BYT3 STK33 Homo sapiens (Human) 9606 Serine/threonine-protein kinase 33 (EC 2.7.11.1) Was initially thought to be required for the survival of mutant KRAS-dependent cell lines (PubMed:19490892). However, it was later shown that it is not essential for the survival of KRAS-dependent AML cell lines (PubMed:21742770). {ECO:0000269|PubMed:19490892, ECO:0000269|PubMed:21742770}. reclassified-function Q13033 STRN3 Homo sapiens (Human) 9606 Striatin-3 (Cell cycle autoantigen SG2NA) (S/G2 antigen) Was originally thought to be nuclear. {ECO:0000305|PubMed:7864889}. reclassified-function Q7L7X3 TAOK1 Homo sapiens (Human) 9606 Serine/threonine-protein kinase TAO1 (EC 2.7.11.1) (Kinase from chicken homolog B) (hKFC-B) (MARK Kinase) (MARKK) (Prostate-derived sterile 20-like kinase 2) (PSK-2) (PSK2) (Prostate-derived STE20-like kinase 2) (Thousand and one amino acid protein kinase 1) (TAOK1) (hTAOK1) Was initially thought to play a role in the spindle checkpoint (PubMed:17417629). However, it was later shown that it is not the case and that phenotypes initially observed are the cause of the siRNA used that has an off-target effect resulting in MAD2L1 inhibition (PubMed:19904549, PubMed:20162290). {ECO:0000305|PubMed:17417629}. reclassified-function Q9P0N9 TBC1D7 Homo sapiens (Human) 9606 TBC1 domain family member 7 (Cell migration-inducing protein 23) Was initially identified as a negative regulator of the TSC-TBC complex (PubMed:17658474). However, it was later shown that TBC1D7 is part of the TSC-TBC complex and participates in GTPase-activating protein activity, leading to inhibition of the TOR signaling cascade (PubMed:22795129). The differences between 2 reports might be explained by experimental conditions in the initial report, in which they overexpressed the TBC1D7 subunit, possibly leading to disrupt the stoichiometric complex and its downstream functions. {ECO:0000305|PubMed:17658474, ECO:0000305|PubMed:22795129}. reclassified-function Q5XG87 TENT4A Homo sapiens (Human) 9606 Terminal nucleotidyltransferase 4A (DNA polymerase sigma) (LAK-1) (Non-canonical poly(A) RNA polymerase PAPD7) (EC 2.7.7.19) (PAP-associated domain-containing protein 7) (TRAMP-like complex polyadenylate polymerase) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal uridylyltransferase 5) (TUTase 5) (Topoisomerase-related function protein 4-1) (TRF4-1) Was originally thought to have DNA polymerase activity. {ECO:0000305}. reclassified-function Q8NDF8 TENT4B Homo sapiens (Human) 9606 Terminal nucleotidyltransferase 4B (Non-canonical poly(A) RNA polymerase PAPD5) (EC 2.7.7.19) (PAP-associated domain-containing protein 5) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal uridylyltransferase 3) (TUTase 3) (Topoisomerase-related function protein 4-2) (TRF4-2) Was originally thought to have DNA polymerase activity. {ECO:0000305}. reclassified-function Q9NYB0 TERF2IP Homo sapiens (Human) 9606 Telomeric repeat-binding factor 2-interacting protein 1 (TERF2-interacting telomeric protein 1) (TRF2-interacting telomeric protein 1) (Dopamine receptor-interacting protein 5) (Repressor/activator protein 1 homolog) (RAP1 homolog) (hRap1) Was reported to participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair in the absence of TERF2 (PubMed:19763083). However, this probably does not corresponds to its primary function and experiments in mouse showed that it is dispensible for such process and is required for repression of homology-directed repair (HDR). {ECO:0000305|PubMed:19763083}. reclassified-function O95455 TGDS Homo sapiens (Human) 9606 UDP-D-glucose 4,6-dehydratase (EC 4.2.1.76) (dTDP-D-glucose 4,6-dehydratase) Was initially thought to have dTDP-D-glucose 4,6-dehydratase activity, based on its similarity with bacterial enzymes involved in the synthesis of rhamnose during bacterial cell wall formation. However, it was later shown to have UTP-glucose 4,6-dehydratase activity (PubMed:40836090). {ECO:0000269|PubMed:40836090, ECO:0000305}. reclassified-function Q96CG3 TIFA Homo sapiens (Human) 9606 TRAF-interacting protein with FHA domain-containing protein A (Putative MAPK-activating protein PM14) (Putative NF-kappa-B-activating protein 20) (TRAF2-binding protein) D-glycero-beta-D-manno-heptose 1,7-bisphosphate (HBP) was initially thought to constitute the bacterial pathogen-associated molecular pattern metabolite (PAMP) triggering the ALPK1-TIFA innate immunune response (PubMed:26068852, PubMed:28222186, PubMed:28877472). It was however shown that ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose) constitutes the main PAMP that activates the kinase activity of ALPK1, promoting phosphorylation of TIFA (PubMed:30111836). {ECO:0000269|PubMed:26068852, ECO:0000269|PubMed:28222186, ECO:0000269|PubMed:28877472, ECO:0000269|PubMed:30111836}. reclassified-function Q96CP7 TLCD1 Homo sapiens (Human) 9606 TLC domain-containing protein 1 (Calfacilitin) Was originally proposed to be a calcium channel facilitator (By similarity). However, a more recent study shows that this protein regulates membrane phospholipid homeostasis (PubMed:30509349). Therefore, any effects on calcium flux are most likely a secondary consequence of defects in membrane composition or fluidity (PubMed:30509349). {ECO:0000250|UniProtKB:F1NZP5, ECO:0000269|PubMed:30509349}. reclassified-function Q9BX74 TM2D1 Homo sapiens (Human) 9606 TM2 domain-containing protein 1 (Amyloid-beta-binding protein) (hBBP) Was originally (PubMed:11278849) thought to modulate amyloid-beta toxicity by coupling to G protein. However, PubMed:12836168 showed that this effect is not direct. {ECO:0000305|PubMed:11278849}. reclassified-function Q9BSA9 TMEM175 Homo sapiens (Human) 9606 Endosomal/lysosomal proton channel TMEM175 (Potassium channel TMEM175) (Transmembrane protein 175) (hTMEM175) A publication claims that potassium transport was initially measured with a luminal side pH above 7.0, which is non-physiological for lysosomal channels (PubMed:35750034). This statement is however incorrect as potassium transport was tested at lumenal pH of 5.5, which is considered physiological (PubMed:26317472). {ECO:0000269|PubMed:26317472, ECO:0000269|PubMed:35750034}. reclassified-function Q5BJF2 TMEM97 Homo sapiens (Human) 9606 Sigma intracellular receptor 2 (S2R) (Sigma-2 receptor) (Sigma2 receptor) (Meningioma-associated protein 30) (MAC30) (Transmembrane protein 97) The molecular identity of the sigma-2 receptor has been unclear for a long time. It is now identified as TMEM97 (PubMed:28559337). Previously identified as PGRMC1 (AC O00264) (PubMed:22292588, PubMed:28007569). {ECO:0000269|PubMed:28007569, ECO:0000269|PubMed:28559337, ECO:0000303|PubMed:22292588}. reclassified-function Q96HA7 TONSL Homo sapiens (Human) 9606 Tonsoku-like protein (Inhibitor of kappa B-related protein) (I-kappa-B-related protein) (IkappaBR) (NF-kappa-B inhibitor-like protein 2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 2) Was reported to share sequence similarities with IKBKB and therefore named 'NF-kappa-B inhibitor-like protein 2' (PubMed:7738005). However, the sequence similarity is remote and effects as regulator of NF-kappa-B are probably indirect and require additional evidence (PubMed:9242696). {ECO:0000305|PubMed:7738005, ECO:0000305|PubMed:9242696}. reclassified-function Q92547 TOPBP1 Homo sapiens (Human) 9606 DNA topoisomerase 2-binding protein 1 (DNA topoisomerase II-beta-binding protein 1) (TopBP1) (DNA topoisomerase II-binding protein 1) Interaction with phosphorylated MDC1 was initially thought to be mediated by BRCT domains 4 and 5 (PubMed:23891287). However, it was later shown to be mainly mediated by BRCT domains 1 and 2 (PubMed:30898438). {ECO:0000269|PubMed:23891287, ECO:0000269|PubMed:30898438}. reclassified-function Q9NS56 TOPORS Homo sapiens (Human) 9606 E3 ubiquitin-protein ligase Topors (EC 2.3.2.27) (RING-type E3 ubiquitin transferase Topors) (SUMO1-protein E3 ligase Topors) (Topoisomerase I-binding RING finger protein) (Topoisomerase I-binding arginine/serine-rich protein) (Tumor suppressor p53-binding protein 3) (p53-binding protein 3) (p53BP3) Was originally thought to bind to the palindromic consensus sequence 5'-TCCCAGCACTTTGGGA-3' and to regulate the transcription of numerous genes in the lung. {ECO:0000305|PubMed:11278651}. reclassified-function O75648 TRMU Homo sapiens (Human) 9606 Mitochondrial tRNA-specific 2-thiouridylase 1 (EC 2.8.1.14) (MTO2 homolog) Was originally thought to be a 5-methylaminomethyl-2-methyltransferase involved in tRNA modification. {ECO:0000305|PubMed:16513084}. reclassified-function Q6DKK2 TTC19 Homo sapiens (Human) 9606 Tetratricopeptide repeat protein 19, mitochondrial (TPR repeat protein 19) Was reported to be required for the abscission step in cytokinesis, possibly regulating the ESCRT-III complex via its interaction with CHMP4B (PubMed:20208530). According to the same authors, localizes to the centrosome during all stages of the cell cycle and is recruited to the midbody during cytokinesis (PubMed:20208530). However, the midbody localization could not be confirmed by others (PubMed:21278747). {ECO:0000269|PubMed:20208530, ECO:0000269|PubMed:21278747}. reclassified-function Q9Y4R7 TTLL3 Homo sapiens (Human) 9606 Tubulin monoglycylase TTLL3 (EC 6.3.2.-) (HOTTL) (Tubulin--tyrosine ligase-like protein 3) TTLL3 and TTLL8 monoglycylase-mediated glycylation of tubulin was initially reported to play a role in ependymal motile ciliary maintenance (By similarity). However, contradictory results were later observed (By similarity). {ECO:0000250|UniProtKB:A4Q9E5}. reclassified-function A6PVC2 TTLL8 Homo sapiens (Human) 9606 Protein monoglycylase TTLL8 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 8) TTLL3 and TTLL8 monoglycylase-mediated glycylation of tubulin was initially reported to play a role in ependymal motile ciliary maintenance (By similarity). However, contradictory results were later observed (By similarity). {ECO:0000250|UniProtKB:A4Q9F1}. reclassified-function Q12792 TWF1 Homo sapiens (Human) 9606 Twinfilin-1 (Protein A6) (Protein tyrosine kinase 9) Was originally thought to have protein tyrosine kinase activity. {ECO:0000305|PubMed:7507208}. reclassified-function P40222 TXLNA Homo sapiens (Human) 9606 Alpha-taxilin Was originally thought to be a high molecular weight interleukin (IL-14 or IL14). {ECO:0000305|PubMed:8327514}. reclassified-function P55851 UCP2 Homo sapiens (Human) 9606 Dicarboxylate carrier SLC25A8 (Mitochondrial uncoupling protein 2) (UCP 2) (Solute carrier family 25 member 8) (UCPH) The role of UCP2/SLC25A8 in mitochondrial proton conductance is a matter of debate. It was initially suggested that it mediates proton leak that increases net proton conductance in response to ROS such as reactive alkenals generated during fatty acid oxidation in mitochondria. By lowering the proton motive force, it would provide for feedback control of mitochondrial ROS metabolism limiting extensive ROS production and protecting cells against oxidative stress. This activity and its potential regulation by ubiquinones and nucleotides was disputed by later studies, which failed to reproduce the effect on proton conductance under physiological conditions. Rather than 'uncoupling' the link between electron transfer and ATP synthesis, it may couple metabolite transport to proton flux to allow for optimal ATP turnover. {ECO:0000269|PubMed:11171965, ECO:0000269|PubMed:11278935, ECO:0000303|PubMed:33798544}. reclassified-function Q16851 UGP2 Homo sapiens (Human) 9606 UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (UDP-glucose pyrophosphorylase) (UDPGP) (UGPase) The human genome was initially thought to contain 2 genes for UTP--glucose-1-phosphate uridylyltransferase: UGP1 and UGP2 (PubMed:8354390, PubMed:8631325). However, the sequence defined as UGP1 (PubMed:8354390) probably does not exist and corresponds to UGP2. {ECO:0000269|PubMed:8354390, ECO:0000269|PubMed:8631325, ECO:0000305|PubMed:8354390, ECO:0000305|PubMed:8631325}. reclassified-function P06133 UGT2B4 Homo sapiens (Human) 9606 UDP-glucuronosyltransferase 2B4 (UDPGT 2B4) (UGT2B4) (EC 2.4.1.17) (HLUG25) (Hyodeoxycholic acid-specific UDPGT) (UDPGTh-1) UGT2B4 has been previously described as an enzyme named UGT2B11. However the name UGT2B11 has now been reused for another human protein (see AC O75310). {ECO:0000305, ECO:0000305|PubMed:8333863}. reclassified-function Q6UW78 UQCC3 Homo sapiens (Human) 9606 Ubiquinol-cytochrome-c reductase complex assembly factor 3 (Assembly factor CBP4 homolog) Was initially reported to be secreted (PubMed:15340161). However, it was later shown to be localized in the inner mitochondrial membrane (PubMed:25008109, PubMed:25605331). {ECO:0000269|PubMed:25008109, ECO:0000269|PubMed:25605331, ECO:0000303|PubMed:15340161}. reclassified-function P14927 UQCRB Homo sapiens (Human) 9606 Cytochrome b-c1 complex subunit 7 (Complex III subunit 7) (Complex III subunit VII) (QP-C) (Ubiquinol-cytochrome c reductase complex 14 kDa protein) Was originally thought to be the ubiquinone-binding protein (QP-C). {ECO:0000305}. reclassified-function P54578 USP14 Homo sapiens (Human) 9606 Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) (Deubiquitinating enzyme 14) (Ubiquitin thioesterase 14) (Ubiquitin-specific-processing protease 14) Was originally thought to be a guanine tRNA-ribosyltransferase. {ECO:0000305, ECO:0000305|Ref.1}. reclassified-function Q96K76 USP47 Homo sapiens (Human) 9606 Ubiquitin carboxyl-terminal hydrolase 47 (EC 3.4.19.12) (Deubiquitinating enzyme 47) (Ubiquitin thioesterase 47) (Ubiquitin-specific-processing protease 47) Was initially thought to catalytically inactive (PubMed:14715245). However, it was later shown that it is active (PubMed:21362556). {ECO:0000305|PubMed:14715245, ECO:0000305|PubMed:21362556}. reclassified-function Q70EK8 USP53 Homo sapiens (Human) 9606 Ubiquitin carboxyl-terminal hydrolase 53 (EC 3.4.19.12) (Ubiquitin-specific peptidase 53) Was initially reported to have no protein deubiquitinase activity due to the absence of a conserved His residue normally found 9 residues before the catalytic His (PubMed:14715245). However, it was later shown to specifically cleave 'Lys-63'-linked polyubiquitin chains composed of at least 3 ubiquitins (PubMed:39587316). {ECO:0000269|PubMed:14715245, ECO:0000269|PubMed:39587316}. reclassified-function Q9UBQ0 VPS29 Homo sapiens (Human) 9606 Vacuolar protein sorting-associated protein 29 (hVPS29) (PEP11 homolog) (Vesicle protein sorting 29) Was originally believed to be a metal-dependent phosphatase but shown to lack catalytic activity; can bind metals with very low affinity suggesting that metal binding is not required for its function. {ECO:0000303|PubMed:16737443, ECO:0000303|PubMed:21629666}. reclassified-function P49842 WHR1 Homo sapiens (Human) 9606 Winged helix repair factor 1 (Inactive serine/threonine-protein kinase 19) (Protein G11) (Protein RP1) (Tandem winged helix protein formerly known as STK19) Was originally reported to be a serine/threonine-protein kinase that phosphorylates CSN1S1/alpha-casein at serine/threonine residues and histones at serine residues (PubMed:9812991). Was also reported to phosphorylate NRAS at serine residues (PubMed:30712867, PubMed:9812991). However, later studies have shown that the protein does not have kinase activity and is involved in transcription-coupled nucleotide excision repair (PubMed:32531245, PubMed:32531246, PubMed:38252411, PubMed:39547228, PubMed:39547229). {ECO:0000269|PubMed:30712867, ECO:0000269|PubMed:32531245, ECO:0000269|PubMed:32531246, ECO:0000269|PubMed:38252411, ECO:0000269|PubMed:39547228, ECO:0000269|PubMed:39547229, ECO:0000269|PubMed:9812991}.; reclassified-function Q13426 XRCC4 Homo sapiens (Human) 9606 DNA repair protein XRCC4 (hXRCC4) (X-ray repair cross-complementing protein 4) [Cleaved into: Protein XRCC4, C-terminus (XRCC4/C)] Sumoylation at Lys-210 was initially reported to regulate nuclear localization and recombination efficiency of XRCC4 (PubMed:16478998). This result is however not confirmed by another study (PubMed:25934149). {ECO:0000269|PubMed:16478998, ECO:0000269|PubMed:25934149}. reclassified-function Q9BYJ9 YTHDF1 Homo sapiens (Human) 9606 YTH domain-containing family protein 1 (DF1) (Dermatomyositis associated with cancer putative autoantigen 1) (DACA-1) Was initially reported to act as a regulator of mRNA translation efficiency by promoting ribosome loading to m6A-containing mRNAs and by interacting with translation initiation factors eIF3 (EIF3A or EIF3B), thereby facilitating translation initiation (PubMed:26046440, PubMed:26593424). These studies suggested that the 3 different paralogs (YTHDF1, YTHDF2 and YTHDF3) have unique functions with limited redundancy (PubMed:26046440, PubMed:26593424). However, later studies showed that YTHDF1, YTHDF2 and YTHDF3 paralogs have redundant functions to a profound extent and directly promote degradation of m6A-containing mRNAs (PubMed:32492408). The effect on translation efficiency observed earlier is probably indirect (PubMed:32492408). {ECO:0000269|PubMed:26046440, ECO:0000269|PubMed:26593424, ECO:0000269|PubMed:32492408}. reclassified-function Q7Z739 YTHDF3 Homo sapiens (Human) 9606 YTH domain-containing family protein 3 (DF3) Was initially reported to act as a regulator of mRNA translation efficiency in cooperation with YTHDF1 by binding to m6A-containing mRNAs and interacting with 40S and 60S ribosome subunits (PubMed:28106072, PubMed:28106076, PubMed:28281539). These studies suggested that the 3 different paralogs (YTHDF1, YTHDF2 and YTHDF3) have unique functions with limited redundancy (PubMed:28106072, PubMed:28106076, PubMed:28281539). However, later studies showed that YTHDF1, YTHDF2 and YTHDF3 paralogs have redundant functions to a profound extent and directly promote degradation of m6A-containing mRNAs (PubMed:32492408). The effect on translation efficiency observed earlier is probably indirect (PubMed:32492408). {ECO:0000269|PubMed:28106072, ECO:0000269|PubMed:28106076, ECO:0000269|PubMed:28281539, ECO:0000269|PubMed:32492408}. reclassified-function Q5D1E8 ZC3H12A Homo sapiens (Human) 9606 Endoribonuclease ZC3H12A (EC 3.1.-.-) (Monocyte chemotactic protein-induced protein 1) (MCP-induced protein 1) (MCPIP-1) (Regnase-1) (Reg1) (Zinc finger CCCH domain-containing protein 12A) Was originally proposed to bind to DNA and act as transcription factor. {ECO:0000305|PubMed:18364357}. reclassified-function P08048 ZFY Homo sapiens (Human) 9606 Zinc finger Y-chromosomal protein Was originally thought to be the testis determining factor (TDF). {ECO:0000305}. reclassified-function P52747 ZNF143 Homo sapiens (Human) 9606 Zinc finger protein 143 (SPH-binding factor) (Selenocysteine tRNA gene transcription-activating factor) (hStaf) Was reported to play a role in chromatin looping together with CTCF (PubMed:25645053, PubMed:38206813). However, it was later shown that the antiboby against ZNF143 crossreacts with CTCF and that ZNF143 is not involved in chromatin looping (PubMed:39708803). {ECO:0000269|PubMed:25645053, ECO:0000269|PubMed:38206813, ECO:0000269|PubMed:39708803}. reclassified-function P20230 Hordeum vulgare (Barley) 4513 Defensin-like protein 1 (Gamma-hordothionin) Was initially thought to be a thionin. {ECO:0000305|PubMed:2176600}. reclassified-function P07597 LTP1 Hordeum vulgare (Barley) 4513 Non-specific lipid-transfer protein 1 (LTP 1) (Probable amylase/protease inhibitor) Was originally thought to be an inhibitor of alpha-amylase or of a protease and was known as PAPI: probable alpha-amylase/protease inhibitor. {ECO:0000305}. reclassified-function P16793 UL52 Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) 10360 Packaging protein UL32 homolog (Protein HFRF1) Was originally thought to be an envelope glycoprotein. {ECO:0000305}. reclassified-function P10216 UL32 Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) 10299 Packaging protein UL32 Was originally thought to be an envelope glycoprotein. {ECO:0000305}. reclassified-function P52463 U36 Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B lymphotropic virus) 10370 Packaging protein UL32 Was originally thought to be an envelope glycoprotein. {ECO:0000305}. reclassified-function P52464 U36 Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus) 57278 Packaging protein UL32 Was originally thought to be an envelope glycoprotein. {ECO:0000305}. reclassified-function Q6Q4H1 PSR Hydra vulgaris (Hydra) (Hydra attenuata) 6087 Bifunctional arginine demethylase and lysyl-hydroxylase PSR (EC 1.14.11.-) (Phosphatidylserine receptor) Was initially thought to constitute the phosphatidylserine receptor, a receptor that mediates recognition of phosphatidylserine, a specific marker only present at the surface of apoptotic cells, and participates in apoptotic cell phagocytosis. However, its nuclear localization and the fact that it is not involved in phagocytosis during apoptosis strongly suggest that it does not constitute the receptor for phosphatidylserine and is not involved in apoptotic cell removal. {ECO:0000305}. reclassified-function B4U7D7 dapA Hydrogenobaculum sp. (strain Y04AAS1) 380749 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q0BYG4 dapA Hyphomonas neptunium (strain ATCC 15444) 228405 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q0R411 Sm1 Hypocrea virens (Gliocladium virens) (Trichoderma virens) 29875 Eliciting plant response-like protein 1 (Extracellular small protein 1) It was previously suggested that monomeric forms were glycosylated at position 29 and glycosylation prevented dimerization that in turn prevented elicitor activity (PubMed:18487198). However, more recent studies demonstrated that the putative glycosylation site is not involved in protein dimerization and deletion of this site does not prevent the protein from testing positive for glycosylation (PubMed:30638659). Thus Sm1 does not seem to be glycosylated but instead may interact with an oligosaccharide or other small molecule (PubMed:30638659). {ECO:0000269|PubMed:18487198, ECO:0000269|PubMed:30638659}. reclassified-function G9MJD8 Sm1 Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens) (Trichoderma virens) 413071 Eliciting plant response-like protein 1 (Extracellular small protein 1) It was previously suggested that monomeric forms were glycosylated at position 29 and glycosylation prevented dimerization that in turn prevented elicitor activity (PubMed:18487198). However, more recent studies demonstrated that the putative glycosylation site is not involved in protein dimerization and deletion of this site does not prevent the protein from testing positive for glycosylation (PubMed:30638659). Thus Sm1 does not seem to be glycosylated but instead may interact with an oligosaccharide or other small molecule (PubMed:30638659). {ECO:0000269|PubMed:18487198, ECO:0000269|PubMed:30638659}. reclassified-function Q5QU03 dapA Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) 283942 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5QXL5 dapB Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) 283942 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7QK46 Qptc Ixodes scapularis (Black-legged tick) (Deer tick) 6945 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry. However, a recent study suggests a Zn(2+)-independent catalytic mechanism. {ECO:0000269|PubMed:24598748}. reclassified-function Q28WG2 dapA Jannaschia sp. (strain CCS1) 290400 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6T235 dapB Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis) 375286 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8Z624 dapA Karelsulcia muelleri (strain GWSS) (Sulcia muelleri) 444179 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6W828 dapA Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) 266940 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q75UN0 fbiB Kitasatospora aureofaciens (Streptomyces aureofaciens) 1894 Bifunctional F420 biosynthesis protein FbiB [Includes: Coenzyme F420:L-glutamate ligase (EC 6.3.2.31) (EC 6.3.2.34) (Coenzyme F420-0:L-glutamate ligase) (Coenzyme F420-1:gamma-L-glutamate ligase); Dehydro-coenzyme F420-0 reductase (EC 1.3.8.17)] Was originally (PubMed:15215601) thought to be a probable tetracycline dehydrogenase since it is essential to the final reaction in the biosynthesis of 6-demethyltetracycline, but enzymatic activity has not been proven. Several facts suggest it is more likely to be a coenzyme F420:L-glutamate ligase: it is a homolog of the characterized protein CofE from Methanococcus jannaschii and FbiB from Mycobacterium smegmatis which are involved in the polyglutamylation of F420-0; F420 is used for tetracycline biosynthesis, probably being necessary for the last step; the gene coding for this protein is close to a homolog of the characterized protein CofD from Methanococcus jannaschii involved in F420-0 production. {ECO:0000305|PubMed:15215601}. reclassified-function A0A0H3H456 dhaM Klebsiella michiganensis (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686 / BUCSAV 143 / CCM 1901) 1006551 PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM (EC 2.7.1.121) (Dihydroxyacetone kinase subunit M) Was reported to be a protein deacetylase that removes acetyl groups on specific lysine residues in target proteins (PubMed:26716769). However, later experiments demonstrate that the protein ortholog in E.coli does not have any protein deacetylase activity; the discrepancy observed seems to be due to contaminants having proteolytic activity (PubMed:29939131). {ECO:0000269|PubMed:26716769, ECO:0000269|PubMed:29939131}. reclassified-function P45415 dapB Klebsiella pneumoniae 573 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6TCA1 dapA Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) 272620 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6T4H8 dapB Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) 272620 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B5Y210 dapB Klebsiella variicola (strain 342) (Klebsiella pneumoniae) 507522 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P0CW87 acsAB Komagataeibacter xylinus (Gluconacetobacter xylinus) 28448 Cellulose synthase 1 [Includes: Cellulose synthase catalytic domain [UDP-forming] (EC 2.4.1.12); Cyclic di-GMP-binding domain (Cellulose synthase 1 regulatory domain)] Was originally proposed to code for two separate adjacent ORFs, ascA and ascB. {ECO:0000305|PubMed:2151718}. reclassified-function Q1INQ6 dapA Koribacter versatilis (strain Ellin345) 204669 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C5CHX9 dapA Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1) 521045 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A9KHY6 dapA Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) (Clostridium phytofermentans) 357809 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9RE09 hprK Lacticaseibacillus casei (Lactobacillus casei) 1582 HPr kinase/phosphorylase (HPrK/P) (EC 2.7.11.-) (EC 2.7.4.-) (HPr kinase/phosphatase) (HPr(Ser) kinase/phosphorylase) Was originally (PubMed:10762262) called HPr kinase/phosphatase, but P-Ser-HPr dephosphorylation was shown (PubMed:12359880) to follow a quite unique mechanism, in which Pi instead of H(2)O is used for the nucleophilic attack on the phosphoryl group. P-Ser-HPr dephosphorylation is therefore not a phosphohydrolysis but a phospho-phosphorolysis reaction, and the bifunctional enzyme was dubbed HPr kinase/phosphorylase. {ECO:0000305|PubMed:10762262, ECO:0000305|PubMed:12359880}. reclassified-function B3W7E5 dapA Lacticaseibacillus casei (strain BL23) (Lactobacillus casei) 543734 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q03CW3 dapA Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei) 321967 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P26298 Lactiplantibacillus pentosus (Lactobacillus pentosus) 1589 D-lactate dehydrogenase (D-LDH) (EC 1.1.1.28) (D-specific 2-hydroxyacid dehydrogenase) Was originally thought to originate from L.plantarum. {ECO:0000305|PubMed:1840590}. reclassified-function P56511 ldh Lactiplantibacillus pentosus (Lactobacillus pentosus) 1589 L-lactate dehydrogenase (L-LDH) (EC 1.1.1.27) Was originally thought to originate from L.plantarum (PubMed:1425707, PubMed:1840590). {ECO:0000305}. reclassified-function Q88W01 dapB Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum) 220668 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5FKQ9 dapA Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) 272621 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5FKQ8 dapB Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) 272621 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8YUT3 dapA Lactobacillus helveticus (strain DPC 4571) 405566 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8YUT4 dapB Lactobacillus helveticus (strain DPC 4571) 405566 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9R5V5 ntd Lactobacillus leichmannii 28039 Nucleoside deoxyribosyltransferase (N-deoxyribosyltransferase) (EC 2.4.2.6) Was originally thought to originate from E.coli. {ECO:0000305|PubMed:7797550}. reclassified-function A2RJL6 dapA Lactococcus lactis subsp. cremoris (strain MG1363) 416870 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A2RJS9 dapB Lactococcus lactis subsp. cremoris (strain MG1363) 416870 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q02XU7 dapA Lactococcus lactis subsp. cremoris (strain SK11) 272622 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q02Y20 dapB Lactococcus lactis subsp. cremoris (strain SK11) 272622 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9CF61 dapA Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) 272623 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9CFC0 dapB Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) 272623 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C1DD55 dapA Laribacter hongkongensis (strain HLHK9) 557598 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C1D7H9 dapB Laribacter hongkongensis (strain HLHK9) 557598 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1MPX7 dapA Lawsonia intracellularis (strain PHE/MN1-00) 363253 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q1MRS7 dapB Lawsonia intracellularis (strain PHE/MN1-00) 363253 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5IEB3 dapA Legionella pneumophila (strain Corby) 400673 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5I9V1 dapB Legionella pneumophila (strain Corby) 400673 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5WUD4 dapA Legionella pneumophila (strain Lens) 297245 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5X090 dapB Legionella pneumophila (strain Lens) 297245 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5X8U7 dapB Legionella pneumophila (strain Paris) 297246 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5ZT51 dapA Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) 272624 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5ZZ80 dapB Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) 272624 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0SL58 dapA Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris) 456481 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B0SCT0 dapA Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames) 355278 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q04U80 dapA Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) 355277 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q04U79 dapB Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) 355277 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q053P3 dapA Leptospira borgpetersenii serovar Hardjo-bovis (strain L550) 355276 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q053P2 dapB Leptospira borgpetersenii serovar Hardjo-bovis (strain L550) 355276 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8F132 dapA Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) 189518 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8F133 dapB Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) 189518 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q72U22 dapA Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) 267671 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q72U21 dapB Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) 267671 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P0C7T0 recA Leptospira meyeri 29508 Protein RecA (Recombinase A) Was originally thought to originate from Leptospira biflexa; taxonomy has been changed based on information in PubMed:11751822. {ECO:0000305|PubMed:8566806}. reclassified-function B1Y7F0 dapA Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) 395495 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1MZM8 dapA Leuconostoc citreum (strain KM20) 349519 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P50889 rps1 Leuconostoc lactis 1246 Small ribosomal subunit protein bS1 (30S ribosomal protein S1) Was originally (PubMed:7721096, PubMed:8568274) thought to originate from human but is most probably the result of a cDNA library contamination by L.lactis. {ECO:0000305}. reclassified-function Q03YE2 dapA Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y) 203120 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q1WU86 dapA Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius) 362948 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q1WU20 dapB Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius) 362948 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2GC11 dapA Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus fermentum) 334390 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B2GC12 dapB Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus fermentum) 334390 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5VJ58 dapA Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri) 557436 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B2G6M9 dapA Limosilactobacillus reuteri subsp. reuteri (strain JCM 1112) (Lactobacillus reuteri) 557433 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q92BS0 dapA Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262) 272626 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q92AA1 dapB Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262) 272626 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8DE74 dapA Listeria monocytogenes serotype 4a (strain HCC23) 552536 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8DC19 dapB Listeria monocytogenes serotype 4a (strain HCC23) 552536 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C1L2Z1 dapA Listeria monocytogenes serotype 4b (strain CLIP80459) 568819 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C1KWK7 dapB Listeria monocytogenes serotype 4b (strain CLIP80459) 568819 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q71ZN5 dapA Listeria monocytogenes serotype 4b (strain F2365) 265669 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q71YA8 dapB Listeria monocytogenes serotype 4b (strain F2365) 265669 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8Y766 dapA Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) 169963 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8Y5Z6 dapB Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) 169963 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7AP54 hbp2 Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) 169963 Hemin/hemoglobin-binding protein 2 (Hn/Hb-binding protein 2) (P64) (Surface virulence-associated protein A) Was originally thought to have a more extreme phenotype upon deletion; however the 100-fold reduction in virulence of the first deletion experiment, and impairment of phagosome escape seen in infected mice, is probably due to the kanamycin-cassette derivative used in that experiment. {ECO:0000269|PubMed:11700342, ECO:0000305|PubMed:15661014}. reclassified-function A0AIN8 dapA Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CCUG 15529 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8) 386043 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0AK12 dapB Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CCUG 15529 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8) 386043 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P22176 MCP Lymphocystis disease virus 1 (isolate Darai) (LCDV-1) 654922 Major capsid protein (MCP) (P50) Was originally thought to be a thymidine kinase. {ECO:0000305|PubMed:2024501}. reclassified-function P39044 X Lysinibacillus sphaericus (Bacillus sphaericus) 1421 Uncharacterized protein X Was originally (Ref.1) incorrectly stated to be similar to the S14P family of ribosomal proteins. {ECO:0000305}. reclassified-function B1HTF0 dapB Lysinibacillus sphaericus (strain C3-41) 444177 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q4R632 AGBL2 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) 9541 Cytosolic carboxypeptidase 2 (EC 3.4.17.-) (ATP/GTP-binding protein-like 2) (Protein deglutamylase CCP2) Was initially shown to catalyze the removal of carboxy-terminus tyrosine from alpha-tubulin (By similarity). However, later studies did not identified any detyrosinase or deglycylase activities from the carboxy-terminus of tubulin (By similarity). {ECO:0000250|UniProtKB:Q5U5Z8, ECO:0000250|UniProtKB:Q8CDK2}.; reclassified-function Q4R683 CDADC1 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) 9541 dCTP deaminase (EC 3.5.4.13) (Cytidine and dCMP deaminase domain-containing protein 1) (Deoxycytidine triphosphate deaminase) (Testis development protein NYD-SP15) CDADC1 was initially reported to exhibit cytidine deaminase activity (By similarity). However, subsequent studies demonstrated that it specifically deaminates dCTP, with no activity toward cytidine or deoxycytidine. The initial attribution may have been an artifact of using partially purified recombinant protein. While one study reported weak activity on dCMP, another failed to detect any dCMP deamination (By similarity). {ECO:0000250|UniProtKB:Q9BWV3}. reclassified-function Q4R942 QPCTL Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) 9541 Glutaminyl-peptide cyclotransferase-like protein (EC 2.3.2.5) (Golgi-resident glutaminyl-peptide cyclotransferase) (isoQC) (gQC) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (By similarity). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000250|UniProtKB:Q16769}. reclassified-function Q5IS35 SLC25A19 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) 9541 Mitochondrial thiamine pyrophosphate carrier (Solute carrier family 25 member 19) Previously identified as the mitochondrial deoxyribonucleotide carrier. However other experiments later demonstrated that SLC25A19 is a thiamine diphosphate transporter and not a mitochondrial deoxyribonucleotide carrier. {ECO:0000250|UniProtKB:Q9HC21}. reclassified-function B9EBZ6 dapA Macrococcoides caseolyticum (strain JCSC5402) (Macrococcus caseolyticus) 458233 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0LDB5 dapA Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1) 156889 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0L4Z4 dapB Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1) 156889 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P36175 tsaD Mannheimia haemolytica (Pasteurella haemolytica) 75985 tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD) (tRNA threonylcarbamoyladenosine biosynthesis protein TsaD) Was originally thought to have endopeptidase activity (PubMed:1885539). But it could not be confirmed with orthologs purified from P.abyssi (PubMed:17766251, PubMed:21183954). {ECO:0000305|PubMed:1885539}. reclassified-function Q65TY2 dapB Mannheimia succiniciproducens (strain KCTC 0769BP / MBEL55E) 221988 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C6BSH4 dapA Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763) (Desulfovibrio salexigens) 526222 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C6BTW9 dapB Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763) (Desulfovibrio salexigens) 526222 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1U1A6 dapA Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter aquaeolei) 351348 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9S3W8 dapB Mastigocladus laminosus (Fischerella sp.) 83541 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P56848 ISPE Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata) 34256 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase, chloroplastic (EC 2.7.1.148) (4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase) (CMK) Was originally thought to be an isopentenyl monophosphate kinase. {ECO:0000305|PubMed:10570138}. reclassified-function P93257 ELI3 Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum) 3544 Probable mannitol dehydrogenase (EC 1.1.1.255) (NAD-dependent mannitol dehydrogenase) Was originally (Ref.1) thought to be a cinnamyl-alcohol dehydrogenase. {ECO:0000305}. reclassified-function P0DRH4 Mesomexovis punctatus (Scorpion) (Vaejovis punctatus) 1532993 Antimicrobial peptide VpCT2 Jimenez-Vargas et al. (2021) report this protein originates from Mesomexovis variegatus, while Quintero-Hernandez et al. (2015) sequenced it from Vaejovis punctatus. This discrepancy may stem from taxonomic history: V.punctatus was previously classified as V.punctatus variegatus Pocock, 1898. It should be noted that Mesomexovis variegatus and Mesomexovis punctatus represent two distinct species. {ECO:0000305}. reclassified-function P0DRH5 Mesomexovis punctatus (Scorpion) (Vaejovis punctatus) 1532993 Antimicrobial peptide VpCT3 Jimenez-Vargas et al. (2021) report this protein originates from Mesomexovis variegatus, while Quintero-Hernandez et al. (2015) sequenced it from Vaejovis punctatus. This discrepancy may stem from taxonomic history: V.punctatus was previously classified as V.punctatus variegatus Pocock, 1898. It should be noted that Mesomexovis variegatus and Mesomexovis punctatus represent two distinct species. {ECO:0000305}. reclassified-function P0DRH6 Mesomexovis punctatus (Scorpion) (Vaejovis punctatus) 1532993 Antimicrobial peptide VpCT4 Jimenez-Vargas et al. (2021) report this protein originates from Mesomexovis variegatus, while Quintero-Hernandez et al. (2015) sequenced it from Vaejovis punctatus. This discrepancy may stem from taxonomic history: V.punctatus was previously classified as V.punctatus variegatus Pocock, 1898. It should be noted that Mesomexovis variegatus and Mesomexovis punctatus represent two distinct species. {ECO:0000305}. reclassified-function P0DRH3 Mesomexovis punctatus (Scorpion) (Vaejovis punctatus) 1532993 Antimicrobial peptide VpCT1 Jimenez-Vargas et al. (2021) report this protein originates from Mesomexovis variegatus, while Quintero-Hernandez et al. (2015) sequenced it from Vaejovis punctatus. This discrepancy may stem from taxonomic history: V.punctatus was previously classified as V.punctatus variegatus Pocock, 1898. It should be noted that Mesomexovis variegatus and Mesomexovis punctatus represent two distinct species. {ECO:0000305}. reclassified-function P58207 dapA Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) 266835 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P58210 dapB1 Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) 266835 4-hydroxy-tetrahydrodipicolinate reductase 1 (HTPA reductase 1) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P58211 dapB2 Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) 266835 4-hydroxy-tetrahydrodipicolinate reductase 2 (HTPA reductase 2) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5ULF8 dapA Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS) 420247 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5ULF7 dapB Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS) 420247 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q58829 Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) 243232 Putative DNA repair glycosylase MJ1434 Was originally thought to have uracil-DNA glycosylase activity, but further protein analysis show that it does not exhibit DNA uracil glycosylase activity when produced in an Ung-deficient Escherichia coli host. {ECO:0000269|PubMed:12682355, ECO:0000269|PubMed:20410075}.; reclassified-function P58416 comE Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) 243232 Sulfopyruvate decarboxylase subunit beta (EC 4.1.1.79) The sequence corresponding to this entry was originally entered in Swiss-Prot as AC Q57704 in November 1997 and was deleted in July 1999 because TIGR removed the CDS for that ORF. We have recreated it because of the evidence (PubMed:10940029) that it really exists. {ECO:0000305|PubMed:10940029}. reclassified-function Q57695 dapA Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) 243232 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q57865 dapB Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) 243232 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q58635 proS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) 243232 Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS) Was originally (PubMed:10642548, PubMed:10869184, PubMed:11141055) thought to have both prolyl- and cysteinyl-tRNA synthetase activities (ProCysRS). However, recent biochemical and structural studies show that ProRS misaminoacylates tRNA(Pro) with cysteine but is unable to aminoacylate tRNA(Cys). These conflicting results may be due to the fact that much of the previous work was done with unfractionated tRNA. {ECO:0000305}.; reclassified-function Q58018 thi4 Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) 243232 Thiamine thiazole synthase (EC 2.4.2.59) This protein was originally thought to have NAD-dependent ribose 1,5-bisphosphate isomerase activity but the recombinant protein was not active in vitro (PubMed:15375115, PubMed:26919468). In contrast, another protein from M.jannaschii likely possesses this activity (MJ0122). {ECO:0000305|PubMed:15375115, ECO:0000305|PubMed:26919468}. reclassified-function Q12ZG2 dapA Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M) 259564 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q12ZG1 dapB Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M) 259564 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6UVG7 dapA Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3) 419665 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6UUT2 dapB Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3) 419665 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A4FYQ3 dapA Methanococcus maripaludis (strain C5 / ATCC BAA-1333) 402880 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4FXV6 dapB Methanococcus maripaludis (strain C5 / ATCC BAA-1333) 402880 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A9A656 dapA Methanococcus maripaludis (strain C6 / ATCC BAA-1332) 444158 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A9AB21 dapB Methanococcus maripaludis (strain C6 / ATCC BAA-1332) 444158 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6VJM9 dapA Methanococcus maripaludis (strain C7 / ATCC BAA-1331) 426368 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6VFL4 dapB Methanococcus maripaludis (strain C7 / ATCC BAA-1331) 426368 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6LZP8 dapA Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL) 267377 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6LYR5 dapB Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL) 267377 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6US71 dapA Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB) 406327 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6UNQ4 dapB Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB) 406327 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q50833 sla Methanococcus voltae 2188 S-layer protein (Cell surface glycoprotein) (Surface layer protein) Was originally thought to be a P-type ATPase. {ECO:0000305|PubMed:1825827}. reclassified-function A2SQU8 dapA Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z) 410358 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A2SQU7 dapB Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z) 410358 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3CVI7 dapA Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) 368407 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A3CVI6 dapB Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) 368407 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8TUZ4 dapA Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) 190192 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8TVG7 dapB Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) 190192 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7I854 dapB Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8) 456442 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8THP1 dapA Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) 188937 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8THP0 dapB Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) 188937 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8TM19 thi4 Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) 188937 Thiamine thiazole synthase (EC 2.4.2.59) This protein was originally thought to have ribose 1,5-bisphosphate isomerase activity despite the fact that some recombinant ortholog proteins were not active in vitro (PubMed:15375115, PubMed:17303759). Moreover, another protein from M.acetivorans likely possesses this activity (MA_0379). Finally, a thiamine synthase activity has been shown for the ortholog protein in M.jannaschii. {ECO:0000305}. reclassified-function Q46DC4 dapA Methanosarcina barkeri (strain Fusaro / DSM 804) 269797 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q46DC3 dapB Methanosarcina barkeri (strain Fusaro / DSM 804) 269797 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8PXL7 dapA Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) 192952 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8PXL6 dapB Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) 192952 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2NHW2 dapA Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3) 339860 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2NHW0 dapB Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3) 339860 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8GKG7 dapA Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c) 521011 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2FNR0 dapA Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) 323259 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2FNQ9 dapB Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) 323259 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O26249 cbiT Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) 187420 Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (EC 2.1.1.196) Was originally thought to be a precorrin-8w decarboxylase. {ECO:0000305}. reclassified-function O26892 dapA Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) 187420 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function O26891 dapB Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) 187420 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O27404 fpaA Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) 187420 Coenzyme F420H(2) oxidase (EC 1.5.3.22) (FMN protein FprA) (Flavoprotein A) (Type A flavoprotein FprA) Was originally thought to be a subunit of methylviologen hydrolase II. {ECO:0000305|PubMed:8376343}. reclassified-function A0B7E1 dapA Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT) (Methanosaeta thermophila) 349307 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A2SIX7 dapA Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1) 420662 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1LTD9 dapA Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1) 426355 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8EIQ3 dapB Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2) 395965 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q60B13 dapA Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) 243233 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q607A7 dapB Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) 243233 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0JL91 dapA Microcystis aeruginosa (strain NIES-843 / IAM M-2473) 449447 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2RJK7 dapA Moorella thermoacetica (strain ATCC 39073 / JCM 9320) 264732 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2RJL2 dapB Moorella thermoacetica (strain ATCC 39073 / JCM 9320) 264732 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P81786 Moraxella sp. (strain TAE123) 191545 Aldehyde dehydrogenase (EC 1.2.1.3) Was originally described as an NAD(+)-dependent alcohol dehydrogenase (ADH) (PubMed:9660191). However, BLAST alignments indicate that this fragment represents the N-terminal sequence of an aldehyde dehydrogenase. The protein characterized in this article does not correspond to the sequenced fragment but to the alcohol dehydrogenase as shown in the UniProtKB AC Q8GIX7 entry. {ECO:0000269|PubMed:9660191, ECO:0000305}. reclassified-function P43142 Ackr5 Mus musculus (Mouse) 10090 Atypical chemokine receptor 5 (G protein-coupled receptor 182) (G10D) (NOW) Was originally thought to be a receptor for adrenomedullin (By similarity). However, this function was later not confirmed (By similarity). {ECO:0000250|UniProtKB:O15218}. reclassified-function Q6F3F9 Adgrg6 Mus musculus (Mouse) 10090 Adhesion G protein-coupled receptor G6 (Developmentally regulated G protein-coupled receptor) (G protein-coupled receptor 126) [Cleaved into: Adhesion G protein-coupled receptor G6, N-terminal fragment (ADGRG6 N-terminal fragment) (ADGRG6-NTF); Adhesion G protein-coupled receptor G6, C-terminal fragment (ADGRG6 C-terminal fragment) (ADGRG6-CTF)] Was initially thought to play a role in cardiac development (PubMed:21124978, PubMed:24082093). However, it was later shown that the cardiac phenotype in knockout mice is due to defects in placental development (PubMed:34767447). {ECO:0000269|PubMed:21124978, ECO:0000269|PubMed:24082093, ECO:0000269|PubMed:34767447}. reclassified-function Q8CDK2 Agbl2 Mus musculus (Mouse) 10090 Cytosolic carboxypeptidase 2 (EC 3.4.17.-) (ATP/GTP-binding protein-like 2) (Protein deglutamylase CCP2) Was initially shown to catalyze the removal of carboxy-terminus tyrosine from alpha-tubulin (By similarity). However, later studies did not identified any detyrosinase or deglycylase activities from the carboxy-terminus of tubulin (PubMed:25103237). {ECO:0000250|UniProtKB:Q5U5Z8, ECO:0000269|PubMed:25103237}.; reclassified-function Q9ESW4 Agk Mus musculus (Mouse) 10090 Acylglycerol kinase, mitochondrial (EC 2.7.1.107) (EC 2.7.1.138) (EC 2.7.1.94) (Multiple substrate lipid kinase) (MuLK) (Multi-substrate lipid kinase) Was originally (PubMed:15252046) thought to have ceramide kinase activity. Such activity is however unlikely in vivo. {ECO:0000305|PubMed:15252046}. reclassified-function P55249 Alox12e Mus musculus (Mouse) 10090 Polyunsaturated fatty acid (12S)/(13S)-lipoxygenase, epidermal-type (EC 1.13.11.-) (Arachidonate (12S)-lipoxygenase, epidermal-type) (12-LOX-e) (e(12S)-LOX) (EC 1.13.11.31) (Linoleate (13S)-lipoxygenase) Was originally thought to be an arachidonate 8-lipoxygenase and was called LOX8. {ECO:0000305}. reclassified-function P98084 Apba2 Mus musculus (Mouse) 10090 Amyloid-beta A4 precursor protein-binding family A member 2 (Adapter protein X11beta) (Neuron-specific X11L protein) (Neuronal Munc18-1-interacting protein 2) (Mint-2) Was originally thought to be the ortholog of human X11 (APBA1). {ECO:0000305|PubMed:15489334}. reclassified-function Q9WV31 Arc Mus musculus (Mouse) 10090 Activity-regulated cytoskeleton-associated protein (mArc) (Activity-regulated gene 3.1 protein) (ARC/ARG3.1) (Arg3.1) Genetic disruption of the protein-coding gene was initially reported to cause early embryonic lethality (PubMed:10727859). However, only a partial deletion of the coding region was performed, leading to dominant-negative effects (PubMed:10727859). A complete deletion of the coding region later showed that mice are viable and display deficits in several forms of long-term memory formation (PubMed:17088210). {ECO:0000269|PubMed:10727859, ECO:0000269|PubMed:17088210}. reclassified-function Q61210 Arhgef1 Mus musculus (Mouse) 10090 Rho guanine nucleotide exchange factor 1 (Lbc's second cousin) (Lymphoid blast crisis-like 2) Ref.2 sequence was originally submitted as from rat origin. {ECO:0000305}. reclassified-function Q8BVM4 Azin2 Mus musculus (Mouse) 10090 Antizyme inhibitor 2 (AzI2) (Arginine decarboxylase-like protein) (ADC) (ARGDC) (Ornithine decarboxylase-like protein) (ODC-like protein) (ornithine decarboxylase paralog) (ODC-p) The human ortholog was initially reported to have ornithine or arginine decarboxylase activities, but it was later found to possess neither of them. {ECO:0000305|PubMed:16916800}.; reclassified-function Q8R2X8 Blzf1 Mus musculus (Mouse) 10090 Golgin-45 (Basic leucine zipper nuclear factor 1) Was initially thought to be a potential transcription factor, localized in the nucleus. {ECO:0000305}. reclassified-function Q9JMG2 C1galt1c1 Mus musculus (Mouse) 10090 C1GALT1-specific chaperone 1 (Core 1 beta1,3-galactosyltransferase 2) (C1Gal-T2) (C1GalT2) (Core 1 beta3-Gal-T2) (mC1Gal-T2) (Core 1 beta3-galactosyltransferase-specific molecular chaperone) Was originally assigned to be a glycosyltransferase. {ECO:0000305}. reclassified-function P24452 Capg Mus musculus (Mouse) 10090 Macrophage-capping protein (Actin regulatory protein CAP-G) (Actin-capping protein GCAP39) (Myc basic motif homolog 1) This protein was originally thought to be a DNA-binding protein with a helix-loop-helix domain. {ECO:0000305}. reclassified-function Q8BMD5 Cdadc1 Mus musculus (Mouse) 10090 dCTP deaminase (EC 3.5.4.13) (Cytidine and dCMP deaminase domain-containing protein 1) (Deoxycytidine triphosphate deaminase) (Testis development protein NYD-SP15) CDADC1 was initially reported to exhibit cytidine deaminase activity (By similarity). However, subsequent studies demonstrated that it specifically deaminates dCTP, with no activity toward cytidine or deoxycytidine. The initial attribution may have been an artifact of using partially purified recombinant protein. While one study reported weak activity on dCMP, another failed to detect any dCMP deamination (By similarity). {ECO:0000250|UniProtKB:Q9BWV3}. reclassified-function Q8R4E9 Cdt1 Mus musculus (Mouse) 10090 DNA replication factor Cdt1 (Double parked homolog) (DUP) (Retroviral insertion site 2 protein) Was originally thought to have DNA binding activity (PubMed:12192004). However, more recent studies show that CDT1 binds DNA indirectly via ORC. {ECO:0000269|PubMed:12192004, ECO:0000305}. reclassified-function Q9WTK2 Cdyl Mus musculus (Mouse) 10090 Chromodomain Y-like protein (CDY-like) (Crotonyl-CoA hydratase) (EC 4.2.1.-) (Putative histone acetyltransferase Cdyl) (EC 2.3.1.48) Was initially reported to display histone acetyltransferase activity, with a preference for histone H4 (PubMed:12072557). Such activity is however unsure in vivo. Histone acetyltransferase activity would be in contradiction with the function of the protein in corepressor complexes (PubMed:12947414). Moreover, crystallographic studies in human demonstrated that it does not share any similarity with other acetyltransferases and instead forms a crotonase-like fold. {ECO:0000250|UniProtKB:Q9Y232, ECO:0000269|PubMed:12072557, ECO:0000269|PubMed:12947414}. reclassified-function Q8VCT4 Ces1d Mus musculus (Mouse) 10090 Carboxylesterase 1D (Carboxylesterase 3) (EC 3.1.1.1, EC 3.1.1.67) (Fatty acid ethyl ester synthase) (FAEE synthase) (Triacylglycerol hydrolase) (TGH) Was originally thought to originate from human. {ECO:0000305|PubMed:10518925}. reclassified-function P01216 Cga Mus musculus (Mouse) 10090 Glycoprotein hormones alpha chain (Anterior pituitary glycoprotein hormones common subunit alpha) (Follicle-stimulating hormone alpha chain) (FSH-alpha) (Follitropin alpha chain) (Luteinizing hormone alpha chain) (LSH-alpha) (Lutropin alpha chain) (Thyroid-stimulating hormone alpha chain) (TSH-alpha) (Thyrotropin alpha chain) PubMed:6177696 sequence was originally thought to originate from rat. {ECO:0000305}. reclassified-function Q8C6L5 Cgas Mus musculus (Mouse) 10090 Cyclic GMP-AMP synthase (cGAMP synthase) (cGAS) (m-cGAS) (EC 2.7.7.86) (2'3'-cGAMP synthase) (Mab-21 domain-containing protein 1) Was reported to homodimerize in presence of double-stranded DNA (dsDNA) (PubMed:24332030). However, this result was based on a structure lacking the N-terminal part (1-146), which caused homodimerization in presence of dsDNA (PubMed:28214358). {ECO:0000269|PubMed:24332030}. reclassified-function Q8C196 Cps1 Mus musculus (Mouse) 10090 Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC 6.3.4.16) (Carbamoyl-phosphate synthetase I) (CPSase I) Was initially reported to be deacetylated by Sirt5 (PubMed:19410549). However, it was later shown that Sirt5 has poor deacetylase activity and mediates desuccinylation of Cps1 instead (PubMed:22076378). {ECO:0000305|PubMed:19410549, ECO:0000305|PubMed:22076378}. reclassified-function Q99LD8 Ddah2 Mus musculus (Mouse) 10090 Putative hydrolase DDAH2 (EC 3.-.-.-) (DDAHII) (Inactive N(G),N(G)-dimethylarginine dimethylaminohydrolase 2) (DDAH-2) (Inactive dimethylarginine dimethylaminohydrolase 2) Was originally thought to be a dimethylarginine dimethylaminohydrolase (with EC:3.5.3.18) able to hydrolyze N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA). However, a recent multicentre study have shown that DDAH2 does not have dimethylarginine dimethylaminohydrolase activity by using different approaches. {ECO:0000269|PubMed:21493890, ECO:0000269|PubMed:37296100}. reclassified-function Q9CXR1 Dhrs7 Mus musculus (Mouse) 10090 Dehydrogenase/reductase SDR family member 7 (EC 1.1.1.-) (Retinal short-chain dehydrogenase/reductase 4) (retSDR4) (Short chain dehydrogenase/reductase family 34C member 1) (Protein SDR34C1) DHRS7 was originally reported to be anchored in the endoplasmic reticulum membrane and facing the lumen (By similarity). However, the catalytic moiety was later shown to be facing the cytosol (By similarity). {ECO:0000250|UniProtKB:Q9Y394}. reclassified-function Q3V0Q1 Dnah12 Mus musculus (Mouse) 10090 Dynein axonemal heavy chain 12 (Axonemal beta dynein heavy chain 12) (Axonemal dynein heavy chain 12-like protein) (Axonemal dynein heavy chain 7-like protein) (Ciliary dynein heavy chain 12) Was originally derived from a readthrough transcript including ASB14 and DNAH12. {ECO:0000305}. reclassified-function Q9QYI6 Dnajb9 Mus musculus (Mouse) 10090 DnaJ homolog subfamily B member 9 (Endoplasmic reticulum DNA J domain-containing protein 4) (ER-resident protein ERdj4) (ERdj4) (mDj7) Was initially thought to be an integral membrane protein (PubMed:11836248). However, it was later shown that it is a soluble luminal protein localized in the endoplasmic reticulum lumen. {ECO:0000269|PubMed:11836248, ECO:0000269|PubMed:22267725}. reclassified-function P0DOY1 Dnmt3c Mus musculus (Mouse) 10090 DNA (cytosine-5)-methyltransferase 3C (Dnmt3c) (EC 2.1.1.37) Evolved via a duplication of Dnmt3B and was initially annotated as a pseudogene. {ECO:0000269|PubMed:27856912}. reclassified-function Q921E6 Eed Mus musculus (Mouse) 10090 Polycomb protein EED Was originally thought (PubMed:9234727) to interact with HNRNPK. This apparent interaction may be mediated by the translated product of the 5'-UTR sequence of the 2-hybrid clone. {ECO:0000305|PubMed:9234727}. reclassified-function Q9CY45 Eef1akmt1 Mus musculus (Mouse) 10090 EEF1A lysine methyltransferase 1 (EC 2.1.1.-) (N(6)-adenine-specific DNA methyltransferase 2) (Protein-lysine N-methyltransferase N6amt2) Was originally thought to be an N(6)-adenine-specific DNA methyltransferase based on primary sequence and predicted secondary structure. {ECO:0000255|HAMAP-Rule:MF_03187}. reclassified-function Q7TT37 Elp1 Mus musculus (Mouse) 10090 Elongator complex protein 1 (ELP1) (IkappaB kinase complex-associated protein) (IKK complex-associated protein) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:O95163}. reclassified-function Q91WG4 Elp2 Mus musculus (Mouse) 10090 Elongator complex protein 2 (ELP2) (STAT3-interacting protein 1) (StIP1) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q6IA86}. reclassified-function Q9CZX0 Elp3 Mus musculus (Mouse) 10090 Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}.; reclassified-function Q9ER73 Elp4 Mus musculus (Mouse) 10090 Elongator complex protein 4 (PAX6 neighbor gene protein) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}. reclassified-function Q99L85 Elp5 Mus musculus (Mouse) 10090 Elongator complex protein 5 (Dermal papilla-derived protein 6 homolog) (Retinoic acid-induced protein 12) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q8TE02}. reclassified-function Q8BK75 Elp6 Mus musculus (Mouse) 10090 Elongator complex protein 6 (Protein TMEM103) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q0PNE2}. reclassified-function Q8C9A2 Endov Mus musculus (Mouse) 10090 Endonuclease V (EC 3.1.26.-) Was initially characterized as an endodeoxyribonuclease involved in DNA repair (PubMed:12853604). While it shows some weak endodeoxyribonuclease activity in vitro, such activity probably does not exist in vivo. {ECO:0000305|PubMed:12853604}. reclassified-function P49222 Epb42 Mus musculus (Mouse) 10090 Protein 4.2 (P4.2) (Erythrocyte membrane protein band 4.2) (Erythrocyte protein 4.2) Was originally thought to be pallidin. {ECO:0000305|PubMed:7959722}. reclassified-function P17257 Fam167b Mus musculus (Mouse) 10090 Protein FAM167B (Protein SEC) Was originally thought to originate from human. {ECO:0000305|PubMed:2349114}. reclassified-function Q61345 Foxd1 Mus musculus (Mouse) 10090 Forkhead box protein D1 (Brain factor 2) (BF-2) (Forkhead-related protein FKHL8) (Forkhead-related transcription factor 4) (FREAC-4) (HFH-BF-2) Was originally assigned to be BF-2 (FOXG1). {ECO:0000305|PubMed:7815060}. reclassified-function Q8CF93 Galnt13 Mus musculus (Mouse) 10090 Polypeptide N-acetylgalactosaminyltransferase 13 (EC 2.4.1.41) (Polypeptide GalNAc transferase 13) (GalNAc-T13) (pp-GaNTase 13) (Protein-UDP acetylgalactosaminyltransferase 13) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13) Was initially wrongly assigned as Galnt8. {ECO:0000305}. reclassified-function Q9JJ61 Galnt16 Mus musculus (Mouse) 10090 Polypeptide N-acetylgalactosaminyltransferase 16 (EC 2.4.1.41) (Polypeptide GalNAc transferase 16) (GalNAc-T16) (Polypeptide GalNAc transferase-like protein 1) (GalNAc-T-like protein 1) (pp-GaNTase-like protein 1) (Polypeptide N-acetylgalactosaminyltransferase-like protein 1) (Protein-UDP acetylgalactosaminyltransferase-like protein 1) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1) Was originally termed Galnt10/pp-GaNTase 10. {ECO:0000305|PubMed:15018805}. reclassified-function Q01721 Gas1 Mus musculus (Mouse) 10090 Growth arrest-specific protein 1 (GAS-1) Was initially reported to act as a negative regulator of smoothened signaling pathway (PubMed:11572986). However, it was later shown to positively regulate smoothened signaling by promoting SHH handoff to its receptor (PubMed:17504940, PubMed:21664576, PubMed:33038332). {ECO:0000269|PubMed:11572986, ECO:0000269|PubMed:17504940, ECO:0000269|PubMed:21664576, ECO:0000269|PubMed:33038332}. reclassified-function Q8BKT3 Gcfc2 Mus musculus (Mouse) 10090 Intron Large complex component GCFC2 (GC-rich sequence DNA-binding factor) (GC-rich sequence DNA-binding factor 2) (Transcription factor 9) (TCF-9) Was originally thought to be a DNA-binding transcriptional repressor (By similarity). However, later work showed that the original sequence was a chimera and that the DNA-binding activity was derived from the incorrect N-terminal sequence (By similarity). {ECO:0000250|UniProtKB:P16383}. reclassified-function Q7TSV6 Got1l1 Mus musculus (Mouse) 10090 Aspartate aminotransferase, cytoplasmic 2 (EC 2.6.1.1) (Glutamate oxaloacetate transaminase 1-like protein 1) (Transaminase A-like protein 1) Was reported to exhibit Asp racemase activity (PubMed:20133766). However, various reports do not confirmed this activity (PubMed:25287256, PubMed:25646960). {ECO:0000269|PubMed:20133766, ECO:0000269|PubMed:25287256, ECO:0000269|PubMed:25646960}.; reclassified-function P35412 Gpr12 Mus musculus (Mouse) 10090 G protein-coupled receptor 12 (GPCR01) Was originally thought to be a receptor for sphingosine 1-phosphate. {ECO:0000305|PubMed:12574419}. reclassified-function Q6YNI2 Gpr6 Mus musculus (Mouse) 10090 G protein-coupled receptor 6 (Sphingosine 1-phosphate receptor GPR6) Was originally (PubMed:14592418) thought to be a receptor for sphingosine 1-phosphate. It has been demonstrated that it is not the case in human. {ECO:0000305|PubMed:14592418}. reclassified-function P11352 Gpx1 Mus musculus (Mouse) 10090 Glutathione peroxidase 1 (GPx-1) (GSHPx-1) (EC 1.11.1.9) (Cellular glutathione peroxidase) (Phospholipid-hydroperoxide glutathione peroxidase GPX1) (EC 1.11.1.12) (Selenium-dependent glutathione peroxidase 1) PubMed:2771650 sequence was originally thought to originate from human. {ECO:0000305}. reclassified-function Q61625 Grid2 Mus musculus (Mouse) 10090 Glutamate receptor ionotropic, delta-2 (GluD2) (GluR delta-2 subunit) The ligand-gated cation channel activity was previously disputed due to a lack of evidence for direct ligand-gated ion channel activity (PubMed:39052831). However, structural studies have shown an asymmetric opening of the ion channel upon D-serine binding, and this would explain the lack of activity in the absence of D-serine (By similarity). {ECO:0000250|UniProtKB:O43424, ECO:0000269|PubMed:39052831}. reclassified-function Q9NYQ2 Hao2 Mus musculus (Mouse) 10090 2-Hydroxyacid oxidase 2 (HAOX2) (EC 1.1.3.15) ((S)-2-hydroxy-acid oxidase, peroxisomal) (Medium chain alpha-hydroxy acid oxidase) (Medium-chain L-2-hydroxy acid oxidase) Was originally thought to originate from human. {ECO:0000305|PubMed:10777549}. reclassified-function Q9Z2V5 Hdac6 Mus musculus (Mouse) 10090 Protein deacetylase HDAC6 (EC 3.5.1.-) (Tubulin-lysine deacetylase HDAC6) (EC 3.5.1.-) (mHDA2) Was originally thought to be a histone deacetylase (PubMed:9891014). However, subsequent work has shown that it is predominantly cytoplasmic and deacetylates a range of non-histone substrates (PubMed:12606581, PubMed:19893491, PubMed:26746851, PubMed:27737934). {ECO:0000269|PubMed:12606581, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:26746851, ECO:0000269|PubMed:27737934, ECO:0000269|PubMed:9891014}. reclassified-function P70349 Hint1 Mus musculus (Mouse) 10090 Adenosine 5'-monophosphoramidase HINT1 (EC 3.9.1.-) (Desumoylating isopeptidase HINT1) (EC 3.4.22.-) (Histidine triad nucleotide-binding protein 1) (Protein kinase C inhibitor 1) (Protein kinase C-interacting protein 1) (PKCI-1) Was originally thought to be a protein kinase C inhibitor and to bind zinc in solution. Both seem to be incorrect. {ECO:0000305}. reclassified-function Q8R1M0 Hmces Mus musculus (Mouse) 10090 Abasic site processing protein HMCES (EC 4.-.-.-) (Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein) (ES cell-specific 5hmC-binding protein) (Peptidase HMCES) (EC 3.4.-.-) (SRAP domain-containing protein 1) Was initially reported to specifically bind 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells (PubMed:23434322). It was later suggested to act as an endonuclease that specifically cleaves 5hmC-containing DNA (PubMed:29020633). However, recent studies question this activity: no alterations in global 5hmC levels are observed in bone marrow cells from knockout mice (PubMed:31806351). {ECO:0000269|PubMed:23434322, ECO:0000269|PubMed:29020633, ECO:0000269|PubMed:31806351}. reclassified-function E9Q3D4 Hsd17b14 Mus musculus (Mouse) 10090 L-fucose dehydrogenase (EC 1.1.1.122) (Hydroxysteroid 17-beta dehydrogenase 14) Was reported as a 17-beta-hydroxysteroid dehydrogenase that catalyzes estradiol and testosterone oxidation in the C17-hydroxyl group to form estrone and androstenedione, respectively (in vitro). However, HSD17B14 is very inefficient in oxidizing steroids, testosterone, suggesting that steroids cannot be physiological substrates for HSD17B14. {ECO:0000250|UniProtKB:Q9BPX1}. reclassified-function Q9D103 Ifitm1 Mus musculus (Mouse) 10090 Interferon-induced transmembrane protein 1 (Dispanin subfamily A member 2a) (DSPA2a) (Fragilis protein 2) (Mouse ifitm-like protein 2) (Mil-2) It has been previously shown that mediates migration of early primordial germ cells (PGCs) (PubMed:16326387). But according to PubMed:16326387, have no detectable effects on development of the germ line or on the generation of live young, hence, is not essential for PGC migration. {ECO:0000305|PubMed:16326387}. reclassified-function Q9CQW9 Ifitm3 Mus musculus (Mouse) 10090 Interferon-induced transmembrane protein 3 (Dispanin subfamily A member 2b) (DSPA2b) (Fragilis protein) (Interferon-inducible protein 15) (Mouse ifitm-like protein 1) (Mil-1) It has been previously shown that mediates migration of early primordial germ cells (PGCs) (PubMed:16326387). But according to PubMed:16326387, have no detectable effects on development of the germ line or on the generation of live young, hence, is not essential for PGC migration. {ECO:0000305|PubMed:16326387}. reclassified-function P19182 Ifrd1 Mus musculus (Mouse) 10090 Interferon-related developmental regulator 1 (Nerve growth factor-inducible protein PC4) (TPA-induced sequence 7) (TIS7 protein) Was originally thought to be interferon beta-2. {ECO:0000305|PubMed:6179042}. reclassified-function Q9D6H2 Ift25 Mus musculus (Mouse) 10090 Intraflagellar transport protein 25 homolog (Heat shock protein beta-11) (Hspb11) (Placental protein 25) (PP25) Was initially classified as a member of the small heat shock family protein. However, it was later shown that it is not the case (PubMed:22595669). {ECO:0000305|PubMed:22595669}. reclassified-function O55222 Ilk Mus musculus (Mouse) 10090 Scaffold protein ILK (ILK-1) (ILK-2) (Inactive integrin-linked kinase) (p59ILK) Was originally thought to act as a serine/threonine-protein kinase. Now thought to be a pseudokinase which does not have kinase activity and which functions solely as a scaffold protein. {ECO:0000250|UniProtKB:Q13418}. reclassified-function P40936 Inmt Mus musculus (Mouse) 10090 Indolethylamine N-methyltransferase (Indolamine N-methyltransferase) (EC 2.1.1.49) (EC 2.1.1.96) (Aromatic alkylamine N-methyltransferase) (Amine N-methyltransferase) (Arylamine N-methyltransferase) (Thioether S-methyltransferase) (TEMT) Was originally thought to be a thioether S-methyltransferase but appears to be the ortholog of human INMT. {ECO:0000305|PubMed:7819283}. reclassified-function Q9ERI5 Jmjd6 Mus musculus (Mouse) 10090 Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR) Was initially thought to constitute the phosphatidylserine receptor, a receptor that mediates recognition of phosphatidylserine, a specific marker only present at the surface of apoptotic cells. Phosphatidylserine receptor probably participates in apoptotic cell phagocytosis. This protein was identified using phage display expressing mAb 217, an antibody that specifically recognizes phosphatidylserine receptor. However, its nuclear localization and the fact that mAb 217 antibody still recognizes the phosphatidylserine receptor in mice lacking Jmjd6, strongly suggest that it does not constitute the receptor for phosphatidylserine and is not involved in apoptotic cell removal. {ECO:0000305}. reclassified-function Q8BGV7 Kctd13 Mus musculus (Mouse) 10090 BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1 (BTB/POZ domain-containing protein KCTD13) (Polymerase delta-interacting protein 1) Down-regulation of Kctd13 was initially reported to cause macrocephaly due to increased proliferation (PubMed:22596160). However, it was later shown that deletion of Kctd13 does not cause any change in brain size, embryonic cell proliferation, neurogenesis, or cortical layering/migration (PubMed:29088697). Experimental conditions used may explain discrepancies. A possible explanation being that shRNAs used in the first study, may have affected off-targets. {ECO:0000269|PubMed:22596160, ECO:0000269|PubMed:29088697}. reclassified-function Q9CQX8 Kgd4 Mus musculus (Mouse) 10090 Alpha-ketoglutarate dehydrogenase component 4 (Alpha-ketoglutarate dehydrogenase subunit 4) Was originally identified in the small subunit (28S) of mitochondrial ribosomes that were purified on sucrose gradients (By similarity). This observation has been challenged by experiments showing KGD4 copurification with the oxoglutarate dehydrogenase complex (OGDHC), also called alpha-ketoglutarate dehydrogenase complex (KGDH). Both mitochondrial ribosome 28S subunit and OGDC have a similar size and OGDC is highly abundant, therefore OGDC has been found to contaminate ribosomal preparations performed by sequential centrifugation steps (PubMed:25165143). In addition, KGD4 could not be located in the structure of the human mitochondrial ribosome, supporting the hypothesis that it is not a mitoribosomal protein (By similarity). {ECO:0000250|UniProtKB:P82908, ECO:0000250|UniProtKB:P82909, ECO:0000269|PubMed:25165143}. reclassified-function P16045 Lgals1 Mus musculus (Mouse) 10090 Galectin-1 (Gal-1) (14 kDa lectin) (Beta-galactoside-binding lectin L-14-I) (Galaptin) (Lactose-binding lectin 1) (Lectin galactoside-binding soluble 1) (S-Lac lectin 1) Was originally thought to originate from human. {ECO:0000305|PubMed:3020551}. reclassified-function Q64327 Mea1 Mus musculus (Mouse) 10090 Male-enhanced antigen 1 (MEA-1) Was originally thought to be the H-Y antigen. {ECO:0000305}.; reclassified-function P51180 Mip Mus musculus (Mouse) 10090 Lens fiber major intrinsic protein (Aquaporin-0) (MIP26) (MP26) Ref.2 sequence was originally thought to originate from Human. {ECO:0000305}. reclassified-function Q5RKZ7 Mocs1 Mus musculus (Mouse) 10090 Molybdenum cofactor biosynthesis protein 1 [Includes: GTP 3',8-cyclase (EC 4.1.99.22) (MOCS1A) (Molybdenum cofactor biosynthesis protein A); Cyclic pyranopterin monophosphate synthase (EC 4.6.1.17) (MOCS1B) (Molybdenum cofactor biosynthesis protein C)] The C-terminus of Mocs1a was previously believed to be thiocarboxylated, but it is now known not to be the case. {ECO:0000250|UniProtKB:Q9NZB8}. reclassified-function A1L314 Mpeg1 Mus musculus (Mouse) 10090 Macrophage-expressed gene 1 protein (Macrophage gene 1 protein) (Mpg-1) (Perforin-2) (P-2) (PFN2) (mPFN2) (Protein MPS1) [Cleaved into: Macrophage-expressed gene 1 protein, processed form] Was initially thought to facilitate killing of intravacuolar bacteria by inserting into the bacterial surface to form pores, thereby breaching the surface of phagocytosed bacteria (PubMed:30249808). These results were however not replicated in a later study (PubMed:35471730). {ECO:0000269|PubMed:30249808, ECO:0000269|PubMed:35471730}. reclassified-function P19258 Mpv17 Mus musculus (Mouse) 10090 Mitochondrial inner membrane protein Mpv17 (Protein Mpv17) (Mpv-17) Was initially thought to be a peroxisomal protein (PubMed:7957077). However, it was later shown in human that it is a mitochondrial protein (PubMed:16582907, PubMed:16582910). {ECO:0000305|PubMed:7957077}. reclassified-function Q80WJ7 Mtdh Mus musculus (Mouse) 10090 Protein LYRIC (3D3/LYRIC) (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein) Was originally thought to be a type II membrane protein but this is inconsistent with the results of multiple phosphorylation studies because this topology would locate the phosphorylation sites in the lumen or extracellularly rather than in the cytoplasm. {ECO:0000305|PubMed:15093543}. reclassified-function Q99JF5 Mvd Mus musculus (Mouse) 10090 Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Mevalonate (diphospho)decarboxylase) (MDDase) (Mevalonate pyrophosphate decarboxylase) Was originally thought to be located in the peroxisome (By similarity). However, was later shown to be cytosolic (PubMed:12736493). {ECO:0000250|UniProtKB:P53602, ECO:0000269|PubMed:12736493}. reclassified-function Q2Q5T5 Mymx Mus musculus (Mouse) 10090 Protein myomixer (Embryonic stem cell- and germ cell-specific protein) (ESGP) (Microprotein inducer of fusion) (Protein minion) (Protein myomerger) Was initially reported to be specifically expressed in embryonic stem cells and germ cells (PubMed:16331322). However, it was later shown by different groups that it is specifically expressed in myoblasts where it promotes myoblast fusion (PubMed:28386024, PubMed:28569745, PubMed:28569755). {ECO:0000269|PubMed:16331322, ECO:0000269|PubMed:28386024, ECO:0000269|PubMed:28569745, ECO:0000269|PubMed:28569755}. reclassified-function P21271 Myo5b Mus musculus (Mouse) 10090 Unconventional myosin-Vb Was originally thought to be a glutamate decarboxylase (GAD). {ECO:0000305|PubMed:2236059}. reclassified-function E0CYC6 Nat8b-ps Mus musculus (Mouse) 10090 N-acetyltransferase 8B (EC 2.3.1.-) (Acetyltransferase 1) (ATase1) (Camello-like protein 2) (Protein-lysine N6-acetyltransferase 8B) Was reported as a possible pseudogene. However an antibody which recognizes both Nat8 and Nat8b detects a product of approximately 27 kDa in brain extracts, which provides some evidence for existence of this protein (PubMed:22267734). {ECO:0000305|PubMed:22267734}. reclassified-function Q8K203 Neil3 Mus musculus (Mouse) 10090 Endonuclease 8-like 3 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase FPG2) (DNA glycosylase/AP lyase Neil3) (Endonuclease VIII-like 3) (Nei-like protein 3) Was originally thought to be inactive as a glycosylase, but recent reports demonstrate that cleavage of the initiator methionine is essential for catalytic activity. {ECO:0000269|PubMed:20185759, ECO:0000269|PubMed:22569481}. reclassified-function O35710 Noct Mus musculus (Mouse) 10090 Nocturnin (EC 3.1.3.108) (Carbon catabolite repression 4-like protein) Was initially shown to have low deadenylase activity that was lost when the metal-binding Glu was mutated (PubMed:17400819). Later studies showed that the purified protein lacked deadenylase activity (PubMed:29860338). Was subsequently shown to act as a phosphatase (By similarity). {ECO:0000250|UniProtKB:Q9UK39, ECO:0000269|PubMed:17400819, ECO:0000269|PubMed:29860338}. reclassified-function Q8R116 Notum Mus musculus (Mouse) 10090 Palmitoleoyl-protein carboxylesterase NOTUM (EC 3.1.1.98) The molecular function of NOTUM has remained unclear for many years. It was initially thought to hydrolyze glycosaminoglycan (GAG) chains of glypicans, thereby affecting glypicans ability to interact with Wnt ligands. It was later reported to trigger glypican shedding, by mediating cleavage of their GPI-anchor (PubMed:17967162). However, while NOTUM specifically inhibit the Wnt signaling pathway, more pleiotropic effects would be expected from an enzyme affecting glypicans. It was finally shown that it requires glypicans to suppress Wnt signaling, but does not cleave their GPI-anchor. It acts by mediating depalmitoleoylation of WNT proteins, impairing WNT binding to frizzled receptors. {ECO:0000269|PubMed:17967162, ECO:0000305}. reclassified-function Q61212 Npy6r Mus musculus (Mouse) 10090 Neuropeptide Y receptor type 6 (NPY6-R) (Pancreatic polypeptide receptor 2) (PP2) Was originally called NPY5-R. {ECO:0000305}. reclassified-function Q8BMT4 Nrros Mus musculus (Mouse) 10090 Transforming growth factor beta activator LRRC33 (Leucine-rich repeat-containing protein 33) (Negative regulator of reactive oxygen species) Was initially thought to act as a negative regulator of reactive oxygen species (ROS) that limits ROS production by phagocytes during inflammatory response, thereby playing a role during host defense (PubMed:24739962). However, these results were based on indirect evidences and could not be confirmed by another group (PubMed:29909984). It was later shown to act as a key regulator of transforming growth factor beta-1 (TGFB1) (PubMed:29909984). {ECO:0000269|PubMed:24739962, ECO:0000269|PubMed:29909984}. reclassified-function Q9EQQ9 Oga Mus musculus (Mouse) 10090 Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Bifunctional protein NCOAT) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (N-acetyl-beta-glucosaminidase) Was initially identified as a bi-functional protein that has an N-terminal domain with O-GlcNAcase activity and a C-terminal domain with histone acetyltransferase activity (PubMed:16356930). The histone acetyltransferase activity was detected only when the protein was expressed in mammalian cells, but not when expressed in bacterial cells, suggesting that the histone acetyltransferase activity might be due to the presence of a contaminant. Characterization of the human protein shows that this protein does not bind acetyl-CoA and therefore cannot have acetyltransferase activity. {ECO:0000305}. reclassified-function P27773 Pdia3 Mus musculus (Mouse) 10090 Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60) Was originally thought to be a phosphatidylinositol 4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha). {ECO:0000305|PubMed:2033248}. reclassified-function Q9QZ09 Phtf1 Mus musculus (Mouse) 10090 Protein PHTF1 The PHTF domain was initially defined as an atypical homeodomain, suggesting that this protein could act as a transcription regulator (By similarity). However, the protein is not found in the nucleus and mainly localizes in the endoplasmic reticulum membrane, suggesting that it does not act as a transcription factor (By similarity). {ECO:0000250|UniProtKB:F1M8G0, ECO:0000250|UniProtKB:Q9UMS5}. reclassified-function Q9D1G2 Pmvk Mus musculus (Mouse) 10090 Phosphomevalonate kinase (PMKase) (EC 2.7.4.2) Was originally thought to be located in the peroxisome. However, was later shown to be cytosolic. {ECO:0000250|UniProtKB:Q15126}. reclassified-function Q5BKQ4 Pnliprp1 Mus musculus (Mouse) 10090 Inactive pancreatic lipase-related protein 1 (PL-RP1) Was originally thought to be the pancreatic lipase, but has been shown to have very low or undetectable lipase activity in vitro. {ECO:0000305}. reclassified-function Q9JJJ7 Porcn Mus musculus (Mouse) 10090 Protein-serine O-palmitoleoyltransferase porcupine (mPORC) (EC 2.3.1.250) Was initially thought to mediate palmitoylation of Wnt proteins. It was later shown that instead it acts as a serine O-palmitoleoyltransferase that mediates the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins (PubMed:17141155, PubMed:24798332). {ECO:0000269|PubMed:17141155, ECO:0000269|PubMed:24798332}. reclassified-function P04768 Prl2c3 Mus musculus (Mouse) 10090 Prolactin-2C3 (Mitogen-regulated protein 2) (Mitogen-regulated protein 3) (Prolactin-2C4) (Proliferin-2) (Proliferin-3) Prl2c3 and Prl2c4 have previously been regarded as different proteins, but they seem to be products of the same gene. {ECO:0000305}. reclassified-function Q3U3W5 Prmt9 Mus musculus (Mouse) 10090 Protein arginine N-methyltransferase 9 (Protein arginine N-methyltransferase 10) (EC 2.1.1.320) This protein should not be confused with Fbxo11 (AC Q7TPD1) that was initially erroneously named Prmt9. {ECO:0000305}. reclassified-function Q812A5 Prr5 Mus musculus (Mouse) 10090 Proline-rich protein 5 (Protein observed with Rictor-1) (Protor-1) Was originally thought to be the sequence of Arhgap8 but is actually the sequence of Prr5. {ECO:0000305, ECO:0000305|PubMed:12559566}. reclassified-function P32240 Ptger4 Mus musculus (Mouse) 10090 Prostaglandin E2 receptor EP4 subtype (PGE receptor EP4 subtype) (PGE2 receptor EP4 subtype) (Prostanoid EP4 receptor) Was originally designated as the EP2 subtype. {ECO:0000305}. reclassified-function Q9CYK2 Qpct Mus musculus (Mouse) 10090 Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (PubMed:21671571). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000269|PubMed:21671571}. reclassified-function Q8BH73 Qpctl Mus musculus (Mouse) 10090 Glutaminyl-peptide cyclotransferase-like protein (EC 2.3.2.5) (Golgi-resident glutaminyl-peptide cyclotransferase) (isoQC) (gQC) It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (By similarity). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). {ECO:0000250|UniProtKB:B7QK46, ECO:0000250|UniProtKB:Q16769}. reclassified-function Q6GYP7 Ralgapa1 Mus musculus (Mouse) 10090 Ral GTPase-activating protein subunit alpha-1 (GAP-related-interacting partner to E12) (GRIPE) (GTPase-activating RapGAP domain-like 1) (Tuberin-like protein 1) (p240) Was initially thought to act as a transcriptional regulator via its interaction with TCF3/E12. {ECO:0000305|PubMed:12200424}. reclassified-function E9Q555 Rnf213 Mus musculus (Mouse) 10090 E3 ubiquitin-protein ligase RNF213 (EC 2.3.2.27) (EC 3.6.4.-) (E3 ubiquitin-lipopolysaccharide ligase RNF213) (EC 2.3.2.-) (Mysterin) (RING finger protein 213) The stoichiometry is unclear: was initially thought to form homohexamers (By similarity). However, the electron microscopy structure showed that it is monomeric and is composed of six ATPase modules within a single polypeptide chain (PubMed:32573437). {ECO:0000250|UniProtKB:Q63HN8, ECO:0000269|PubMed:32573437}. reclassified-function P97353 Sec1 Mus musculus (Mouse) 10090 Galactoside 2-alpha-L-fucosyltransferase Sec1 (EC 2.4.1.-) (Alpha(1,2)FT 3) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 3) (Secretory blood group protein 1) Was originally thought to be Fut2. {ECO:0000305}. reclassified-function Q91WC0 Setd3 Mus musculus (Mouse) 10090 Actin-histidine N-methyltransferase (EC 2.1.1.85) (Endothelial differentiation inhibitory protein D10) (Protein-L-histidine N-tele-methyltransferase) (SET domain-containing protein 3) Was initially reported to have histone methyltransferase activity and methylate 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me) (PubMed:21832073). However, this conclusion was based on mass spectrometry data wherin mass shifts were inconsistent with a bona fide methylation event and the histone methyltransferase activity could not be confirmed (PubMed:30626964). {ECO:0000269|PubMed:21832073, ECO:0000269|PubMed:30626964}. reclassified-function Q62420 Sh3gl2 Mus musculus (Mouse) 10090 Endophilin-A1 (Endophilin-1) (SH3 domain protein 2A) (SH3 domain-containing GRB2-like protein 2) (SH3p4) Was originally thought to have lysophosphatidic acid acyltransferase activity, but has since been experimentally shown not to have this activity. {ECO:0000305|PubMed:11978849}. reclassified-function Q9JK48 Sh3glb1 Mus musculus (Mouse) 10090 Endophilin-B1 (SH3 domain-containing GRB2-like protein B1) Was originally thought to have lysophosphatidic acid acyltransferase activity, but by homology with SH3GL2/endophilin A1 is unlikely to have this activity. {ECO:0000305|PubMed:12456676}. reclassified-function P57787 Slc16a3 Mus musculus (Mouse) 10090 Monocarboxylate transporter 4 (MCT 4) (Solute carrier family 16 member 3) Was initially thought to be considered to be a low affinity lactate transporter with negligible affinity for pyruvate (By similarity). However, it was later shown that SLC16A3 is a high affinity lactate transporter with physiologically relevant affinity for pyruvate (By similarity). {ECO:0000250|UniProtKB:O15427}. reclassified-function Q9DAM5 Slc25a19 Mus musculus (Mouse) 10090 Mitochondrial thiamine pyrophosphate carrier (Solute carrier family 25 member 19) Previously identified as the mitochondrial deoxyribonucleotide carrier. However other experiments later demonstrated that SLC25A19 is a thiamine diphosphate transporter and not a mitochondrial deoxyribonucleotide carrier. {ECO:0000250|UniProtKB:Q9HC21}. reclassified-function Q8BL03 Slc25a29 Mus musculus (Mouse) 10090 Mitochondrial basic amino acids transporter (Carnitine/acylcarnitine translocase-like) (CACT-like) (Mitochondrial carnitine/acylcarnitine carrier protein CACL) (Mitochondrial ornithine transporter 3) (Solute carrier family 25 member 29) Was initially proposed to transport palmitoylcarnitine, based on complementation experiments in yeast mutants lacking CRC1 and CIT2 and release of radiolabeled carnitine from mitochondria incubated with radiolabeled palmitoylcarnithine (PubMed:12882971). Later experiments done primarily with human indicate the protein functions instead as transporter of basic amino acids (By similarity). {ECO:0000250|UniProtKB:Q8N8R3, ECO:0000269|PubMed:12882971}. reclassified-function P48962 Slc25a4 Mus musculus (Mouse) 10090 ADP/ATP translocase 1 (ADP,ATP carrier protein 1) (ADP,ATP carrier protein, heart/skeletal muscle isoform T1) (Adenine nucleotide translocator 1) (ANT 1) (Solute carrier family 25 member 4) Was reported as a homodimer (PubMed:11809823). However, 3D structure data show that it forms a monomer (By similarity). {ECO:0000250|UniProtKB:G2QNH0, ECO:0000250|UniProtKB:P02722, ECO:0000269|PubMed:11809823}.; reclassified-function Q8VCX2 Slc35h1 Mus musculus (Mouse) 10090 Solute carrier family 35 member H1 (Ovarian cancer-overexpressed gene 1 protein) (Solute carrier family 35 member C2) SLC35H1, a homolog of the GDP-fucose transporter SLC35C1, was initially predicted to mediate GDP-fucose transport. A study indicates that SLC35H1 promotes Notch1 fucosylation and is essential for optimal Notch signaling in cultured mammalian cells (By similarity). However, Slc35h1 knockout mice are viable and fertile, showing no signs of impaired Notch signaling during skeletal or T cell development (PubMed:38270391). Additionally, deleting SLC35H1 in HEK293T cells does not affect Golgi or ER O-fucosylation, arguing against a primary role for SLC35H1 as a GDP-fucose transporter (By similarity). {ECO:0000250|UniProtKB:Q9NQQ7, ECO:0000269|PubMed:38270391}. reclassified-function G3X943 Slc39a2 Mus musculus (Mouse) 10090 Zinc transporter ZIP2 (Solute carrier family 39 member 2) (Zrt- and Irt-like protein 2) (ZIP-2) (hZIP2) It was previously proposed that SLC39A2 operates as a Zn2(+)/HCO3(-) symport mechanism (By similarity). However in more recent studies, SLC39A2-mediated transport is independent of both HCO3(-) and H(+)-driving forces, but modulated by extracellular pH and voltage (By similarity). {ECO:0000250|UniProtKB:Q9NP94}. reclassified-function Q0P5V9 Slc45a4 Mus musculus (Mouse) 10090 Polyamine-transporter SLC45A4 (Solute carrier family 45 member 4) Was initially characterized as a proton-associated sucrose transporter in vitro (PubMed:25164149). However, the sucrose transporter activity could not be confirmed by a subsequent article, which showed that it acts as a polyamine-transporter (PubMed:40836097). {ECO:0000269|PubMed:25164149, ECO:0000269|PubMed:40836097}. reclassified-function Q78KK3 Slc67a1 Mus musculus (Mouse) 10090 Solute carrier family 22 member 18 (Imprinted multi-membrane-spanning polyspecific transporter-related protein 1) (Multi-membrane-spanning polyspecific transporter) (Organic cation transporter-like protein 2) (ORCTL-2) Was initially classified as a member of the SLC22 family. However, an evolutionary and phylogenetic analysis suggested that SLC22A18 is unique and that it is most distantly related to SLC22 family members. {ECO:0000250|UniProtKB:Q96BI1}. reclassified-function Q925Q3 Slc8b1 Mus musculus (Mouse) 10090 Mitochondrial sodium/calcium exchanger protein (Na(+)/K(+)/Ca(2+)-exchange protein 6) (Sodium/calcium exchanger protein, mitochondrial) (Sodium/potassium/calcium exchanger 6) (Solute carrier family 24 member 6) (Solute carrier family 8 member B1) Isoform 1 was reported to not have cation exchanger activity (PubMed:12080145). However, such result is unclear. {ECO:0000305|PubMed:12080145}.; reclassified-function Q9CW03 Smc3 Mus musculus (Mouse) 10090 Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) (Basement membrane-associated chondroitin proteoglycan) (Bamacan) (Chondroitin sulfate proteoglycan 6) (Chromosome segregation protein SmcD) (Mad member-interacting protein 1) Was originally isolated as a proteoglycan protein (explaining its name). Although not excluded, such secreted function is not clear. {ECO:0000305}. reclassified-function P15265 Smcp Mus musculus (Mouse) 10090 Sperm mitochondrial-associated cysteine-rich protein Was originally (PubMed:2303168, PubMed:1418626) thought to be a selenoprotein and was known as sperm mitochondrial capsule selenoprotein. {ECO:0000305}. reclassified-function Q8R5A0 Smyd2 Mus musculus (Mouse) 10090 N-lysine methyltransferase SMYD2 (EC 2.1.1.-) (Histone methyltransferase SMYD2) (EC 2.1.1.354) (SET and MYND domain-containing protein 2) The protein was previously thought to dimethylate histone 3 'Lys-36', but this is now known not to take place in vivo. {ECO:0000269|PubMed:18065756}. reclassified-function Q05AH6 Spindoc Mus musculus (Mouse) 10090 Spindlin interactor and repressor of chromatin-binding protein (SPIN1-docking protein) (SPIN-DOC) Was initially reported to inhibit the ability of SPIN1 to bind methylated histones (PubMed:29061846). However, it was later shown to play an opposite role and promote SPIN1 association with bivalent H3K4me3K9me3 mark (By similarity). {ECO:0000250|UniProtKB:Q9BUA3, ECO:0000269|PubMed:29061846}. reclassified-function Q9WUP4 Srd5a3 Mus musculus (Mouse) 10090 Polyprenal reductase (EC 1.3.1.94) (3-oxo-5-alpha-steroid 4-dehydrogenase 3) (EC 1.3.1.22) (Steroid 5-alpha-reductase 2-like) (Steroid 5-alpha-reductase 3) (S5AR 3) (SR type 3) Was initially characterized as a polyprenol reductase, mediating the conversion of polyprenol into dolichol (PubMed:20637498). However, it was later shown to catalyze an intermediate step in this pathway and reduce polyprenal (By similarity). {ECO:0000250|UniProtKB:Q9H8P0, ECO:0000269|PubMed:20637498}. reclassified-function B2RWW0 Tagap Mus musculus (Mouse) 10090 T-cell activation Rho GTPase-activating protein (T-cell activation GTPase-activating protein) Previously thought to be the same gene as Tagap1. These are distinct loci that encode proteins with identical C-termini but each with a unique N-terminus. {ECO:0000305}. reclassified-function P0CAX8 Tagap1 Mus musculus (Mouse) 10090 T-cell activation GTPase-activating protein 1 Previously thought to be the same gene as Tagap. These are distinct loci that encode proteins with identical C-termini but each with a unique N-terminus. {ECO:0000305}. reclassified-function P59528 Tas2r123 Mus musculus (Mouse) 10090 Taste receptor type 2 member 123 (T2R123) (STC9-2) (Taste receptor type 2 member 23) (T2R23) (mT2R55) This protein was previously referred to as T2R2 but is now considered to be an ortholog of rat TAS2R23. {ECO:0000305}. reclassified-function P59532 Tas2r41 Mus musculus (Mouse) 10090 Taste receptor type 2 member 41 (T2R41) (T2R12) (T2R26) This protein was previously referred to as T2R26 or T2R12 but is now considered to be the ortholog of human TAS2R41. {ECO:0000305}. reclassified-function Q6PB75 Tent4a Mus musculus (Mouse) 10090 Terminal nucleotidyltransferase 4A (DNA polymerase sigma) (Non-canonical poly(A) RNA polymerase PAPD7) (EC 2.7.7.19) (PAP-associated domain-containing protein 7) (TRAMP-like complex polyadenylate polymerase) (Terminal guanylyltransferase) (EC 2.7.7.-) Was originally thought to have DNA polymerase activity. {ECO:0000305}. reclassified-function Q68ED3 Tent4b Mus musculus (Mouse) 10090 Terminal nucleotidyltransferase 4B (Non-canonical poly(A) RNA polymerase PAPD5) (EC 2.7.7.19) (PAP-associated domain-containing protein 5) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal uridylyltransferase 3) (TUTase 3) (Topoisomerase-related function protein 4-2) (TRF4-2) Was originally thought to have DNA polymerase activity. {ECO:0000305}. reclassified-function Q8VDR7 Tgds Mus musculus (Mouse) 10090 UDP-D-glucose 4,6-dehydratase (EC 4.2.1.76) (dTDP-D-glucose 4,6-dehydratase) Was initially thought to have dTDP-D-glucose 4,6-dehydratase activity, based on its similarity with bacterial enzymes involved in the synthesis of rhamnose during bacterial cell wall formation. However, it was later shown to have UTP-glucose 4,6-dehydratase activity (PubMed:40836090). {ECO:0000269|PubMed:40836090, ECO:0000305}. reclassified-function Q99JT6 Tlcd1 Mus musculus (Mouse) 10090 TLC domain-containing protein 1 (Calfacilitin) Was originally proposed to be a calcium channel facilitator (By similarity). However, a more recent study shows that this protein regulates membrane phospholipid homeostasis (By similarity). Therefore, any effects on calcium flux are most likely a secondary consequence of defects in membrane composition or fluidity (By similarity). {ECO:0000250|UniProtKB:F1NZP5, ECO:0000250|UniProtKB:Q96CP7}. reclassified-function Q61663 Tlx2 Mus musculus (Mouse) 10090 T-cell leukemia homeobox protein 2 (Enteric neuron homeobox protein) (Homeobox TLX-2) (Homeobox protein Hox-11L1) (Hox11L.1) (PMUR10F) Was originally thought to be the ortholog of human HOX11. {ECO:0000305|PubMed:1681546}. reclassified-function Q9DAT5 Trmu Mus musculus (Mouse) 10090 Mitochondrial tRNA-specific 2-thiouridylase 1 (EC 2.8.1.14) Was originally thought to be a 5-methylaminomethyl-2-methyltransferase involved in tRNA modification. {ECO:0000305|PubMed:14746906}. reclassified-function A4Q9E5 Ttll3 Mus musculus (Mouse) 10090 Tubulin monoglycylase TTLL3 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 3) TTLL3 and TTLL8 monoglycylase-mediated glycylation of tubulin was initially reported to play a role in ependymal motile ciliary maintenance (PubMed:23897886). However, contradictory results were later observed (PubMed:33414192). {ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:33414192}. reclassified-function A4Q9F0 Ttll7 Mus musculus (Mouse) 10090 Tubulin polyglutamylase TTLL7 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 7) (mTTLL7) Was initially though to be involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (PubMed:17499049). However, it was later shown to be involved in both steps (PubMed:19152315). {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:19152315}. reclassified-function A4Q9F1 Ttll8 Mus musculus (Mouse) 10090 Protein monoglycylase TTLL8 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 8) TTLL3 and TTLL8 monoglycylase-mediated glycylation of tubulin was initially reported to play a role in ependymal motile ciliary maintenance (PubMed:23897886). However, contradictory results were later observed (PubMed:33414192). {ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:33414192}. reclassified-function P46686 Tulp2 Mus musculus (Mouse) 10090 Tubby-related protein 2 (Protein P4-6) (Tubby-like protein 2) Was originally thought to be a phosphodiesterase on the basis of spurious sequence similarities. {ECO:0000305|PubMed:7509194}. reclassified-function Q8VE47 Uba5 Mus musculus (Mouse) 10090 Ubiquitin-like modifier-activating enzyme 5 (Ubiquitin-activating enzyme 5) (UFM1-activating enzyme) Was initially reported to mediate activation of SUMO2 in addition to UFM1 (By similarity). However, it was later shown that it is specific for UFM1 (PubMed:21304510). {ECO:0000250|UniProtKB:Q9GZZ9, ECO:0000269|PubMed:21304510}. reclassified-function P70406 Ucp2 Mus musculus (Mouse) 10090 Dicarboxylate carrier UCP2 (Mitochondrial uncoupling protein 2) (UCP 2) (Solute carrier family 25 member 8) (UCPH) The role of UCP2/SLC25A8 in mitochondrial proton conductance is a matter of debate. It was initially suggested that it mediates proton leak that increases net proton conductance in response to ROS such as reactive alkenals generated during fatty acid oxidation in mitochondria. By lowering the proton motive force, it would provide for feedback control of mitochondrial ROS metabolism limiting extensive ROS production and protecting cells against oxidative stress. This activity and its potential regulation by ubiquinones and nucleotides was disputed by later studies, which failed to reproduce the effect on proton conductance under physiological conditions. Rather than 'uncoupling' the link between electron transfer and ATP synthesis, it may couple metabolite transport to proton flux to allow for optimal ATP turnover. {ECO:0000269|PubMed:11101840, ECO:0000269|PubMed:12011051, ECO:0000269|PubMed:9133562, ECO:0000303|PubMed:33798544}. reclassified-function Q9QZ88 Vps29 Mus musculus (Mouse) 10090 Vacuolar protein sorting-associated protein 29 (Vesicle protein sorting 29) Was originally believed to be a metal-dependent phosphatase but shown to lack catalytic activity; can bind metals (Zn(2+) and Mn(2+)) with very low affinity suggesting that metal binding is not required for its function. {ECO:0000303|PubMed:15965486, ECO:0000303|PubMed:21629666}. reclassified-function Q9JHN8 Whr1 Mus musculus (Mouse) 10090 Winged helix repair factor 1 (Inactive serine/threonine-protein kinase 19) (Protein RP1) (Tandem winged helix protein formerly known as STK19) Was originally reported to be a serine/threonine-protein kinase. However, later studies have shown that the protein does not have kinase activity and is involved in transcription-coupled nucleotide excision repair. {ECO:0000250|UniProtKB:P49842}. reclassified-function P59326 Ythdf1 Mus musculus (Mouse) 10090 YTH domain-containing family protein 1 (Dermatomyositis associated with cancer putative autoantigen 1 homolog) (DACA-1 homolog) Was initially reported to act as a regulator of mRNA translation efficiency by promoting ribosome loading to m6A-containing mRNAs and by interacting with translation initiation factors eIF3 (EIF3A or EIF3B), thereby facilitating translation initiation (PubMed:30401835, PubMed:30728504, PubMed:30843071). These studies suggested that the 3 different paralogs (YTHDF1, YTHDF2 and YTHDF3) have unique functions with limited redundancy (PubMed:30401835, PubMed:30728504, PubMed:30843071). However, later studies showed that YTHDF1, YTHDF2 and YTHDF3 paralogs have redundant functions to a profound extent and directly promote degradation of m6A-containing mRNAs (PubMed:32943573). The effect on translation efficiency observed earlier is probably indirect (PubMed:32943573). {ECO:0000269|PubMed:30401835, ECO:0000269|PubMed:30728504, ECO:0000269|PubMed:30843071, ECO:0000269|PubMed:32943573}. reclassified-function Q8BYK6 Ythdf3 Mus musculus (Mouse) 10090 YTH domain-containing family protein 3 Was initially reported to act as a regulator of mRNA translation efficiency by binding to m6A-containing mRNAs (PubMed:30591559). This study suggested that the 3 different paralogs (YTHDF1, YTHDF2 and YTHDF3) have unique functions with limited redundancy (PubMed:32943573). However, later studies showed that YTHDF1, YTHDF2 and YTHDF3 paralogs have redundant functions to a profound extent and directly promote degradation of m6A-containing mRNAs (PubMed:32943573). The effect on translation efficiency observed earlier is probably indirect (PubMed:32943573). {ECO:0000269|PubMed:30591559, ECO:0000269|PubMed:32943573}. reclassified-function O70230 Znf143 Mus musculus (Mouse) 10090 Zinc finger protein 143 (Zfp-143) (Selenocysteine tRNA gene transcription-activating factor) (mStaf) Was reported to play a role in chromatin looping together with CTCF (PubMed:33397967). However, it was later shown that the antiboby against ZNF143 crossreacts with CTCF and that ZNF143 is not involved in chromatin looping (PubMed:39708803, PubMed:39708805). {ECO:0000269|PubMed:33397967, ECO:0000269|PubMed:39708803, ECO:0000269|PubMed:39708805}. reclassified-function P63946 dapA Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) 233413 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7TXX0 dapB Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) 233413 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1KM94 dapA Mycobacterium bovis (strain BCG / Pasteur 1173P2) 410289 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1KMB5 dapB Mycobacterium bovis (strain BCG / Pasteur 1173P2) 410289 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C1AFL5 dapA Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019) 561275 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C1AFN6 dapB Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019) 561275 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8ZRR3 dapA Mycobacterium leprae (strain Br4923) 561304 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9CBW4 dapA Mycobacterium leprae (strain TN) 272631 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B2HKW6 dapB Mycobacterium marinum (strain ATCC BAA-535 / M) 216594 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3PYA0 dapB Mycobacterium sp. (strain JLS) 164757 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1UEU3 dapB Mycobacterium sp. (strain KMS) 189918 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1BA69 dapB Mycobacterium sp. (strain MCS) 164756 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5U6A6 dapA Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) 419947 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5U6C6 dapB Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) 419947 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P9WLL7 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 F420H(2)-dependent biliverdin reductase (F-BVR) (EC 1.3.98.-) Was originally thought to be an FMN-dependent pyridoxine 5'-phosphate oxidase. {ECO:0000305|PubMed:16880544}. reclassified-function P9WMS9 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Arabinogalactan biosynthesis recruiting protein Rv3789 Was originally thought to be a lipid-linked sugar translocase involved in the reorientation and export of decaprenyl-phospho-arabinose (DPA) across the plasma membrane to the site of AG (arabinogalactan) and LAM (lipoarabinomannan) synthesis (PubMed:23038254). It was later shown that synthesis of DPA takes place in the periplasm and it was suggested that Rv3789 does not act as a DPA flippase but, rather, recruits AftA for arabinogalactan biosynthesis (PubMed:25906160, PubMed:26369580). {ECO:0000305|PubMed:23038254, ECO:0000305|PubMed:25906160, ECO:0000305|PubMed:26369580}. reclassified-function O06553 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 F420H(2)-dependent reductase Rv1155 (EC 1.-.-.-) Was originally thought to be an FMN-dependent pyridoxine 5'-phosphate oxidase. {ECO:0000305|PubMed:16239726}.; reclassified-function P9WL63 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Uncharacterized protein Rv2629 A fairly frequent variant (Ala-64) was originally (PubMed:17970586) suggested to be responsible for some cases of rifampicin resistance. This has since been shown not to be true (PubMed:18550732), although it is a good marker for the Beijing-W clade/SCG-2 phylogenetic group. {ECO:0000305|PubMed:17970586, ECO:0000305|PubMed:18550732}. reclassified-function P9WHY9 PPE46 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Uncharacterized PPE family protein PPE46 Was originally thought to be a dihydrofolate reductase. {ECO:0000305|Ref.2}. reclassified-function P9WIR7 apa Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Alanine and proline-rich secreted protein Apa (45 kDa glycoprotein) (45/47 kDa antigen) (Antigen MPT-32) (FAP-B) (Fibronectin attachment protein) (Immunogenic protein MPT32) Was originally thought to be involved in molybdenum transport. {ECO:0000305}. reclassified-function P9WIU5 arfA Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Peptidoglycan-binding protein ArfA (Outer membrane porin A) (Outer membrane protein A) (OmpATb) (Outer membrane protein ArfA) Was originally thought to be a porin. {ECO:0000305|PubMed:12366842}. reclassified-function P9WP25 dapA Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P9WP23 dapB Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P9WNA5 eccC5 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 ESX-5 secretion system protein EccC5 (ESX conserved component C5) (Type VII secretion system protein EccC5) (T7SS protein EccC5) Was originally thought to be the product of two separate ORFs, eccCa5 and eccCb5. {ECO:0000305|PubMed:19876390}. reclassified-function P9WJB7 espR Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Nucleoid-associated protein EspR (ESX-1 transcriptional regulatory protein EspR) Was originally thought to be secreted via the ESX-1 secretion system, but it was probably released in the medium via cell lysis. {ECO:0000305|PubMed:18685700, ECO:0000305|PubMed:22479184}. reclassified-function P9WQ55 fadD10 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Medium/long-chain-fatty-acid--[acyl-carrier-protein] ligase FadD10 (EC 6.2.1.20) (EC 6.2.1.47) (FAAL10) Was originally thought to be a fatty acyl-CoA ligase (FACL) (PubMed:19182784). However, although FadD10 has a primary sequence similar to FACLs, it is indeed a fatty acyl-AMP ligase (FAAL) that is only able to acylate an ACP (Rv0100) rather than coenzyme A (PubMed:22451903, PubMed:23625916). {ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:22451903, ECO:0000269|PubMed:23625916}. reclassified-function P9WMV3 gmhB Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase (EC 3.1.3.83) (D,D-heptose 1,7-bisphosphate phosphatase) (HBP phosphatase) Was originally proposed to be fused with GmhA. {ECO:0000305}. reclassified-function P9WIS5 kgd Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)] Was originally annotated as sucA because of sequence similarity (PubMed:12218036, PubMed:9634230). But this protein was shown not to be able to serve as the E1 component of 2-oxoglutarate dehydrogenase (ODH) (PubMed:16045627). However, it was later shown that this protein does in fact sustain ODH activity, and requires specific activation by acetyl-CoA (PubMed:21867916). {ECO:0000305|PubMed:16045627, ECO:0000305|PubMed:21867916}. reclassified-function A0A089QRB9 msl3 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Mycolipanoate synthase (EC 2.3.1.252) (Mycocerosic acid synthase-like polyketide synthase) (MAS-like PKS) (Mycolipanoic/mycolipenic acids synthase-like polyketide synthase) The previously assigned stop codon (TAA) of pks3 (Rv1180) is found to be a Tyr codon (TAC), and with this change, pks3 and pks4 become a single open reading frame designated msl3 (PubMed:12207710). Large scale proteomics studies identify protein sequence that extends N-terminal to the initially annotated start site of Rv1181, more evidence that a single protein is translated from this locus. {ECO:0000269|PubMed:12207710, ECO:0000305|PubMed:21969609, ECO:0000305|PubMed:34915127}. reclassified-function O05461 mycP1 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Mycosin-1 (EC 3.4.21.-) (MycP1 protease) Was originally thought to be proteolytically processed intracellularly. {ECO:0000305|PubMed:12366866}. reclassified-function P9WMX5 pimF Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Putative glycosyltransferases (EC 2.4.-.-) Was originally thought (PubMed:14960574) to be a mannosyltransferase involved in the biosynthesis of phosphatidylinositol mannosides (PIMs), but further in vivo and in vitro characterizations (PubMed:18585090) clearly show that inactivation of Rv1500 does not affect the expression pattern of PIMs. {ECO:0000305|PubMed:14960574, ECO:0000305|PubMed:18585090}. reclassified-function A0PQF8 dapB Mycobacterium ulcerans (strain Agy99) 362242 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A4TCJ3 dapA Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain PYR-GCK)) 350054 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4TCI6 dapB Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain PYR-GCK)) 350054 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q73VZ7 dapA Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) (Mycobacterium paratuberculosis) 262316 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q73VY3 dapB Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) (Mycobacterium paratuberculosis) 262316 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P21795 Mycolicibacterium smegmatis (Mycobacterium smegmatis) 1772 L-lactate 2-monooxygenase (LMO) (EC 1.13.12.4) (Lactate monooxygenase) This enzyme was originally referred to as 'lactate oxidase' but this acetate producing enzyme is now referred to as 'lactate monooxygenase' (LMO), and 'lactate oxidase' (LOX) refers to a related flavoenzyme that converts lactate and molecular oxygen to pyruvate and hydrogen peroxide. {ECO:0000305|PubMed:30207005}. reclassified-function A0QVR3 dapB Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) 246196 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A0R756 lerI Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) 246196 L-erythrulose-1-phosphate isomerase (EC 5.3.1.33) The substrate of the reaction was originally identified as L-erythrulose 4-phosphate (PubMed:26560079). It was then corrected to L-erythrulose 1-phosphate by the same group (PubMed:26978037). {ECO:0000269|PubMed:26560079, ECO:0000269|PubMed:26978037}. reclassified-function A0R758 lerK Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) 246196 L-erythrulose 1-kinase (EC 2.7.1.209) The product of the reaction was originally identified as L-erythrulose 4-phosphate (PubMed:26560079). It was then corrected to L-erythrulose 1-phosphate by the same group (PubMed:26978037). {ECO:0000269|PubMed:26560079, ECO:0000269|PubMed:26978037}. reclassified-function A0QSC0 mftE Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) 246196 Mycofactocin precursor peptide peptidase (EC 3.4.14.14) Was originally thought to cleave the C-terminal dipeptide from the first intermediate product formed by the action of MftC on MftA, i.e. MftA modified with a C-terminal glycyl-L-valyl-decarboxylated L-tyrosine (PubMed:28077628). However, it was later shown that the terminal product formed by the action of MftC on MftA is the true substrate of MftE, i.e. MftA modified with a C-terminal glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one (PubMed:30183269). {ECO:0000269|PubMed:28077628, ECO:0000269|PubMed:30183269}. reclassified-function A1T7N8 dapB Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii) 350058 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P38037 infA Mycoplasma sp 2108 Translation initiation factor IF-1 Was originally thought to originate from Chlamydia trachomatis. {ECO:0000305|PubMed:8226662}. reclassified-function P38015 rpmJ Mycoplasma sp 2108 Large ribosomal subunit protein bL36 (50S ribosomal protein L36) Was originally thought to originate from Chlamydia trachomatis. {ECO:0000305|PubMed:8226662}. reclassified-function P38018 rpoA Mycoplasma sp 2108 DNA-directed RNA polymerase subunit alpha (RNAP subunit alpha) (EC 2.7.7.6) (RNA polymerase subunit alpha) (Transcriptase subunit alpha) Was originally thought to originate from Chlamydia trachomatis. {ECO:0000305|PubMed:8226662}. reclassified-function Q46451 rpsK Mycoplasma sp 2108 Small ribosomal subunit protein uS11 (30S ribosomal protein S11) Was originally thought to originate from Chlamydia trachomatis. {ECO:0000305|PubMed:8226662}. reclassified-function P38017 rpsM Mycoplasma sp 2108 Small ribosomal subunit protein uS13 (30S ribosomal protein S13) Was originally thought to originate from Chlamydia trachomatis. {ECO:0000305|PubMed:8226662}. reclassified-function P47658 dnaX Mycoplasmoides genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) (Mycoplasma genitalium) 243273 DNA polymerase III subunit gamma/tau (EC 2.7.7.7) Was originally thought to be two separate ORFs named DnaX and DnaZ. {ECO:0000305|PubMed:7569993}. reclassified-function P75548 hprK Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasma pneumoniae) 272634 HPr kinase/phosphorylase (HPrK/P) (EC 2.7.11.-) (EC 2.7.4.-) (HPr kinase/phosphatase) (HPr(Ser) kinase/phosphorylase) Was originally called HPr kinase/phosphatase (PubMed:12368461, PubMed:12589763). But P-Ser-HPr dephosphorylation was shown in several bacteria to follow a quite unique mechanism, in which Pi instead of H(2)O is used for the nucleophilic attack on the phosphoryl group. P-Ser-HPr dephosphorylation is therefore not a phosphohydrolysis but a phospho-phosphorolysis reaction, and the bifunctional enzyme was dubbed HPr kinase/phosphorylase. {ECO:0000305}. reclassified-function B3EWR1 Mytilus galloprovincialis (Mediterranean mussel) 29158 Alpha-D-galactose-binding lectin (Galactose-binding lectin) (Lectin) (MytiLec) (MytiLec-1) (R-type lectin) Was originally thought to be a monomer in solution on the basis of gel filtration. {ECO:0000269|PubMed:23093409}. reclassified-function Q1CZV9 dapB Myxococcus xanthus (strain DK1622) 246197 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P12393 SPI-1 Myxoma virus (strain Lausanne) (MYXV) 31530 Serine proteinase inhibitor 1 (Serp-1) (Serpin-1) Was originally (PubMed:3023828, PubMed:3021526) thought to originate from a plasmid rabbit DNA. The original sample was contaminated and the gene is derived from myxoma virus. {ECO:0000305}. reclassified-function P14556 Naja pallida (Red spitting cobra) 8658 Basic phospholipase A2 nigexine (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) The venom of this snake was originally thought to be that of N.nigricollis. {ECO:0000305}. reclassified-function P01426 Naja pallida (Red spitting cobra) 8658 Short neurotoxin 1 (Neurotoxin alpha) (Toxin alpha) The venom of this snake was originally thought to be that of N.nigricollis. {ECO:0000305}. reclassified-function P01468 Naja pallida (Red spitting cobra) 8658 Cytotoxin 1 (CTX-1) (Cardiotoxin gamma) The venom of this snake was originally thought to be that of N.nigricollis while it is really from N.pallida. {ECO:0000305}. reclassified-function B2A3B2 dapA Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF) 457570 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3ISQ0 dapA Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis) 348780 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3ISP9 dapB Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis) 348780 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P14929 ftsY Neisseria gonorrhoeae 485 Signal recognition particle receptor FtsY (SRP receptor) (EC 3.6.5.4) Was originally thought to activate the pilin promoter. {ECO:0000305|PubMed:2854063}. reclassified-function P14930 msrAB Neisseria gonorrhoeae 485 Peptide methionine sulfoxide reductase MsrA/MsrB [Includes: Thioredoxin; Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase); Peptide methionine sulfoxide reductase MsrB (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase)] Was originally thought to play a role along with PilA in the transcription regulation of PilE. {ECO:0000305|PubMed:2854063}. reclassified-function P31033 ngoMIVM Neisseria gonorrhoeae 485 Type II methyltransferase M.NgoMIV (M.NgoMIV) (EC 2.1.1.37) (Cytosine-specific methyltransferase NgoMIV) (DNA methylase M.NgoMI) (M.NgoMI) (Modification methylase NgoMIV) Was originally known as M.NgoMI. {ECO:0000305|PubMed:1321116}. reclassified-function P31032 ngoMIVR Neisseria gonorrhoeae 485 Type II restriction enzyme NgoMIV (R.NgoMIV) (EC 3.1.21.4) (Endonuclease NgoMIV) (Restriction enzyme NgoMI) (NgoMI) (Type-2 restriction enzyme NgoMIV) Was originally known as R.NgoMI. {ECO:0000305|PubMed:1321116}. reclassified-function Q5F849 dapA Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) 242231 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5F5Y7 dapB Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) 242231 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B4RR35 dapB Neisseria gonorrhoeae (strain NCCP11945) 521006 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9JUU9 dapA Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491) 122587 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9JX48 dapB Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491) 122587 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9JXW7 crgA Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58) 122586 HTH-type transcriptional regulator CrgA (Contact-regulated gene A) In strain 8013 (AC Q9JPU9), CrgA was reported to control the expression of pili and capsule genes. However, Ieva et al. reported that CrgA and MBL have no effect on transcription of pilus and capsule genes in strain MC58 (PubMed:15866928). {ECO:0000269|PubMed:15866928, ECO:0000305}. reclassified-function Q9JZR4 dapA Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58) 122586 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9K1F1 dapB Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58) 122586 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O30391 ftsY Neisseria meningitidis serogroup C 135720 Signal recognition particle receptor FtsY (SRP receptor) (EC 3.6.5.4) Was originally thought to activate the pilin promoter. {ECO:0000305|PubMed:9434748}. reclassified-function A9M4C8 dapA Neisseria meningitidis serogroup C (strain 053442) 374833 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A9M3H7 dapB Neisseria meningitidis serogroup C (strain 053442) 374833 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9JPU9 crgA Neisseria meningitidis serogroup C (strain 8013) 604162 HTH-type transcriptional regulator CrgA (Contact-regulated gene A) In strain MC58 (AC Q9JXW7), CrgA was reported to control the expression of its upstream gene, mdaB, but not the expression of the pili and capsule genes. {ECO:0000305}. reclassified-function A1KTJ9 dapA Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18) 272831 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1KRN3 dapB Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18) 272831 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P38678 cot-2 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) 367110 Glucan synthesis regulatory protein (Colonial temperature-sensitive protein 2) Was originally thought to be a glucan synthase. {ECO:0000305|PubMed:7937796}. reclassified-function Q1K8B6 gh61-4 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) 367110 Lytic polysaccharide monooxygenase NCU01050 (LPMO NCU01050) (EC 1.14.99.56) (Endoglucanase II) (LPMO9D) (NcLPMO9D) (NcPMO-2) (NcPMO2) (Polysaccharide monooxygenase 2) (PMO-2) (PMO2) (Type-2 polysaccharide monooxygenase) (Type-2 PMO) Was originally classified in the glycosyl hydrolase 61 family, but is since reclassified in the auxiliary activity 9 (AA9) protein family. {ECO:0000305|PubMed:31431506}. reclassified-function P20285 mrp-3 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) 367110 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (MRP3) (Pyruvate dehydrogenase complex component E2) (PDC-E2) (PDCE2) Was originally thought to be a ribosomal protein. {ECO:0000305|PubMed:2521217}. reclassified-function Q4H4F3 btrD Niallia circulans (Bacillus circulans) 1397 2'-N-acetylparomamine deacetylase (EC 3.5.1.112) (Butirosin biosynthesis protein D) Was initially thought to function as a nucleotidyltransferase (PubMed:15701005). But it was later shown that it is a deacetylase (PubMed:17226887). {ECO:0000305|PubMed:15701005, ECO:0000305|PubMed:17226887}. reclassified-function Q8L1A7 pdxT Niallia circulans (Bacillus circulans) 1397 Pyridoxal 5'-phosphate synthase subunit PdxT (EC 4.3.3.6) (Pdx2) (Pyridoxal 5'-phosphate synthase glutaminase subunit) (EC 3.5.1.2) Was originally believed to be a subunit of the 2-deoxy-scyllo-inosose synthase. {ECO:0000305|PubMed:12224638}. reclassified-function O24115 THIO1 Nicotiana paniculata 62141 Defensin-like protein 1 (Gamma-thionin 1) Was initially thought (Ref.1) to be a thionin. {ECO:0000305}. reclassified-function P27484 GRP-2 Nicotiana sylvestris (Wood tobacco) (South American tobacco) 4096 Glycine-rich protein 2 Was originally thought to be a cell wall structural protein. {ECO:0000305|PubMed:1912512}. reclassified-function Q42948 DHPS1 Nicotiana tabacum (Common tobacco) 4097 4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P32026 FST Nicotiana tabacum (Common tobacco) 4097 Defensin-like protein (Flower-specific gamma-thionin) Was initially thought to be a thionin. {ECO:0000305|PubMed:1495489}. reclassified-function P62094 psaC Nicotiana tabacum (Common tobacco) 4097 Photosystem I iron-sulfur center (EC 1.97.1.12) (9 kDa polypeptide) (PSI-C) (Photosystem I subunit VII) (PsaC) Was originally thought to originate from Synechocystis PCC6803. {ECO:0000305|PubMed:1907869}. reclassified-function Q72AX2 dapA Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris) 882 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q72BM6 dapB Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris) 882 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P20418 dfx Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris) 882 Desulfoferrodoxin (Dfx) (EC 1.15.1.2) (Superoxide reductase) (SOR) Was originally thought to be a rubredoxin oxidoreductase. {ECO:0000305|PubMed:2549009}. reclassified-function P31101 hcp Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris) 882 Hydroxylamine reductase (EC 1.7.99.1) (Hybrid-cluster protein) (HCP) (Prismane protein) Was originally thought to contain a [6Fe-6S] cluster as indicated. {ECO:0000305|PubMed:1318833}. reclassified-function P24931 rbr Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris) 882 Rubrerythrin (Rr) Was originally thought to have inorganic pyrophosphatase activity. {ECO:0000305}. reclassified-function A1VCZ9 dapA Nitratidesulfovibrio vulgaris (strain DP4) (Desulfovibrio vulgaris) 391774 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1VDM6 dapB Nitratidesulfovibrio vulgaris (strain DP4) (Desulfovibrio vulgaris) 391774 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8DKU0 dapA Nitratidesulfovibrio vulgaris (strain DSM 19637 / Miyazaki F) (Desulfovibrio vulgaris) 883 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8DJT5 dapB Nitratidesulfovibrio vulgaris (strain DSM 19637 / Miyazaki F) (Desulfovibrio vulgaris) 883 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6Q2V4 dapA Nitratiruptor sp. (strain SB155-2) 387092 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6Q596 dapB Nitratiruptor sp. (strain SB155-2) 387092 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1QL43 dapA Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14) 323097 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3SW72 dapB Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255) 323098 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3J869 dapA Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107) 323261 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3J7E0 dapB Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107) 323261 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q82SD7 dapA Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298) 228410 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q82WP9 dapB Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298) 228410 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0AI27 dapA Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57) 335283 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q0AER1 dapB Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57) 335283 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2Y8S8 dapA Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71) 323848 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2YBT6 dapB Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71) 323848 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5YSW2 dapB Nocardia farcinica (strain IFM 10152) 247156 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5YTV5 rox Nocardia farcinica (strain IFM 10152) 247156 Rifampicin monooxygenase (RIFMO) (EC 1.14.13.211) Was initially characterized as an N-monooxygenase proposed to hydroxylate rifampicin at the N2' atom to produce 2'-N-hydroxyrifampicin. Later structural studies showed that RIFMO catalyzes a different reaction involving monooxygenation of position 2 of the naphthyl group, followed by linearization of the antibiotic (PubMed:29578336). {ECO:0000269|PubMed:29578336, ECO:0000305|PubMed:19942945}. reclassified-function B2IT87 dapA Nostoc punctiforme (strain ATCC 29133 / PCC 73102) 63737 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B2J0A9 dapB Nostoc punctiforme (strain ATCC 29133 / PCC 73102) 63737 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P07125 cpcE Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) 103690 Phycocyanobilin lyase subunit alpha (EC 4.-.-.-) (Phycocyanin operon protein CpcE) Was originally thought to be a linker peptide. {ECO:0000305|PubMed:3109890}. reclassified-function Q8YQY1 dapA Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) 103690 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8YU19 dapB Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) 103690 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2G8D6 dapA Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 / F199) 279238 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8EQJ1 dapA Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831) 221109 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8EQD3 dapB Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831) 221109 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q04FS1 dapA Oenococcus oeni (strain ATCC BAA-331 / PSU-1) 203123 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q310Q2 dapA Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20) (Desulfovibrio alaskensis) 207559 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q30ZK7 dapB Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20) (Desulfovibrio alaskensis) 207559 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P50260 TUBB2 Oomycete-like sp. (strain MacKay2000) 129195 Tubulin beta-2 chain (Beta-2-tubulin) Was originally (Ref.1) thought to originate from Porphyra purpurea. {ECO:0000305}. reclassified-function P50261 TUBB3 Oomycete-like sp. (strain MacKay2000) 129195 Tubulin beta-3 chain (Beta-3-tubulin) Was originally (Ref.1) thought to originate from Porphyra purpurea. {ECO:0000305}. reclassified-function P50262 TUBB4 Oomycete-like sp. (strain MacKay2000) 129195 Tubulin beta-4 chain (Beta-4-tubulin) Was originally (Ref.1) thought to originate from Porphyra purpurea. {ECO:0000305}. reclassified-function P14597 DUT Orf virus (strain NZ2) (OV NZ-2) 10259 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) Was originally thought to be a protease-like protein (pseudoprotease). {ECO:0000305}. reclassified-function C0HMC3 Ornithodoros savignyi (African eyed tampan) (Soft tick) 69826 BaSO(4)-adsorbing protein 1 (BSAP1) The protein was initially described as an inhibitor of host extrinsic blood coagulation pathway (PubMed:12427468). In another study, it was tested in chromogenic assays with TF-VIIa (F3-F7) and Xa (F10), but no inhibitory activity was observed (PubMed:34118237). {ECO:0000269|PubMed:12427468, ECO:0000269|PubMed:34118237}. reclassified-function P21109 CXCR1 Oryctolagus cuniculus (Rabbit) 9986 C-X-C chemokine receptor type 1 (CXC-R1) (CXCR-1) (High affinity interleukin-8 receptor A) (IL-8R A) (CD antigen CD181) Was originally thought to be the receptor for fMet-Leu-Phe (N-formyl peptide receptor). {ECO:0000305|PubMed:1700779}. reclassified-function Q8WND5 ELP1 Oryctolagus cuniculus (Rabbit) 9986 Elongator complex protein 1 (ELP1) (IkappaB kinase complex-associated protein) (IKK complex-associated protein) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:O95163}. reclassified-function P80912 HINT1 Oryctolagus cuniculus (Rabbit) 9986 Adenosine 5'-monophosphoramidase HINT1 (EC 3.9.1.-) (Desumoylating isopeptidase HINT1) (EC 3.4.22.-) (Histidine triad nucleotide-binding protein 1) (P13.7) Was originally thought to be a protein kinase C inhibitor and to bind zinc in solution. Both seem to be incorrect. {ECO:0000305}. reclassified-function O46480 NDEL1 Oryctolagus cuniculus (Rabbit) 9986 Nuclear distribution protein nudE-like 1 (Protein Nudel) Was originally thought to function as an oligopeptidase (NUDEL-oligopeptidase or endooligopeptidase A) which could regulate peptide levels relevant to brain function. {ECO:0000305|PubMed:10694468}. reclassified-function P13642 SARS1 Oryctolagus cuniculus (Rabbit) 9986 Serine--tRNA ligase, cytoplasmic (EC 6.1.1.11) (62 kDa RNA-binding protein) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) Was originally thought to function in mRNA expression. {ECO:0000305|PubMed:2452088}. reclassified-function Q29503 UBE2R2 Oryctolagus cuniculus (Rabbit) 9986 Ubiquitin-conjugating enzyme E2 R2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme R2) (Ubiquitin carrier protein R2) (Ubiquitin-conjugating enzyme E2-CDC34B) (Ubiquitin-protein ligase R2) Was originally thought to be UBE2R1/CDC34. {ECO:0000305|PubMed:9116038}. reclassified-function P40826 USP14 Oryctolagus cuniculus (Rabbit) 9986 Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) (Deubiquitinating enzyme 14) (Ubiquitin thioesterase 14) (Ubiquitin-specific-processing protease 14) Was originally thought to be a guanine tRNA-ribosyltransferase. {ECO:0000305|PubMed:8579355}. reclassified-function P23612 WARS1 Oryctolagus cuniculus (Rabbit) 9986 Tryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (TrpRS) [Cleaved into: T1-TrpRS; T2-TrpRS] Was originally thought to be a eukaryotic release factor (ERF). {ECO:0000305|PubMed:2185472}. reclassified-function A2ZHF1 LTP Oryza sativa subsp. indica (Rice) 39946 Non-specific lipid-transfer protein 1 (LTP 1) (PAPI) Was originally thought to be an inhibitor of alpha-amylase or of a protease and was known as PAPI: probable alpha-amylase/protease inhibitor. {ECO:0000305}. reclassified-function Q6ZD89 COMT Oryza sativa subsp. japonica (Rice) 39947 Flavone 3'-O-methyltransferase 1 (OsOMT1) (EC 2.1.1.42) (Acetylserotonin O-methyltransferase COMT) (EC 2.1.1.4) (Caffeate O-methyltransferase 1) (OsCOMT1) (EC 2.1.1.68) (OsCOMT) (Quercetin 3'-O-methyltransferase 1) Was initially thought to constitute the naringenin 7-O-methyltransferase (NOMT), a methyltransferase involved in the biosynthesis of the sakuranetin, an inducible defense mechanism of O.sativa against pathogen attack (PubMed:10814825). However, it was later shown that it is not the case (PubMed:22493492). {ECO:0000305|PubMed:10814825, ECO:0000305|PubMed:22493492}. reclassified-function Q67W29 DAPB1 Oryza sativa subsp. japonica (Rice) 39947 Probable 4-hydroxy-tetrahydrodipicolinate reductase 1, chloroplastic (HTPA reductase 1) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q10P67 DAPB2 Oryza sativa subsp. japonica (Rice) 39947 Probable 4-hydroxy-tetrahydrodipicolinate reductase 2, chloroplastic (HTPA reductase 2) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0DX67 DSP2 Oryza sativa subsp. japonica (Rice) 39947 Inositol diphosphatase DSP2 (EC 3.6.1.52) (Inositol pyrophosphate phosphatase DSP2) (Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 2) (OsPFA-DSP2) Was initially described as a protein tyrosine phosphatase and has phosphotyrosine phosphatase activity in vitro but is now thought to function as an inositol pyrophosphate phosphatase. {ECO:0000305}. reclassified-function Q7X7L3 ELP3 Oryza sativa subsp. japonica (Rice) 39947 Elongator complex protein 3 (EC 2.3.1.311) (Elongator component 3) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function Q0IQK9 LTP Oryza sativa subsp. japonica (Rice) 39947 Non-specific lipid-transfer protein 1 (LTP 1) (PAPI) Was originally thought to be an inhibitor of alpha-amylase or of a protease and was known as PAPI: probable alpha-amylase/protease inhibitor. {ECO:0000305}. reclassified-function Q28553 CXCR4 Ovis aries (Sheep) 9940 C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (Fusin) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184) Was originally (Ref.1) thought to be a receptor for neuropeptide Y type 3 (NPY3R) (NPY3-R). {ECO:0000305}. reclassified-function D4GL26 dhaM Pantoea ananatis (strain LMG 20103) 706191 PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM (EC 2.7.1.121) (Dihydroxyacetone kinase subunit M) Was reported to be a protein deacetylase that removes acetyl groups on specific lysine residues in target proteins (PubMed:26716769). However, later experiments demonstrate that the protein ortholog in E.coli does not have any protein deacetylase activity; the discrepancy observed seems to be due to contaminants having proteolytic activity (PubMed:29939131). {ECO:0000269|PubMed:26716769, ECO:0000269|PubMed:29939131}. reclassified-function A6LA57 dapA Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152) 435591 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B2JGX9 dapB Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815) (Burkholderia phymatum) 391038 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7UA33 dapA Parasynechococcus marenigrum (strain WH8102) 84588 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7U807 dapB Parasynechococcus marenigrum (strain WH8102) 84588 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7HX36 dapA Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966) 402881 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7HZ36 dapB Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966) 402881 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9CLZ7 dapA Pasteurella multocida (strain Pm70) 272843 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P57867 dapB Pasteurella multocida (strain Pm70) 272843 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6D0C7 dapB Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica) 218491 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C6DF00 dapB Pectobacterium carotovorum subsp. carotovorum (strain PC1) 561230 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q03HT2 dapA Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w) 278197 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q4FLS1 dapA Pelagibacter ubique (strain HTCC1062) 335992 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q4FNQ1 dapB Pelagibacter ubique (strain HTCC1062) 335992 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1ATI8 dapA Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1) 338966 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1ATI7 dapB Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1) 338966 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B4SE03 dapA Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1) 324925 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B4SEU9 dapB Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1) 324925 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5D2Q5 dapA Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI) 370438 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C0QT41 dapA Persephonella marina (strain DSM 14350 / EX-H1) 123214 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q40901 Petunia integrifolia (Violet-flowered petunia) (Salpiglossis integrifolia) 4103 Defensin-like protein (Gamma-thionin homolog PPT) Was initially thought to be a thionin. {ECO:0000305|PubMed:7948892}. reclassified-function P12628 ME1 Phaseolus vulgaris (Kidney bean) (French bean) 3885 NADP-dependent malic enzyme (NADP-ME) (EC 1.1.1.40) Was originally thought to be a cinnamyl-alcohol dehydrogenase. {ECO:0000305|PubMed:3041415}. reclassified-function B4RCW4 dapA Phenylobacterium zucineum (strain HLK1) 450851 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6L5G7 dapA Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC 11154) (Bacteroides vulgatus) 435590 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P09142 luxF Photobacterium leiognathi 553611 Non-fluorescent flavoprotein (NFP) (FP390) Was originally termed luxG. {ECO:0000305}. reclassified-function Q6LN85 dapA Photobacterium profundum (strain SS9) 298386 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6LUK7 dapB Photobacterium profundum (strain SS9) 298386 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7N8W3 dapB Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) (Photorhabdus luminescens subsp. laumondii) 243265 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1XIL4 dapB Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) 32049 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P21727 Pisum sativum (Garden pea) (Lathyrus oleraceus) 3888 Triose phosphate/phosphate translocator, chloroplastic (cTPT) (E30) (p36) Was originally thought to function as a chloroplast protein import receptor. {ECO:0000305}. reclassified-function Q41015 PIP20-1 Pisum sativum (Garden pea) (Lathyrus oleraceus) 3888 Kunitz-type trypsin inhibitor-like 1 protein (Protease inhibitor from pea 1) Was originally thought to be an alpha-L-fucosidase. {ECO:0000305|PubMed:7559605}.; reclassified-function O82711 PIP20-2 Pisum sativum (Garden pea) (Lathyrus oleraceus) 3888 Kunitz-type trypsin inhibitor-like 2 protein (Protease inhibitor from pea 2) Was originally thought to be an alpha-L-fucosidase. {ECO:0000305|PubMed:7559605}. reclassified-function A0A143ZZK9 ATP4 Plasmodium falciparum (isolate 3D7) 36329 P-type sodium-transporting ATPase4 (PfATP4) (PfATPase4) (EC 7.2.2.3) (P-type cation-transporter ATPase4) Was initially described as Ca(2+)-transporting ATPase (PubMed:11145964). In the later studies, Ca(2+) transport function has not been demonstrated (PubMed:20813948, PubMed:23414762). {ECO:0000269|PubMed:11145964, ECO:0000269|PubMed:20813948, ECO:0000269|PubMed:23414762}. reclassified-function Q25861 TRXR Plasmodium falciparum (isolate FCH-5) 132416 Thioredoxin reductase (PfTrxR) (EC 1.8.1.9) Was originally thought to be a glutathione reductase. {ECO:0000305|PubMed:8719241}. reclassified-function A4SX51 dapA Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus) 312153 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1XT71 dapB Polynucleobacter necessarius subsp. necessarius (strain STIR1) 452638 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5RAX4 CDADC1 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 dCTP deaminase (EC 3.5.4.13) (Cytidine and dCMP deaminase domain-containing protein 1) (Deoxycytidine triphosphate deaminase) (Testis development protein NYD-SP15) CDADC1 was initially reported to exhibit cytidine deaminase activity (By similarity). However, subsequent studies demonstrated that it specifically deaminates dCTP, with no activity toward cytidine or deoxycytidine. The initial attribution may have been an artifact of using partially purified recombinant protein. While one study reported weak activity on dCMP, another failed to detect any dCMP deamination (By similarity). {ECO:0000250|UniProtKB:Q9BWV3}. reclassified-function Q5R5V4 ILK Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Scaffold protein ILK (ILK-1) (ILK-2) (Inactive integrin-linked kinase) (p59ILK) Was originally thought to act as a serine/threonine-protein kinase. Now thought to be a pseudokinase which does not have kinase activity and which functions solely as a scaffold protein. {ECO:0000250|UniProtKB:Q13418}. reclassified-function Q5NVC1 SLC25A19 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Mitochondrial thiamine pyrophosphate carrier (Solute carrier family 25 member 19) Previously identified as the mitochondrial deoxyribonucleotide carrier. However other experiments later demonstrated that SLC25A19 is a thiamine diphosphate transporter and not a mitochondrial deoxyribonucleotide carrier. {ECO:0000250|UniProtKB:Q9HC21}. reclassified-function Q5R5A8 UCP2 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) 9601 Dicarboxylate carrier UCP2 (Mitochondrial uncoupling protein 2) (UCP 2) (Solute carrier family 25 member 8) The role of UCP2/SLC25A8 in mitochondrial proton conductance is a matter of debate. It was initially suggested that it mediates proton leak that increases net proton conductance in response to ROS such as reactive alkenals generated during fatty acid oxidation in mitochondria. By lowering the proton motive force, it would provide for feedback control of mitochondrial ROS metabolism limiting extensive ROS production and protecting cells against oxidative stress. This activity and its potential regulation by ubiquinones and nucleotides was disputed by later studies, which failed to reproduce the effect on proton conductance under physiological conditions. Rather than 'uncoupling' the link between electron transfer and ATP synthesis, it may couple metabolite transport to proton flux to allow for optimal ATP turnover. {ECO:0000250|UniProtKB:P55851, ECO:0000250|UniProtKB:P70406}. reclassified-function B2RMB9 dapA Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) 431947 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A2BTN4 dapA Prochlorococcus marinus (strain AS9601) 146891 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A9BD97 dapA Prochlorococcus marinus (strain MIT 9211) 93059 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8G7F8 dapA Prochlorococcus marinus (strain MIT 9215) 93060 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A3PFE1 dapA Prochlorococcus marinus (strain MIT 9301) 167546 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A2C5R9 dapA Prochlorococcus marinus (strain MIT 9303) 59922 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q317Y9 dapA Prochlorococcus marinus (strain MIT 9312) 74546 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7V990 dapA Prochlorococcus marinus (strain MIT 9313) 74547 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7V7D4 dapB Prochlorococcus marinus (strain MIT 9313) 74547 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A2BZ39 dapA Prochlorococcus marinus (strain MIT 9515) 167542 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q46ID7 dapA Prochlorococcus marinus (strain NATL2A) 59920 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q46KV7 dapB Prochlorococcus marinus (strain NATL2A) 59920 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P49423 dapA Prochlorococcus marinus (strain SARG / CCMP1375 / SS120) 167539 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7VC38 dapB Prochlorococcus marinus (strain SARG / CCMP1375 / SS120) 167539 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7UZK9 dapA Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4) 59919 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7V1N1 dapB Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4) 59919 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B4S5J5 dapA Prosthecochloris aestuarii (strain DSM 271 / SK 413) 290512 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B4F2T9 dapB Proteus mirabilis (strain HI4320) 529507 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6MDD9 dapA Protochlamydia amoebophila (strain UWE25) 264201 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P0DN88 dhaM Providencia stuartii (strain MRSN 2154) 1157951 PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM (EC 2.7.1.121) (Dihydroxyacetone kinase subunit M) Was reported to be a protein deacetylase that removes acetyl groups on specific lysine residues in target proteins (PubMed:26716769). However, later experiments demonstrate that the protein ortholog in E.coli does not have any protein deacetylase activity; the discrepancy observed seems to be due to contaminants having proteolytic activity (PubMed:29939131). {ECO:0000269|PubMed:26716769, ECO:0000269|PubMed:29939131}. reclassified-function Q15SZ4 dapA Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) 3042615 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q15TQ4 dapB Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) 3042615 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3IKQ7 dapB Pseudoalteromonas translucida (strain TAC 125) 326442 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9I4V0 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 NADH:quinone reductase (EC 1.6.5.9) Was reported to be a 2-nitropropane dioxygenase, the previous name for nitronate monooxygenase (PubMed:16682407). However, later experiments demonstrate that this protein does not have any nitronate monooxygenase activity, the activity reported by Ha et al. was likely due to the non-enzymatic reaction of propyl-2-nitronate with oxygen (PubMed:27502282). {ECO:0000269|PubMed:16682407, ECO:0000269|PubMed:27502282}. reclassified-function P40882 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 Uncharacterized protein PA3753 Was originally (Ref.1) thought to be a ferripyochelin binding protein (gene fbp). {ECO:0000305}. reclassified-function Q9HY80 bfd Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 Bacterioferritin-associated ferredoxin (Bfd) Was originally thought to not require the [2Fe-2S] cluster for iron mobilization from BfrB (PubMed:19575528). Subsequent experiments show the [2Fe-2S] cluster is necessary (PubMed:22812654). {ECO:0000269|PubMed:19575528, ECO:0000269|PubMed:22812654}. reclassified-function Q9I589 cbpD Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 Chitin-binding protein CbpD (Protease LasD) Was originally thought to be a protease that processes pro-LasA. {ECO:0000269|PubMed:7565088, ECO:0000269|PubMed:9721177}. reclassified-function O05927 cysH Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 Adenosine 5'-phosphosulfate reductase (APS reductase) (EC 1.8.4.10) (5'-adenylylsulfate reductase) (Thioredoxin-dependent 5'-adenylylsulfate reductase) The [4Fe-4S] cluster was originally thought to be ligated by three cysteine residues, but the crystal structure establishes that it is ligated by four cysteine residues. {ECO:0000269|PubMed:15491155, ECO:0000269|PubMed:16289027, ECO:0000269|PubMed:17010373}. reclassified-function Q9HTQ0 dadA1 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 D-amino acid dehydrogenase 1 (EC 1.4.99.-) (D-alanine dehydrogenase 1) Was originally thought to be a heterodimer based on the purification of the enzyme first reported from E.coli B, but results of enzyme assays in PubMed:21378189 have indicated that DadA is solely responsible for the observed dehydrogenase activity. {ECO:0000305}. reclassified-function Q9I4W3 dapA Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P38103 dapB Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9HWF9 ftnA Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 Bacterial ferritin (FtnA) (EC 1.16.3.1) (Bacterial non-heme ferritin) (Bacterioferritin alpha subunit) (BFR alpha subunit) (Nonheme-iron-containing cytochrome b557) Was originally thought to be a bacterioferritin (PubMed:10984043). Its inability to bind heme shows it is actually a bacterial ferritin (PubMed:21574546). {ECO:0000269|PubMed:21574546, ECO:0000305|PubMed:10984043}. reclassified-function P42812 lolB Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 Outer-membrane lipoprotein LolB Was originally thought to be involved in delta-aminolevulinic acid biosynthesis. {ECO:0000305}. reclassified-function P32265 nfxB Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 HTH-type transcriptional regulator NfxB The previously assigned start codon can be mutated without significantly affecting function, whereas altering the current start codon abolishes repressor function, justifying the 12 amino-acid N-terminal extension. {ECO:0000269|PubMed:23924707}. reclassified-function B7V1H1 dapB Pseudomonas aeruginosa (strain LESB58) 557722 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q02FR3 dapB Pseudomonas aeruginosa (strain UCBPP-PA14) 208963 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q52419 dapB Pseudomonas amygdali pv. tabaci (Pseudomonas syringae pv. tabaci) 322 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1IF57 dapB Pseudomonas entomophila (strain L48) 384676 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P0C1F6 ccmE Pseudomonas fluorescens 294 Cytochrome c-type biogenesis protein CcmE (Cytochrome c maturation protein E) (Heme chaperone CcmE) Was originally proposed to be fused with ccmD. {ECO:0000305|PubMed:8692990}. reclassified-function Q4KIG9 dapB Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5) 220664 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3KI98 dapB Pseudomonas fluorescens (strain Pf0-1) 205922 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q84CP9 dapB Pseudomonas fluorescens (strain SBW25) 216595 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6VCL6 dapB Pseudomonas paraeruginosa (strain DSM 24068 / PA7) (Pseudomonas aeruginosa (strain PA7)) 381754 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P11124 P2 Pseudomonas phage phi6 (Bacteriophage phi-6) 2928686 RNA-directed RNA polymerase (EC 2.7.7.48) (Protein P2) Was originally thought to be a capsid protein. {ECO:0000305|PubMed:3346944}. reclassified-function Q5PWZ8 acdS Pseudomonas putida (Arthrobacter siderocapsulatus) 303 1-aminocyclopropane-1-carboxylate deaminase (ACC deaminase) (ACCD) (EC 3.5.99.7) Was originally (PubMed:9851025) thought to originate from Pseudomonas sp. Then it was changed to Enterobacter cloacae, then to P.putida. {ECO:0000305|PubMed:9851025}. reclassified-function P00436 pcaG Pseudomonas putida (Arthrobacter siderocapsulatus) 303 Protocatechuate 3,4-dioxygenase alpha chain (EC 1.13.11.3) (3,4-PCD) Strain ATCC 23975 was originally classified as being from Pseudomonas aeruginosa. {ECO:0000305}. reclassified-function P00437 pcaH Pseudomonas putida (Arthrobacter siderocapsulatus) 303 Protocatechuate 3,4-dioxygenase beta chain (EC 1.13.11.3) (3,4-PCD) Strain ATCC 23975 was originally classified as being from Pseudomonas aeruginosa. {ECO:0000305}. reclassified-function Q88DU4 dapB Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) 160488 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5W9A1 dapB Pseudomonas putida (strain ATCC 700007 / DSM 6899 / JCM 31910 / BCRC 17059 / LMG 24140 / F1) 351746 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function F8G0P1 pnao Pseudomonas putida (strain DSM 28022 / S16) 1042876 Pseudooxynicotine dehydrogenase (EC 1.4.2.3) (Pon amine dehydrogenase) (Pseudooxynicotine amine oxidase) (Pnao) Was originally thought to act as an oxidase (PubMed:26634650). However, it was shown later that this enzyme is actually a dehydrogenase, using a cytochrome c as the natural electron acceptor (PubMed:35835223). {ECO:0000269|PubMed:26634650, ECO:0000269|PubMed:35835223}. reclassified-function B0KIS3 dapB Pseudomonas putida (strain GB-1) 76869 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1JDB7 dapA Pseudomonas putida (strain W619) 390235 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1J256 dapB Pseudomonas putida (strain W619) 390235 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q48LD5 dapA Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)) 264730 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q48E64 dapB Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)) 264730 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function H8ZPX1 pao Pseudomonas sp 306 Pseudooxynicotine dehydrogenase (EC 1.4.2.3) (Pseudooxynicotine amine oxidase) (PNAO) Was originally thought to act as an oxidase, but it was shown later in Pseudomonas putida S16 (AC F8G0P1) that this enzyme actually functions as a dehydrogenase, using a cytochrome c as the natural electron acceptor. {ECO:0000305}. reclassified-function Q936X3 atzE Pseudomonas sp. (strain ADP) 47660 1-carboxybiuret hydrolase subunit AtzE (EC 3.5.1.131) Was originally thought to use biuret as substrate (PubMed:11544232). But new evidence has shown that 1-carboxybiuret is the real substrate. The error occurred since 1-carboxybiuret hydrolyzes spontaneously to biuret (PubMed:29523689). {ECO:0000269|PubMed:11544232, ECO:0000269|PubMed:29523689}. reclassified-function P27101 tcbF Pseudomonas sp. (strain P51) 65067 Maleylacetate reductase (EC 1.3.1.32) Was originally thought to be a trans-dienelactoneisomerase. {ECO:0000305|PubMed:2013566}. reclassified-function Q4ZW75 dapA Pseudomonas syringae pv. syringae (strain B728a) 205918 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q4ZNP9 dapB Pseudomonas syringae pv. syringae (strain B728a) 205918 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q87WP2 dapB Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000) 223283 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q4FVD6 dapA Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4) 259536 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q4FVQ6 dapB Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4) 259536 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5WHC3 dapA Psychrobacter sp. (strain PRwf-1) 349106 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1SVX2 dapA Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37) 357804 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8ZU79 surE1 Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2) 178306 5'-nucleotidase SurE 1 (EC 3.1.3.5) (Nucleoside 5'-monophosphate phosphohydrolase 1) Was originally annotated as an acid phosphatase (EC 3.1.3.2). {ECO:0000305}. reclassified-function Q9UXT7 kae1 Pyrococcus abyssi (strain GE5 / Orsay) 272844 tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (Pa-Kae1) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1) (tRNA threonylcarbamoyladenosine biosynthesis protein Kae1) Was originally (PubMed:17766251) thought to have endonuclease activity, but it could not be confirmed with orthologs purified from M.jannaschii (PubMed:18951093) and S.cerevisiae (PubMed:21183954). {ECO:0000305|PubMed:17766251}. reclassified-function P59856 apcA Pyropia yezoensis (Susabi-nori) (Porphyra yezoensis) 2788 Allophycocyanin alpha chain Neither a protein sequence nor a nucleotide sequence had been determined for this protein when the crystallographic structure was reported. The sequence of a model fit to electron density plots at 2.2 Angstroms resolution was used. When a nucleotide sequence became available, it replaced the model sequence. There are 14 differences between the model and the nucleotide sequences. {ECO:0000305}. reclassified-function Q8Y099 dapA Ralstonia nicotianae (strain ATCC BAA-1114 / GMI1000) (Ralstonia solanacearum) 267608 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8XVT2 dapB Ralstonia nicotianae (strain ATCC BAA-1114 / GMI1000) (Ralstonia solanacearum) 267608 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2UCA2 dapB Ralstonia pickettii (strain 12J) 402626 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P02532 Rana temporaria (European common frog) 8407 Rho crystallin Was originally called epsilon crystallin. {ECO:0000305}. reclassified-function P29188 Rattus norvegicus (Rat) 10116 Putative N-acylneuraminate cytidylyltransferase (EC 2.7.7.43) (CMP-N-acetylneuraminic acid synthase) (CMP-NeuNAc synthase) Was originally (PubMed:1577759) thought to be the main N-acylneuraminate cytidylyltransferase enzyme in rat. However, it does not correspond to the CMAS protein, which was then been shown to correspond to the major N-acylneuraminate cytidylyltransferase enzyme. The relevance and existence of this sequence is therefore unsure. {ECO:0000305|PubMed:1577759}. reclassified-function P31392 Ackr5 Rattus norvegicus (Rat) 10116 Atypical chemokine receptor 5 (G protein-coupled receptor 182) (G10D) (NOW) Was originally thought to be a receptor for adrenomedullin. However, this function was later not confirmed (PubMed:9535752). {ECO:0000269|PubMed:9535752, ECO:0000305|PubMed:7592696}. reclassified-function Q9QZ81 Ago2 Rattus norvegicus (Rat) 10116 Protein argonaute-2 (Argonaute2) (EC 3.1.26.n2) (Argonaute RISC catalytic component 2) (Eukaryotic translation initiation factor 2C 2) (eIF-2C 2) (eIF2C 2) (Golgi ER protein 95 kDa) (GERp95) (Protein slicer) Was originally thought to be membrane-associated. {ECO:0000305|PubMed:10512872}. reclassified-function P02770 Alb Rattus norvegicus (Rat) 10116 Albumin A peptide arising from positions 166 to 174 was originally termed neurotensin-related peptide (NRP) and was thought to regulate fat digestion, lipid absorption, and blood flow. {ECO:0000305|PubMed:2437111}. reclassified-function P52303 Ap1b1 Rattus norvegicus (Rat) 10116 AP-1 complex subunit beta-1 (Adaptor protein complex AP-1 subunit beta-1) (Adaptor-related protein complex 1 subunit beta-1) (Beta-1-adaptin) (Beta-adaptin 1) (Clathrin assembly protein complex 1 beta large chain) (Golgi adaptor HA1/AP1 adaptin beta subunit) Was originally thought to be part of the complex AP-2. {ECO:0000305|PubMed:2495531}. reclassified-function P18890 Arhgap39 Rattus norvegicus (Rat) 10116 Rho GTPase-activating protein 39 (Preoptic regulatory factor 2) (PORF-2) Was originally thought to be a precursor for a secreted GNRH-like peptide. {ECO:0000305|PubMed:2293025}. reclassified-function D4A693 Azin2 Rattus norvegicus (Rat) 10116 Antizyme inhibitor 2 (AzI2) (Ornithine decarboxylase-like protein) (ODC-like protein) (ornithine decarboxylase paralog) (ODC-p) Human ortholog was initially reported to have ornithine decarboxylase or arginine decarboxylase activities, but it was later found that the mouse ortholog does not possess neither of them. {ECO:0000305}. reclassified-function Q6AYB8 Blzf1 Rattus norvegicus (Rat) 10116 Golgin-45 (Basic leucine zipper nuclear factor 1) Was initially thought to be a potential transcription factor, localized in the nucleus. {ECO:0000305}. reclassified-function P18418 Calr Rattus norvegicus (Rat) 10116 Calreticulin (CALBP) (CRP55) (Calcium-binding protein 3) (CABP3) (Calregulin) (Endoplasmic reticulum resident protein 60) (ERp60) (HACBP) Was originally (Ref.9) thought to be D-beta-hydroxybutyrate dehydrogenase. {ECO:0000305}. reclassified-function B2GV72 Cbr3 Rattus norvegicus (Rat) 10116 Carbonyl reductase [NADPH] 3 (EC 1.1.1.184) (Monomeric carbonyl reductase 3) (Quinone reductase CBR3) (EC 1.6.5.10) There are conflicting results on the ability of CBR3 to metabolize menadione. Although menadione was originally reported as a good substrate of CBR3 (By similarity). Results of later studies showed that CBR3 possesses very low or no activity toward menadione (PubMed:18983987). {ECO:0000250|UniProtKB:O75828, ECO:0000269|PubMed:18983987}. reclassified-function Q4KLH6 Cep162 Rattus norvegicus (Rat) 10116 Centrosomal protein of 162 kDa (Cep162) (Protein QN1 homolog) Was initially thought to regulate chromosome segregation and mitotic spindle assembly (PubMed:16302001). However, it was later shown that its absence neither affect mitosis nor centriole duplication. {ECO:0000305|PubMed:16302001}. reclassified-function Q04753 Clns1a Rattus norvegicus (Rat) 10116 Methylosome subunit pICln (Chloride channel, nucleotide sensitive 1A) (Chloride conductance regulatory protein ICln) (I(Cln)) Was originally thought to be a chloride channel. {ECO:0000305}. reclassified-function P55091 Ctrc Rattus norvegicus (Rat) 10116 Chymotrypsin-C (EC 3.4.21.2) (Caldecrin) (Serum calcium-decreasing factor) Was originally thought to be elastase IV. {ECO:0000305|PubMed:1537555}. reclassified-function Q6MG60 Ddah2 Rattus norvegicus (Rat) 10116 Putative hydrolase DDAH2 (EC 3.-.-.-) (DDAHII) (Inactive N(G),N(G)-dimethylarginine dimethylaminohydrolase 2) (DDAH-2) (Inactive dimethylarginine dimethylaminohydrolase 2) Was originally thought to be a dimethylarginine dimethylaminohydrolase (with EC:3.5.3.18) able to hydrolyze N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) (By similarity). However, a recent multicentre study has shown that DDAH2 does not have dimethylarginine dimethylaminohydrolase activity by using different approaches (By similarity). {ECO:0000250|UniProtKB:O95865}. reclassified-function P97554 Dnajb9 Rattus norvegicus (Rat) 10116 DnaJ homolog subfamily B member 9 (Endoplasmic reticulum DNA J domain-containing protein 4) (ER-resident protein ERdj4) (ERdj4) (Microvascular endothelial differentiation gene 1 protein) (Mdg-1) Was initially reported to localize in the nucleus (PubMed:11525638). However, it was later shown to localize in the endoplasmic reticulum lumen. {ECO:0000305|PubMed:11525638}. reclassified-function Q8VHU4 Elp1 Rattus norvegicus (Rat) 10116 Elongator complex protein 1 (ELP1) (IkappaB kinase complex-associated protein) (IKK complex-associated protein) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:O95163}. reclassified-function Q496Z0 Elp2 Rattus norvegicus (Rat) 10116 Elongator complex protein 2 (ELP2) (SHINC-2) (STAT3-interacting protein 1) (StIP1) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q6IA86}. reclassified-function Q6IUP3 Elp5 Rattus norvegicus (Rat) 10116 Elongator complex protein 5 (Dermal papilla-derived protein 6 homolog) (Retinoic acid-induced protein 12) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q8TE02}.; reclassified-function B2RYG8 Elp6 Rattus norvegicus (Rat) 10116 Elongator complex protein 6 (Protein TMEM103) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q0PNE2}. reclassified-function P11475 Esrrb Rattus norvegicus (Rat) 10116 Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2) Was originally (PubMed:3267207) thought to originate from human but was later shown (PubMed:10072763) to be derived from rat. {ECO:0000305|PubMed:10072763, ECO:0000305|PubMed:3267207}. reclassified-function Q9R0C5 Galnt7 Rattus norvegicus (Rat) 10116 N-acetylgalactosaminyltransferase 7 (EC 2.4.1.41) (Polypeptide GalNAc transferase 7) (GalNAc-T7) (pp-GaNTase 7) (Protein-UDP acetylgalactosaminyltransferase 7) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7) Was originally termed Galnt6/pp-GaNTase 6. {ECO:0000305|PubMed:10488133}. reclassified-function Q63226 Grid2 Rattus norvegicus (Rat) 10116 Glutamate receptor ionotropic, delta-2 (GluD2) (GluR delta-2 subunit) The ligand-gated cation channel activity was previously disputed due to a lack of evidence for direct ligand-gated ion channel activity (By similarity). However, structural studies have shown an asymmetric opening of the ion channel upon D-serine binding, and this would explain the lack of activity in the absence of D-serine (By similarity). {ECO:0000250|UniProtKB:O43424}. reclassified-function A0A8I6GM68 Hdac6 Rattus norvegicus (Rat) 10116 Protein deacetylase HDAC6 (EC 3.5.1.-) (E3 ubiquitin-protein ligase HDAC6) (EC 2.3.2.-) (Tubulin-lysine deacetylase HDAC6) (EC 3.5.1.-) Was originally thought to be a histone deacetylase. However, subsequent work has shown that it is predominantly cytoplasmic and deacetylates a range of non-histone substrates. {ECO:0000250|UniProtKB:Q9UBN7}. reclassified-function P62959 Hint1 Rattus norvegicus (Rat) 10116 Adenosine 5'-monophosphoramidase HINT1 (EC 3.9.1.-) (17 kDa inhibitor of protein kinase C) (Desumoylating isopeptidase HINT1) (EC 3.4.22.-) (Histidine triad nucleotide-binding protein 1) (Protein kinase C inhibitor 1) (Protein kinase C-interacting protein 1) (PKCI-1) Was originally thought to be a protein kinase C inhibitor and to bind zinc in solution. Both seem to be incorrect. {ECO:0000305}. reclassified-function Q8N7M5 Hjv Rattus norvegicus (Rat) 10116 Hemojuvelin (Hemochromatosis type 2 protein homolog) (Hemojuvelin BMP coreceptor) (RGM domain family member C) Was originally (Ref.1) thought to originate from human. {ECO:0000305}. reclassified-function Q61453 Il17a Rattus norvegicus (Rat) 10116 Interleukin-17A (IL-17) (IL-17A) (Cytotoxic T-lymphocyte-associated antigen 8) (CTLA-8) Was originally thought to be from mouse but, on the basis of subsequent work (PubMed:8654948, PubMed:8877732) has been shown to be of rat origin. {ECO:0000305|PubMed:8390535}. reclassified-function Q99J82 Ilk Rattus norvegicus (Rat) 10116 Scaffold protein ILK (ILK-1) (ILK-2) (Inactive integrin-linked kinase) (p59ILK) Was originally thought to act as a serine/threonine-protein kinase. Now thought to be a pseudokinase which does not have kinase activity and which functions solely as a scaffold protein. {ECO:0000250|UniProtKB:Q13418}. reclassified-function Q99068 Lrpap1 Rattus norvegicus (Rat) 10116 Alpha-2-macroglobulin receptor-associated protein (Alpha-2-MRAP) (Gp330-binding 45 kDa protein) (Low density lipoprotein receptor-related protein-associated protein 1) (RAP) Was originally thought to be Heymann nephritis antigen gp330. {ECO:0000305|PubMed:2408041}. reclassified-function P15205 Map1b Rattus norvegicus (Rat) 10116 Microtubule-associated protein 1B (MAP-1B) (Neuraxin) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1] A C-terminal fragment of this protein (residues 1599 to 2461) was originally described as neuraxin in PubMed:2555150. {ECO:0000305}. reclassified-function Q9Z311 Mecr Rattus norvegicus (Rat) 10116 Enoyl-[acyl-carrier-protein] reductase, mitochondrial (EC 1.3.1.104) (2-enoyl thioester reductase) (Nuclear receptor-binding factor 1) (NRBF-1) Was originally (PubMed:9795230) thought to be a nuclear protein that interact with nuclear receptor. However, it was shown later to be mitochondrial (PubMed:12654921), a function related to nuclear receptors being unsure. {ECO:0000305|PubMed:12654921, ECO:0000305|PubMed:9795230}. reclassified-function Q7TN49 Mrgpra Rattus norvegicus (Rat) 10116 Mas-related G protein-coupled receptor member A Was originally thought to be an adenine receptor but PubMed:12397184 found no activation by adenine of the mouse ortholog. {ECO:0000305|PubMed:12084918}. reclassified-function Q62967 Mvd Rattus norvegicus (Rat) 10116 Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Mevalonate (diphospho)decarboxylase) (MDDase) (Mevalonate pyrophosphate decarboxylase) Was originally thought to be located in the peroxisome (By similarity). However, was later shown to be cytosolic (PubMed:11725955). {ECO:0000250|UniProtKB:P53602, ECO:0000269|PubMed:11725955}. reclassified-function Q78PB6 Ndel1 Rattus norvegicus (Rat) 10116 Nuclear distribution protein nudE-like 1 (Protein Nudel) Was originally thought to function as an oligopeptidase (NUDEL-oligopeptidase or endooligopeptidase A) which could regulate peptide levels relevant to brain function. {ECO:0000305|PubMed:15728732}. reclassified-function Q9ET55 Noct Rattus norvegicus (Rat) 10116 Nocturnin (EC 3.1.3.108) (Carbon catabolite repression 4-like protein) Was initially shown to have low deadenylase activity that was lost when the metal-binding Glu was mutated (By similarity). Later studies showed that the purified protein lacked deadenylase activity (By similarity). Was subsequently shown to act as a phosphatase (By similarity). {ECO:0000250|UniProtKB:O35710, ECO:0000250|UniProtKB:Q9UK39}. reclassified-function Q06518 Nos2 Rattus norvegicus (Rat) 10116 Nitric oxide synthase, inducible (EC 1.14.13.39) (Inducible NO synthase) (Inducible NOS) (iNOS) (NOS type II) (Peptidyl-cysteine S-nitrosylase NOS2) sequence Was originally thought to originate from human but appears to be from rat. {ECO:0000305|PubMed:9851365}. reclassified-function P70563 Nudt6 Rattus norvegicus (Rat) 10116 Nudix hydrolase 6 (FAD diphosphatase NUDT6) (EC 3.6.1.18) (NADH pyrophosphatase NUDT6) (EC 3.6.1.22) (Nucleoside diphosphate-linked moiety X motif 6) (Nudix motif 6) (Protein GFG) The rat protein was reported to play a role in DNA repair (PubMed:9406864), based on its ability to complement E.coli deficient in the DNA repair enzyme mutT that hydrolyzes oxidized guanine nucleotides. PubMed:17569023 found no such activity, neither for the human nor the rat protein. {ECO:0000305|PubMed:9406864}. reclassified-function Q8VIJ5 Oga Rattus norvegicus (Rat) 10116 Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Bifunctional protein NCOAT) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (N-acetyl-beta-glucosaminidase) Was initially identified as a bi-functional protein that has an N-terminal domain with O-GlcNAcase activity and a C-terminal domain that has histone acetyltransferase activity (PubMed:15485860). The protein has apparent histone acetyltransferase activity when expressed in mammalian cells, but not when expressed in bacterial cells (PubMed:15485860), suggesting that the histone acetyltransferase activity might be due to the presence of a contaminant. Characterization of the human ortholog shows that this protein does not bind acetyl-CoA and therefore cannot have acetyltransferase activity. {ECO:0000305}. reclassified-function Q6Y1R5 Oxgr1 Rattus norvegicus (Rat) 10116 2-oxoglutarate receptor 1 (Alpha-ketoglutarate receptor 1) (G protein-coupled receptor 80) (P2Y purinoceptor 15) (P2Y15) Was originally thought to be a P2Y receptor. {ECO:0000305|PubMed:15001573}. reclassified-function Q64663 P2rx7 Rattus norvegicus (Rat) 10116 P2X purinoceptor 7 (P2X7) (ATP receptor) (P2Z receptor) (Purinergic receptor) Was originally thought to form a dilated pore (macropore) after prolonged exposure to ATP, permitting passage of large organic cations (PubMed:10204537, PubMed:8614837). Two mechanisms have been proposed to explain macropore formation: progressive dilatation and/or the recruitment of an accessory pore-forming molecule (PubMed:10204537, PubMed:17036048). However, convincing evidences now clearly suggest that P2RX7 channel itself has the ability to form a large-conductance pore in the absence of any significant dilatation. The P2RX7 channel allows the passage of large cationic molecules immediately from its initial activation, but at a much slower pace than that of the small cations Na(+), K(+), and Ca(2+) (By similarity). {ECO:0000250|UniProtKB:Q99572, ECO:0000269|PubMed:10204537, ECO:0000269|PubMed:17036048, ECO:0000269|PubMed:8614837}. reclassified-function Q64375 P3h4 Rattus norvegicus (Rat) 10116 Endoplasmic reticulum protein SC65 (Leprecan-like protein 4) (Prolyl 3-hydroxylase family member 4) (Synaptonemal complex protein SC65) Was initially identified in the synaptonemal complex (PubMed:1363622). Characterization data from human and mouse indicate the protein is in the endoplasmic reticulum, which agrees with its biological function and the predicted signal sequence. {ECO:0000269|PubMed:1363622, ECO:0000305}. reclassified-function P04785 P4hb Rattus norvegicus (Rat) 10116 Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Cellular thyroid hormone-binding protein) (Prolyl 4-hydroxylase subunit beta) Was originally (PubMed:8251535, PubMed:3178809) thought to be identical to thyroxine deiodinase but this was later shown to be incorrect. {ECO:0000305|PubMed:2757644}. reclassified-function P11598 Pdia3 Rattus norvegicus (Rat) 10116 Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60) (HIP-70) (Q-2) Was originally thought to be a phosphatidyl-inositol 4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha) then was thought (PubMed:1321829, PubMed:1330685) to be a thiol protease. {ECO:0000305|PubMed:3398923}. reclassified-function O08654 Phaf1 Rattus norvegicus (Rat) 10116 Phagosome assembly factor 1 Was originally thought to be a lin-10 homolog. {ECO:0000305|PubMed:9480860}. reclassified-function F1M8G0 Phtf1 Rattus norvegicus (Rat) 10116 Protein PHTF1 The PHTF domain was initially defined as an atypical homeodomain, suggesting that this protein could act as a transcription regulator (By similarity). However, the protein is not found in the nucleus and mainly localizes in the endoplasmic reticulum membrane, suggesting that it does not act as a transcription factor (PubMed:12604659). {ECO:0000250|UniProtKB:Q9UMS5, ECO:0000269|PubMed:12604659}. reclassified-function P54316 Pnliprp1 Rattus norvegicus (Rat) 10116 Inactive pancreatic lipase-related protein 1 (PL-RP1) Was originally thought to be the pancreatic lipase, but has been shown to have very low or undetectable lipase activity in vitro. {ECO:0000305}. reclassified-function P09217 Prkcz Rattus norvegicus (Rat) 10116 Protein kinase C zeta type (EC 2.7.11.13) (nPKC-zeta) Isoform 2 (PKMzeta) was initially thought to be generated by proteolysis of full-length PRKCZ (PubMed:8378304). However, PKMzeta is a bona fide isoform produced by an alternative promoter in intron 4 (PubMed:12857744). {ECO:0000269|PubMed:12857744, ECO:0000303|PubMed:8378304}. reclassified-function P02782 Psbpc1 Rattus norvegicus (Rat) 10116 Prostatic steroid-binding protein C1 (Prostatein peptide C1) Was originally (Ref.4) thought to originate from mouse. {ECO:0000305}. reclassified-function P43114 Ptger4 Rattus norvegicus (Rat) 10116 Prostaglandin E2 receptor EP4 subtype (PGE receptor EP4 subtype) (PGE2 receptor EP4 subtype) (Prostanoid EP4 receptor) Was originally designated as the EP2 subtype. {ECO:0000305}. reclassified-function Q8CJB9 Rnf40 Rattus norvegicus (Rat) 10116 E3 ubiquitin-protein ligase BRE1B (BRE1-B) (EC 2.3.2.27) (RING finger protein 40) (RING-type E3 ubiquitin transferase BRE1B) (Syntaxin-1-interacting RING finger protein) (Protein staring) Was originally thought to be cytoplasmic and membrane-associated and to mediate ubiquitination and subsequent degradation of STX1A. {ECO:0000305|PubMed:12121982}. reclassified-function P02634 S100g Rattus norvegicus (Rat) 10116 Protein S100-G (9 kDa CaBP) (Calbindin-D9k) (Cholecalcin) (S100 calcium-binding protein G) (Vitamin D-dependent calcium-binding protein, intestinal) (CABP) Was originally thought to originate from chick. {ECO:0000305|PubMed:7750504}. reclassified-function O35910 Slc16a3 Rattus norvegicus (Rat) 10116 Monocarboxylate transporter 4 (MCT 4) (Monocarboxylate transporter 3) (MCT 3) (Solute carrier family 16 member 3) Was initially thought to be considered to be a low affinity lactate transporter with negligible affinity for pyruvate (By similarity). However, it was later shown that SLC16A3 is a high affinity lactate transporter with physiologically relevant affinity for pyruvate (By similarity). {ECO:0000250|UniProtKB:O15427}.; reclassified-function Q9P290 Slc22a17 Rattus norvegicus (Rat) 10116 Solute carrier family 22 member 17 (24p3 receptor) (24p3R) (Brain-type organic cation transporter) (Lipocalin-2 receptor) Was originally (Ref.1) thought to originate from human. {ECO:0000305}. reclassified-function P97700 Slc25a11 Rattus norvegicus (Rat) 10116 Mitochondrial 2-oxoglutarate/malate carrier protein (Alpha-oxoglutarate carrier) (OGCP) (Solute carrier family 25 member 11) (SLC25A11) Was previously reported to transport glutathione (PubMed:16291728). However, subsequent work showed that the human protein does not transport glutathione and that previous results reporting a role in glutathione transport are likely to be an artifact of the experimental conditions. {ECO:0000269|PubMed:16291728, ECO:0000305}. reclassified-function Q6AYL0 Slc25a19 Rattus norvegicus (Rat) 10116 Mitochondrial thiamine pyrophosphate carrier (Mitochondrial uncoupling protein 1) (Solute carrier family 25 member 19) Previously identified as the mitochondrial deoxyribonucleotide carrier. However other experiments later demonstrated that SLC25A19 is a thiamine diphosphate transporter and not a mitochondrial deoxyribonucleotide carrier. {ECO:0000250|UniProtKB:Q9HC21}. reclassified-function Q6AY78 Slc67a1 Rattus norvegicus (Rat) 10116 Solute carrier family 22 member 18 (Organic cation transporter-like protein 2) (ORCTL-2) Was initially classified as a member of the SLC22 family. However, an evolutionary and phylogenetic analysis suggested that SLC22A18 is unique and that it is most distantly related to SLC22 family members. {ECO:0000250|UniProtKB:Q96BI1}. reclassified-function P28570 Slc6a8 Rattus norvegicus (Rat) 10116 Sodium- and chloride-dependent creatine transporter 1 (CHOT1) (CT1) (Creatine transporter 1) (Solute carrier family 6 member 8) Was originally thought to be a choline transporter. {ECO:0000305|PubMed:1633856}. reclassified-function Q00910 Slco2a1 Rattus norvegicus (Rat) 10116 Solute carrier organic anion transporter family member 2A1 (SLCO2A1) (Matrin F/G 1) (OATP2A1) (PHOAR2) (Prostaglandin transporter) (PGT) (Solute carrier family 21 member 2) (SLC21A2) Was originally thought to be a nuclear DNA-binding protein. {ECO:0000305|PubMed:2068100}. reclassified-function Q64298 Smcp Rattus norvegicus (Rat) 10116 Sperm mitochondrial-associated cysteine-rich protein Was originally thought to be a selenoprotein and was known as sperm mitochondrial capsule selenoprotein. {ECO:0000305|PubMed:8634143}. reclassified-function Q5RJM1 Srd5a3 Rattus norvegicus (Rat) 10116 Polyprenal reductase (EC 1.3.1.94) (3-oxo-5-alpha-steroid 4-dehydrogenase 3) (EC 1.3.1.22) (Steroid 5-alpha-reductase 3) (S5AR 3) (SR type 3) Was initially characterized as a polyprenol reductase, mediating the conversion of polyprenol into dolichol (PubMed:8486680). However, it was later shown to catalyze an intermediate step in this pathway and reduce polyprenal (By similarity). {ECO:0000250|UniProtKB:Q9H8P0, ECO:0000269|PubMed:8486680}. reclassified-function Q9JKT7 Tas2r13 Rattus norvegicus (Rat) 10116 Taste receptor type 2 member 13 (T2R13) (Taste receptor type 2 member 121) (Taste receptor type 2 member 7) (T2R7) This protein was previously referred to as T2R7 but is now considered to be the ortholog of human TAS2R13. {ECO:0000305}. reclassified-function Q9JKE7 Tas2r41 Rattus norvegicus (Rat) 10116 Taste receptor type 2 member 41 (T2R41) (T2R12) (Taste receptor type 2 member 126) This protein was previously referred to as T2R26 or T2R12 but is now considered to be the ortholog of human TAS2R41. {ECO:0000305}. reclassified-function Q5U2T1 Tlcd1 Rattus norvegicus (Rat) 10116 TLC domain-containing protein 1 (Calfacilitin) Was originally proposed to be a calcium channel facilitator (By similarity). However, a more recent study shows that this protein regulates membrane phospholipid homeostasis (By similarity). Therefore, any effects on calcium flux are most likely a secondary consequence of defects in membrane composition or fluidity (By similarity). {ECO:0000250|UniProtKB:F1NZP5, ECO:0000250|UniProtKB:Q96CP7}. reclassified-function P56500 Ucp2 Rattus norvegicus (Rat) 10116 Dicarboxylate carrier UCP2 (Mitochondrial uncoupling protein 2) (UCP 2) (Solute carrier family 25 member 8) The role of UCP2/SLC25A8 in mitochondrial proton conductance is a matter of debate. It was initially suggested that it mediates proton leak that increases net proton conductance in response to ROS such as reactive alkenals generated during fatty acid oxidation in mitochondria. By lowering the proton motive force, it would provide for feedback control of mitochondrial ROS metabolism limiting extensive ROS production and protecting cells against oxidative stress. This activity and its potential regulation by ubiquinones and nucleotides was disputed by later studies, which failed to reproduce the effect on proton conductance under physiological conditions. Rather than 'uncoupling' the link between electron transfer and ATP synthesis, it may couple metabolite transport to proton flux to allow for optimal ATP turnover. {ECO:0000250|UniProtKB:P55851, ECO:0000250|UniProtKB:P70406}. reclassified-function Q5J3N1 Vom1r92 Rattus norvegicus (Rat) 10116 Vomeronasal type-1 receptor 92 (M24 pheromone receptor) (Vomeronasal type-1 receptor B6) Was originally thought to originate from mouse (PubMed:9757043, Ref.1). {ECO:0000305}. reclassified-function Q5J3L7 Vom1r93 Rattus norvegicus (Rat) 10116 Vomeronasal type-1 receptor 93 (M21 pheromone receptor) (Pheromone receptor VN4) (Vomeronasal receptor 4) (Vomeronasal type-1 receptor B5) (mV1R3) Was originally (Ref.2, PubMed:9757043) thought to originate from mouse. {ECO:0000305}. reclassified-function Q08815 Rhizobium etli 29449 Uncharacterized 19.2 kDa protein in syrM 5'region (ORF2) Strain CNPAF512 was originally thought to originate from R.leguminosarum bv phaseoli. {ECO:0000305}. reclassified-function Q52784 Rhizobium etli 29449 Uncharacterized protein in rpoN-linked probable transport protein 5'region Strain CNPAF512 was originally thought to originate from R.leguminosarum bv phaseoli. {ECO:0000305}. reclassified-function P00462 nifH Rhizobium etli 29449 Nitrogenase iron protein (EC 1.18.6.1) (Nitrogenase Fe protein) (Nitrogenase component II) (Nitrogenase reductase) Plasmid p42d was originally thought to originate from Rhizobium leguminosarum (biovar phaseoli). {ECO:0000305}. reclassified-function P24543 recA Rhizobium etli 29449 Protein RecA (Recombinase A) Strain CNPAF512 was originally thought to originate from R.leguminosarum bv phaseoli. {ECO:0000305}. reclassified-function P49989 rpoN Rhizobium etli 29449 RNA polymerase sigma-54 factor Strain CNPAF512 was originally thought to originate from R.leguminosarum bv phaseoli. {ECO:0000305}. reclassified-function Q08812 syrM Rhizobium etli 29449 HTH-type transcriptional regulator SyrM (Symbiotic regulator) Strain CNPAF512 was originally thought to originate from R.leguminosarum bv phaseoli. {ECO:0000305}. reclassified-function P24154 nodA Rhizobium etli (strain ATCC 51251 / DSM 11541 / JCM 21823 / NBRC 15573 / CFN 42) 347834 Nodulation protein A (EC 2.3.1.-) Plasmid p42d was originally thought to originate from Rhizobium leguminosarum (biovar phaseoli). {ECO:0000305}. reclassified-function P24150 nodB Rhizobium leguminosarum bv. phaseoli 385 Chitooligosaccharide deacetylase (EC 3.5.1.-) (Nodulation protein B) Plasmid p42d was originally thought to originate from Rhizobium leguminosarum (biovar phaseoli). {ECO:0000305}. reclassified-function P24151 nodC Rhizobium leguminosarum bv. phaseoli 385 N-acetylglucosaminyltransferase (EC 2.4.1.-) (Nodulation protein C) Plasmid p42d was originally thought to originate from Rhizobium leguminosarum (biovar phaseoli). {ECO:0000305}. reclassified-function Q07607 dapA Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti) 382 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) (Protein MosA) Was originally thought to be involved in the biosynthesis of a rhizopine, catalyzing the conversion of scyllo-inosamine to 3-O-methyl-scyllo-inosamine (PubMed:8349559). However, does not show methyltransferase activity in the presence of scyllo-inosamine and S-adenosylmethionine (SAM), and does not interact with rhizopines and SAM (PubMed:18536061). {ECO:0000305|PubMed:18536061, ECO:0000305|PubMed:8349559}.; reclassified-function O69783 dapB Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti) 382 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q92R55 dapA Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) 266834 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P58326 dapB Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) 266834 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P20402 rolB Rhizobium rhizogenes (Agrobacterium rhizogenes) 359 Protein-tyrosine phosphatase RolB (ROL B protein) (EC 3.1.3.48) Was originally thought to release indoles from indoxyl-beta-glucosides. {ECO:0000305|PubMed:1915286}. reclassified-function B9J6R4 dapB Rhizobium rhizogenes (strain K84 / ATCC BAA-868) (Agrobacterium radiobacter) 311403 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5V3L9 dapA Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1) (Sphingomonas wittichii) 392499 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P26236 bchM Rhodobacter capsulatus (Rhodopseudomonas capsulata) 1061 Magnesium-protoporphyrin O-methyltransferase (EC 2.1.1.11) (Magnesium-protoporphyrin IX methyltransferase) Was originally thought to be involved in formation of the cyclopentone ring of protochlorophyllide from Mg-protoporphyrin IX monomethyl ester. {ECO:0000305|PubMed:6744416}. reclassified-function Q08384 modD Rhodobacter capsulatus (Rhodopseudomonas capsulata) 1061 Putative pyrophosphorylase ModD (EC 2.4.2.-) Was originally thought to be involved in molybdate transport. {ECO:0000305|PubMed:8491722}. reclassified-function Q08111 dus Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) 272942 Probable tRNA-dihydrouridine synthase (EC 1.3.1.-) (Nitrogen regulation protein nifR3) Was originally thought to be involved in the activation of nitrogen assimilatory genes. {ECO:0000305|PubMed:8355615}. reclassified-function Q7UJD7 dapB Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1) 243090 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6NCX8 dapB Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) 258594 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q07M65 dapA Rhodopseudomonas palustris (strain BisA53) 316055 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q07UT2 dapB Rhodopseudomonas palustris (strain BisA53) 316055 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q21CH6 dapB Rhodopseudomonas palustris (strain BisB18) 316056 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q13E66 dapB Rhodopseudomonas palustris (strain BisB5) 316057 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2J314 dapB Rhodopseudomonas palustris (strain HaA2) 316058 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B3Q978 dapB Rhodopseudomonas palustris (strain TIE-1) 395960 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B6IN13 dapA Rhodospirillum centenum (strain ATCC 51521 / SW) 414684 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C3PNF5 dapA Rickettsia africae (strain ESF-5) 347255 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C3PMI6 dapB Rickettsia africae (strain ESF-5) 347255 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8GNF1 dapA Rickettsia akari (strain Hartford) 293614 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8GMB6 dapB Rickettsia akari (strain Hartford) 293614 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8GWS1 dapA Rickettsia bellii (strain OSU 85-389) 391896 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8GV42 dapB Rickettsia bellii (strain OSU 85-389) 391896 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1RIJ3 dapA Rickettsia bellii (strain RML369-C) 336407 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q1RHE5 dapB Rickettsia bellii (strain RML369-C) 336407 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8EYZ4 dapA Rickettsia canadensis (strain McKiel) 293613 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8EXL6 dapB Rickettsia canadensis (strain McKiel) 293613 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q92I25 dapA Rickettsia conorii (strain ATCC VR-613 / Malish 7) 272944 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q92J79 dapB Rickettsia conorii (strain ATCC VR-613 / Malish 7) 272944 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q4ULR2 dapA Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi) 315456 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q4UKE7 dapB Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi) 315456 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8F1K3 dapA Rickettsia massiliae (strain Mtu5) 416276 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9AKQ3 dapA Rickettsia montanensis 33991 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C4K288 dapA Rickettsia peacockii (strain Rustic) 562019 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C4K0R8 dapB Rickettsia peacockii (strain Rustic) 562019 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O05969 dapA Rickettsia prowazekii (strain Madrid E) 272947 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9ZE14 dapB Rickettsia prowazekii (strain Madrid E) 272947 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9AKJ9 dapA Rickettsia rickettsii 783 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B0BXJ1 dapA Rickettsia rickettsii (strain Iowa) 452659 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8GS25 dapA Rickettsia rickettsii (strain Sheila Smith) 392021 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8GQX3 dapB Rickettsia rickettsii (strain Sheila Smith) 392021 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9AKE4 dapA Rickettsia typhi (strain ATCC VR-144 / Wilmington) 257363 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q68XM0 dapB Rickettsia typhi (strain ATCC VR-144 / Wilmington) 257363 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7JW41 dapB Rippkaea orientalis (strain PCC 8801 / RF-1) (Cyanothece sp. (strain PCC 8801)) 41431 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P24551 ANXA1 Rodentia sp 69158 Annexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Lipocortin I) [Cleaved into: Annexin Ac2-26] Was originally thought to originate from the sponge Geodia cydonium, but, on the basis of phylogenetic studies (Ref.2) it seems very probable that the DNA sequence coding for this protein comes from a rodent as agreed by the original authors (Ref.3). {ECO:0000305|PubMed:2146952}. reclassified-function P21563 INS Rodentia sp 69158 Insulin [Cleaved into: Insulin B chain; Insulin A chain] Was originally (PubMed:2531072) thought to originate from the sponge Geodia cydonium, but, on the basis of phylogenetic studies (Ref.2) it seems very probable that the DNA sequence coding for this protein comes from a rodent as agreed by the original authors (Ref.3). It is also doubtful that this is a real active insulin. {ECO:0000305|PubMed:2531072}. reclassified-function Q16BK4 dapA Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans) 375451 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q16CE5 dapB Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans) 375451 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1AZV2 dapB Rubrobacter xylanophilus (strain DSM 9941 / JCM 11954 / NBRC 16129 / PRD-1) 266117 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5LMK7 dapA Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) 246200 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5LLT7 dapB Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) 246200 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1GKJ6 dapB Ruegeria sp. (strain TM1040) (Silicibacter sp.) 292414 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1AVV3 dapA Ruthia magnifica subsp. Calyptogena magnifica 413404 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P19211 ANB1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Eukaryotic translation initiation factor 5A-2 (eIF-5A-2) (Anaerobically induced protein 1) (Hypusine-containing protein HP1) (eIF-4D) Was originally thought to be a translation initiation factor but further analysis (PubMed:19424157, PubMed:19338753) clearly suggests that it is involved in translation elongation and not translation initiation. {ECO:0000305|PubMed:641056}. reclassified-function Q00618 BET4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Geranylgeranyl transferase type-2 subunit alpha (EC 2.5.1.60) (GGTase-II-alpha) (Geranylgeranyl transferase type II subunit alpha) (PGGT) (Type II protein geranyl-geranyltransferase subunit alpha) (YPT1/SEC4 proteins geranylgeranyltransferase subunit alpha) Was originally thought to be MAD2. {ECO:0000305|PubMed:1651172}. reclassified-function P53194 BRP1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Uncharacterized protein BRP1 Was originally (PubMed:15855155) thought to function in polyamine resistance, hence the name BRP1, but this phenotype was later (PubMed:16374585) attributed to down-regulation of PMA1. {ECO:0000305|PubMed:15855155, ECO:0000305|PubMed:16374585}. reclassified-function P41735 CAT5 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 5-demethoxyubiquinone hydroxylase, mitochondrial (DMQ hydroxylase) (EC 1.14.99.60) (Catabolite repression protein 5) (NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase) (EC 1.14.13.253) (Ubiquinone biosynthesis monooxygenase COQ7) Was originally thought to be involved in carbon catabolite repression (PubMed:8557031). It has later been demonstrated that the catabolite-regulation defect in COQ7 mutants was a secondary effect of the respiration deficiency in ubiquinone-deficient mutants and could be rescued by the addition of exogenous ubiquinone (PubMed:9452453). {ECO:0000305|PubMed:8557031, ECO:0000305|PubMed:9452453}. reclassified-function P14724 CDC26 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Anaphase-promoting complex subunit CDC26 (Cell division control protein 26) Was originally thought to be a suppressor of CDC26. {ECO:0000305|PubMed:2690018}. reclassified-function P29465 CHS3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Chitin synthase 3 (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase 3) (Class-IV chitin synthase 3) Was originally thought that the N- and C-termini were extracellular (PubMed:16847258). However, more recent data suggests that the N- and C-termini are cytoplasmic (PubMed:28346351). {ECO:0000269|PubMed:16847258, ECO:0000269|PubMed:28346351}. reclassified-function P14747 CMP2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Serine/threonine-protein phosphatase 2B catalytic subunit A2 (EC 3.1.3.16) (Calcineurin A2) (Calmodulin-binding protein 2) Was originally thought to originate from a rabbit cDNA library and was known as protein phosphatase 2Bw (PP2Bw). {ECO:0000305|PubMed:2557079}. reclassified-function Q07560 CRD1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Cardiolipin synthase (CMP-forming) (CLS) (EC 2.7.8.41) Ref.3 sequence was originally thought to originate from Mycobacterium phlei. {ECO:0000305}. reclassified-function P25603 CWH36 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Putative uncharacterized protein CWH36 Product of a dubious gene prediction unlikely to encode a functional protein. Was originally (PubMed:7992502) thought to function in calcofluor white resistance, hence the name CWH36, but this phenotype was later (PubMed:14594803) attributed to the overlapping gene VMA9. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set. {ECO:0000305|PubMed:14594803, ECO:0000305|PubMed:24374639, ECO:0000305|PubMed:7992502}. reclassified-function P40526 DFG10 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Polyprenal reductase (EC 1.3.1.94) Was initially characterized as a polyprenol reductase, mediating the conversion of polyprenol into dolichol (PubMed:20637498). However, it was later shown to catalyze an intermediate step in this pathway and reduce polyprenal (PubMed:38821050). {ECO:0000269|PubMed:20637498, ECO:0000269|PubMed:38821050}. reclassified-function Q06143 DIC1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Mitochondrial dicarboxylate transporter (DTP) (Dicarboxylate carrier 1) Was previously identified as a homodimer (PubMed:10027973). However, subsequent studies reported that the human ortholog is a monomer. {ECO:0000269|PubMed:10027973, ECO:0000305}. reclassified-function Q08162 DIS3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Exosome complex exonuclease DIS3 (EC 3.1.13.-) (EC 3.1.26.-) (Chromosome disjunction protein 3) (Ribosomal RNA-processing protein 44) It was originally thought that there are multiple subunits in the exosome that have exonuclease activity but it was later shown (PubMed:17173052, PubMed:17174896) that only this DIS3/RRP44 subunit of the exosome core has this activity. {ECO:0000305|PubMed:9390555}. reclassified-function P33309 DOM34 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Protein DOM34 The Dom34-Hbs1 complex was initially thought to mediate endonucleolytic cleavage of the mRNA to release non-functional ribosomes and degrade damaged mRNAs. DOM34 was reported to have endoribonuclease activity (PubMed:16554824, PubMed:17889667). However, it was later shown that it is not the case (PubMed:19420139). {ECO:0000269|PubMed:16554824, ECO:0000269|PubMed:17889667, ECO:0000269|PubMed:19420139}. reclassified-function P32644 ECM32 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Putative ATP-dependent RNA helicase ECM32 (EC 3.6.4.13) (DNA helicase B) (Hcs B) (DNA helicase III) (Extracellular mutant protein 32) (Helicase 1) (scHelI) (Modulator of translation termination protein 1) ECM32 was originally identified as a DNA helicase and as component of DNA polymerase I. {ECO:0000305}. reclassified-function P53200 EFM5 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Protein-lysine N-methyltransferase EFM5 (EC 2.1.1.-) (Elongation factor methyltransferase 5) (N(6)-adenine-specific DNA methyltransferase-like 1) Was originally thought to be an N(6)-adenine-specific DNA methyltransferase based on primary sequence and predicted secondary structure. {ECO:0000305|PubMed:20582239}. reclassified-function P42935 ELP2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Elongator complex protein 2 (Gamma-toxin target 2) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:10024884, ECO:0000305|PubMed:11689709, ECO:0000305|PubMed:11904415, ECO:0000305|PubMed:15138274, ECO:0000305|PubMed:29332244}. reclassified-function Q02908 ELP3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Elongator complex protein 3 (EC 2.3.1.311) (Gamma-toxin target 3) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. Was reported to display histone acetyltransferase activity and to acetylate histone H3 preferentially at 'Lys-14', and H4 preferentially at 'Lys-8' (PubMed:10445034, PubMed:11904415, PubMed:15138274). However, it was later shown that the effect on histone acetylation and chromatin regulation is indirect and that the elongator complex is primarily involved in tRNA modification (PubMed:17018299, PubMed:18986986, PubMed:21912530). {ECO:0000269|PubMed:10445034, ECO:0000269|PubMed:11904415, ECO:0000269|PubMed:17018299, ECO:0000269|PubMed:18986986, ECO:0000269|PubMed:21912530, ECO:0000305|PubMed:10024884, ECO:0000305|PubMed:11689709, ECO:0000305|PubMed:15138274}. reclassified-function Q02884 ELP4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Elongator complex protein 4 (Gamma-toxin target 7) (HAT-associated protein 1) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:10024884, ECO:0000305|PubMed:11689709, ECO:0000305|PubMed:11904415, ECO:0000305|PubMed:15138274, ECO:0000305|PubMed:29332244}. reclassified-function Q04868 ELP6 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Elongator complex protein 6 (Gamma-toxin target 6) (HAT-associated protein 3) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:10024884, ECO:0000305|PubMed:11689709, ECO:0000305|PubMed:11904415, ECO:0000305|PubMed:29332244}. reclassified-function P25340 ERG4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Delta(24(24(1)))-sterol reductase ERG4 (EC 1.3.1.71) (C-24(28) sterol reductase ERG4) (Ergosterol biosynthetic protein 4) (Sterol Delta(24(28))-reductase ERG4) Was originally thought to be a transport protein. {ECO:0000305|PubMed:1882555}. reclassified-function P38071 ETR1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Enoyl-[acyl-carrier-protein] reductase, mitochondrial (EC 1.3.1.104) (2-enoyl thioester reductase) (Mitochondrial respiratory function protein 1) Was originally (PubMed:8195160) thought to be a nuclear protein involved in transcriptional regulation of genes required for the functional assembly of mitochondrial respiratory proteins. This was later proven not to be the case (PubMed:11509667). {ECO:0000305|PubMed:11509667, ECO:0000305|PubMed:8195160}. reclassified-function P15624 FRS1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) Was originally erroneously assigned as an alpha subunit. {ECO:0000305|PubMed:3049607}. reclassified-function P15625 FRS2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Phenylalanine--tRNA ligase alpha subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS) Was originally erroneously assigned as a beta subunit. {ECO:0000305|PubMed:3049607}. reclassified-function P31380 FUN30 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Chromatin remodeling protein FUN30 (EC 3.6.4.-) (Chromatin remodeler FUN30) Was initially reported to contain a CUE domain (PubMed:19956593). However, no CUE domain is predicted by prediction tools and the CUE-like region has no affinity for ubiquitinated histones (PubMed:20075079). {ECO:0000305|PubMed:19956593, ECO:0000305|PubMed:20075079}. reclassified-function P37020 GEF1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Anion/proton exchange transporter GEF1 (CLC protein GEF1) (ClC-A) (ClC-Y1) (Voltage-gated chloride channel) [Cleaved into: GEF1 N-terminal; GEF1 C-terminal] Was originally thought to be a voltage-gated ClC-type chloride channel. {ECO:0000305}. reclassified-function Q05584 GLO2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Hydroxyacylglutathione hydrolase, cytoplasmic isozyme (EC 3.1.2.6) (Glyoxalase II) (Glx II) The enzyme reported here differs from 2 previously reported yeast proteins with glyoxalase II activity both in molecular weight and in the kinetic parameters determined (Ref.5, Ref.6). The lower molecular masses and the much lower specific activities could indicate that these proteins were degradation products of either GLO2 or GLO4. In extracts of a yeast strain lacking both glyoxalase II genes no residual glyoxalase II activity was detected, indicating that there is no further protein with glyoxalase II activity present in yeast cells (PubMed:9261170). {ECO:0000269|PubMed:9261170, ECO:0000305|Ref.5, ECO:0000305|Ref.6}. reclassified-function Q12320 GLO4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Hydroxyacylglutathione hydrolase, mitochondrial (EC 3.1.2.6) (Glyoxalase II) (Glx II) The enzyme reported here differs from 2 previously reported yeast proteins with glyoxalase II activity both in molecular weight and in the kinetic parameters determined (Ref.5, Ref.6). The lower molecular masses and the much lower specific activities could indicate that these proteins were degradation products of either GLO2 or GLO4. In extracts of a yeast strain lacking both glyoxalase II genes no residual glyoxalase II activity was detected, indicating that there is no further protein with glyoxalase II activity present in yeast cells (PubMed:9261170). {ECO:0000269|PubMed:9261170, ECO:0000305|Ref.5, ECO:0000305|Ref.6}. reclassified-function Q00055 GPD1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Glycerol-3-phosphate dehydrogenase [NAD(+)] 1 (EC 1.1.1.8) Was originally thought to be GUT2, the FAD-dependent glycerol-3-phosphate dehydrogenase. {ECO:0000305|PubMed:1676389}. reclassified-function P36014 GPX1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Glutathione peroxidase-like peroxiredoxin 1 (EC 1.11.1.24) (EC 1.11.1.9) (Glutathione peroxidase homolog 1) (GPx 1) Was originally thought to be a glutathione peroxidase (PubMed:10480913) or a phospholipid hydroperoxide glutathione peroxidase (PubMed:11445588), but functions as an atypical 2-Cys peroxiredoxin using both glutathione and thioredoxin almost equally as reducing power instead (PubMed:20572871). {ECO:0000305|PubMed:10480913, ECO:0000305|PubMed:11445588, ECO:0000305|PubMed:20572871}. reclassified-function P38143 GPX2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Glutathione peroxidase-like peroxiredoxin 2 (EC 1.11.1.24) (Glutathione peroxidase homolog 2) (GPx 2) Was originally thought to be a glutathione peroxidase (PubMed:10480913) or a phospholipid hydroperoxide glutathione peroxidase (PubMed:11445588), but functions as an atypical 2-Cys peroxiredoxin using thioredoxin as reducing power instead (PubMed:16251189). {ECO:0000305|PubMed:10480913, ECO:0000305|PubMed:11445588, ECO:0000305|PubMed:16251189}. reclassified-function P53154 GUP1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Membrane-bound O-acyltransferase GUP1 (Glycerol uptake protein 1) Was originally thought to be involved in active uptake of glycerol driven by electrogenic proton symport (PubMed:10931309), but has later been shown to be an acyltransferase and that effects on glycerol transport may be indirect (PubMed:10694878, PubMed:15381122). {ECO:0000305|PubMed:10694878, ECO:0000305|PubMed:10931309, ECO:0000305|PubMed:15381122}. reclassified-function Q08929 GUP2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Membrane-bound O-acyltransferase GUP2 (Glycerol uptake protein 2) Was originally thought to be involved in active uptake of glycerol driven by electrogenic proton symport (PubMed:10931309), but has later been shown to be an acyltransferase and that effects on glycerol transport may be indirect (PubMed:15381122). {ECO:0000305|PubMed:10931309, ECO:0000305|PubMed:15381122}. reclassified-function P06174 HEM4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Uroporphyrinogen-III synthase (UROIIIS) (UROS) (EC 4.2.1.75) (Hydroxymethylbilane hydrolyase [cyclizing]) (Uroporphyrinogen-III cosynthase) Was originally thought to be involved in mitochondrial import. {ECO:0000305|PubMed:2834088}. reclassified-function P23301 HYP2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Eukaryotic translation initiation factor 5A-1 (eIF-5A-1) (Hypusine-containing protein HP2) (eIF-4D) Was originally thought (PubMed:641056) to be a translation initiation factor but further analysis (PubMed:19424157, PubMed:19338753) clearly suggests that it is involved in translation elongation and not translation initiation. subclass. {ECO:0000305|PubMed:641056}. reclassified-function P40581 HYR1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Glutathione peroxidase-like peroxiredoxin HYR1 (EC 1.11.1.24) (Glutathione peroxidase homolog 3) (GPx 3) (Hydrogen peroxide resistance protein 1) (Oxidant receptor peroxidase 1) (Phospholipid hydroperoxide glutathione peroxidase 3) (PHGPx3) Was originally thought to be a glutathione peroxidase (PubMed:10480913) or a phospholipid hydroperoxide glutathione peroxidase (PubMed:11445588), but functions as an atypical 2-Cys peroxiredoxin using thioredoxin as reducing power instead (PubMed:12437921). {ECO:0000305|PubMed:10480913, ECO:0000305|PubMed:11445588, ECO:0000305|PubMed:12437921}. reclassified-function P38874 IKI1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Elongator complex protein 5 (Gamma-toxin target 5) (HAT-associated protein 2) (Protein IKI1) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:10024884, ECO:0000305|PubMed:11689709, ECO:0000305|PubMed:11904415, ECO:0000305|PubMed:29332244}. reclassified-function Q06706 IKI3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Elongator complex protein 1 (Gamma-toxin target 1) (Protein IKI3) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:10024884, ECO:0000305|PubMed:11689709, ECO:0000305|PubMed:11904415, ECO:0000305|PubMed:29332244}. reclassified-function Q07532 IWR1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 RNA polymerase II nuclear localization protein IWR1 (Interacting with RNA polymerase II protein 1) Due to the effects of deletion on gene expression, was originally thought to be a general transcription factor (PubMed:19679657). Further studies clearly suggest that it is involved in nuclear localization of the RNA polymerase II complex (PubMed:21504834). {ECO:0000305|PubMed:19679657, ECO:0000305|PubMed:21504834}. reclassified-function P53128 MET13 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Methylenetetrahydrofolate reductase 2 (EC 1.5.1.53) (YmL45) Was originally thought to be a mitochondrial ribosomal protein. {ECO:0000305|PubMed:9151978}. reclassified-function P33441 MFT1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 THO complex subunit MFT1 (Mitochondrial fusion target protein 1) Was originally thought to be involved in mitochondrial protein import. {ECO:0000305|PubMed:8458428}. reclassified-function P41800 MMM1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Maintenance of mitochondrial morphology protein 1 (Mitochondrial outer membrane protein MMM1) (Yeast mitochondrial escape protein 6) Was originally proposed to be inserted into either the outer or inner mitochondrial membrane (PubMed:12972421, PubMed:8089172). More recent data indicates that it is instead inserted into the ER (PubMed:19556461). {ECO:0000305|PubMed:19556461}. reclassified-function P35719 MRP8 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Uncharacterized protein MRP8 Was originally thought to be a mitochondrial ribosomal protein. {ECO:0000305|PubMed:1574929}. reclassified-function Q01926 MRS2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Magnesium transporter MRS2, mitochondrial (RNA-splicing protein MRS2) Was originally (PubMed:1551905, PubMed:8252639) identified in genetic screens for bona fide RNA splicing factors, but it has later been shown that not the MRS2 protein per se but certain magnesium concentrations are essential for group II intron splicing. {ECO:0000305|PubMed:11544180}. reclassified-function Q05874 NNT1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Protein N-terminal and lysine N-methyltransferase EFM7 (EC 2.1.1.-) (Elongation factor methyltransferase 7) (Nicotinamide N-methyltransferase-like protein 1) Was originally thought to be a nicotinamide N-methyltransferase. {ECO:0000305|PubMed:12736687}. reclassified-function P39744 NOC2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Nucleolar complex protein 2 Was originally thought to be RAD4. {ECO:0000305|PubMed:2263475}. reclassified-function P06102 NOT3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 General negative regulator of transcription subunit 3 Was originally thought to be CDC39 (which is in fact NOT1). {ECO:0000305|PubMed:3018676}. reclassified-function P33751 PAD1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Flavin prenyltransferase PAD1, mitochondrial (EC 2.5.1.129) (Phenylacrylic acid decarboxylase 1) (PAD) Was initially thought to be a phenylacrylic acid decarboxylase (PubMed:11693915, PubMed:17766451). However, direct assays could not confirm decarboxylase activity (PubMed:12903944, PubMed:25852989). It has been shown that this enzyme synthesizes the essential cofactor for the associated decarboxylase FDC1. It is therefore thought that decarboxylation defects due to the disruption of this gene were in fact a secondary effect of inactive FDC1 decarboxylase missing its essential cofactor (PubMed:25647642). {ECO:0000269|PubMed:11693915, ECO:0000269|PubMed:12903944, ECO:0000269|PubMed:17766451, ECO:0000269|PubMed:25852989, ECO:0000305|PubMed:25647642}. reclassified-function P32521 PAN1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Actin cytoskeleton-regulatory complex protein PAN1 (Mitochondrial distribution of proteins protein 3) Was originally thought to be a subunit of PAB-dependent poly(A)-specific ribonuclease. {ECO:0000305|PubMed:1339314}. reclassified-function P53112 PEX14 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Peroxisomal membrane protein PEX14 (Peroxin-14) Was initially believed to associate peripherally with the peroxisomal membrane (PubMed:9094717). A later study however concluded it is an intrinsic membrane protein (PubMed:33323485). {ECO:0000269|PubMed:33323485, ECO:0000269|PubMed:9094717}. reclassified-function P39985 POL5 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 rRNA processing protein POL5 (rDNA transcriptional regulator POL5) Was originally thought to belong to the DNA polymerase type-B family based on conserved motifs (PubMed:12093911). Has later been shown to be unrelated to B class DNA polymerases. The observation of a low level of polymerase activity in vitro, which is not required for its essential cellular function, may require further validation (PubMed:12695662). {ECO:0000305|PubMed:12093911, ECO:0000305|PubMed:12695662}. reclassified-function P38796 PPE1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Protein phosphatase methylesterase 1 (PME-1) (EC 3.1.1.89) (Yms2) Was originally thought to be a mitochondrial ribosomal protein (PubMed:9151978), but has not been identified in the structure of the yeast mitoribosome (PubMed:28154081). {ECO:0000305|PubMed:28154081, ECO:0000305|PubMed:9151978}. reclassified-function P26570 PPZ1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Serine/threonine-protein phosphatase PP-Z1 (EC 3.1.3.16) Was originally thought to originate from a rabbit cDNA library and was known as protein phosphatase Z (PP-Z). {ECO:0000305|PubMed:2166691}. reclassified-function Q08931 PRM3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Pheromone-regulated membrane protein 3 Was originally shown to be localized in the inner nuclear membrane by using a truncated protein (PubMed:12514182). Was used as an inner nuclear membrane marker (PubMed:17996101, PubMed:18660802, PubMed:19369416). However, more recent studies showed that it is localized in the nuclear outer membrane, which is consistent with a function in the initiation of nuclear fusion (PubMed:19297527, PubMed:19570912). {ECO:0000305|PubMed:12514182}. reclassified-function P00128 QCR7 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Cytochrome b-c1 complex subunit 7, mitochondrial (Complex III subunit 7) (Complex III subunit VII) (Ubiquinol-cytochrome c oxidoreductase subunit 7) (Ubiquinol-cytochrome c reductase 14 kDa protein) Was originally thought to be the ubiquinone-binding protein (QP-C). {ECO:0000305}. reclassified-function P23248 RPS1B Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Small ribosomal subunit protein eS1B (40S ribosomal protein S1-B) (RP10B) Was originally thought to be MFT1, the mitochondrial fusion target protein. {ECO:0000305|PubMed:2017143}. reclassified-function P38792 RRP4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Exosome complex component RRP4 (Ribosomal RNA-processing protein 4) Was originally (PubMed:9390555, PubMed:8600032) thought to have exonuclease activity but it was later shown (PubMed:17173052, PubMed:17174896) that only DIS3/RRP44 subunit of the exosome core has this activity. {ECO:0000305}. reclassified-function P38332 RRT2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Diphthine methyltransferase (EC 3.1.1.97) (Diphthamide biosynthesis protein 7) (Endosomal recycling protein 1) (Regulator of rDNA transcription protein 2) Was originally (PubMed:19965467) thought to be required for the first step of diphthamide biosynthesis but further studies (PubMed:22188241, PubMed:23468660) clearly suggest that it is involved in the third step of diphthamide biosynthesis. {ECO:0000305|PubMed:19965467, ECO:0000305|PubMed:22188241, ECO:0000305|PubMed:23468660}. reclassified-function P46948 SKI6 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Exosome complex component SKI6 (Extracellular mutant protein 20) (Ribosomal RNA-processing protein 41) (Superkiller protein 6) Was originally thought to have exonuclease activity but it was later shown (PubMed:17173052, PubMed:17174896) that only DIS3/RRP44 subunit of the exosome core has this activity. {ECO:0000305|PubMed:9390555}. reclassified-function Q12093 SLM3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Mitochondrial tRNA-specific 2-thiouridylase 1 (EC 2.8.1.13) (Mitochondrial translation optimization protein 2) (Synthetic lethal with MSS4 3) Was originally thought to be a 5-methylaminomethyl-2-methyltransferase involved in tRNA modification. {ECO:0000305}. reclassified-function P39929 SNF7 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Vacuolar-sorting protein SNF7 (DOA4-independent degradation protein 1) (Sucrose nonfermenting protein 7) (Vacuolar protein-sorting-associated protein 32) Was originally thought to be a nuclear protein and mutations were shown to prevent full derepression of the SUC2 (invertase) gene. {ECO:0000305|PubMed:8224817}. reclassified-function P39986 SPF1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Endoplasmic reticulum transmembrane helix translocase (EC 7.4.2.-) (Complexed with DOR1 protein 1) (Endoplasmic reticulum P5A-ATPase) (Sensitivity to the P.farinosa killer toxin protein 1) Was initially thought to mediate ion transport such as calcium or manganese (PubMed:12058017, PubMed:24392018). However, different publications have shown that it does not act as an ion transporter (PubMed:22745129, PubMed:32353073, PubMed:32973005). Specifically binds moderately hydrophobic transmembrane with short hydrophilic lumenal domains that misinsert into the endoplasmic reticulum (PubMed:32973005). {ECO:0000269|PubMed:12058017, ECO:0000269|PubMed:22745129, ECO:0000269|PubMed:24392018, ECO:0000269|PubMed:32353073, ECO:0000269|PubMed:32973005}. reclassified-function P32363 SPT14 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit (GPI-GlcNAc transferase complex subunit GPI3) (GPI-GnT subunit GPI3) (EC 2.4.1.198) (GlcNAc-PI synthesis protein) Was originally thought to be involved in transcription. {ECO:0000305|PubMed:1660567}. reclassified-function P32914 SPT4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Transcription elongation factor SPT4 (Chromatin elongation factor SPT4) Was originally thought to be involved in the transcription initiation step. {ECO:0000305|PubMed:8483459}. reclassified-function Q00947 STP1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Transcription factor STP1 Was originally thought to be an amino-acid permease. {ECO:0000305|PubMed:1803818}. reclassified-function P53230 TAM41 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Phosphatidate cytidylyltransferase, mitochondrial (EC 2.7.7.41) (CDP-diacylglycerol synthase) (CDP-DAG synthase) (Mitochondrial import protein MMP37) (Mitochondrial matrix protein of 37 kDa) (Mitochondrial translocator assembly and maintenance protein 41) Was initially identified as protein involved in the translocation of transit peptide-containing proteins across the mitochondrial inner membrane by its role in maintaining the integrity and stability of the inner membrane translocase TIM23 complex (PubMed:16790493, PubMed:16943180). It has later been shown that this phenotype can be attributed to the pleiotropic effects of mitochondria lacking cardiolipin (PubMed:19114592). {ECO:0000305|PubMed:16790493, ECO:0000305|PubMed:16943180, ECO:0000305|PubMed:19114592}. reclassified-function P48561 TRF5 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Poly(A) RNA polymerase protein 1 (EC 2.7.7.19) (Topoisomerase 1-related protein TRF5) Was originally thought to have DNA polymerase activity. {ECO:0000305}. reclassified-function Q04235 TRM12 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 tRNA wybutosine-synthesizing protein 2 (tRNA-yW-synthesizing protein 2) (EC 2.5.1.114) (tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase) Was originally thought to be a methyltransferase. {ECO:0000305|PubMed:16005430}. reclassified-function Q04311 VMS1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 tRNA endonuclease VMS1 (EC 3.1.-.-) (VCP/CDC48-associated mitochondrial stress-responsive protein 1) Was initially thought to act as an atypical peptidyl-tRNA hydrolase (PubMed:29632312). However, it was later shown to act as a nuclease that cleaves off the terminal 3'-CCA nucleotides from the tRNA part of polypeptidyl-tRNAs (PubMed:31189955). {ECO:0000269|PubMed:29632312, ECO:0000269|PubMed:31189955}. reclassified-function P38838 WSS1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 DNA-dependent metalloprotease WSS1 (EC 3.4.24.-) (DNA damage response protein WSS1) (SUMO-dependent isopeptidase WSS1) (Weak suppressor of SMT3 protein 1) Was initially reported to be a SUMO-dependent isopeptidase (PubMed:20516210), but this activity could not be confirmed (PubMed:24998930). {ECO:0000305|PubMed:20516210, ECO:0000305|PubMed:24998930}. reclassified-function Q04013 YHM2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Citrate/oxoglutarate carrier protein (Coc1p) (Mitochondrial DNA replication protein YHM2) Was originally proposed to function in mitochondrial DNA replication and maintenance. {ECO:0000303|PubMed:9742088}. reclassified-function P19955 YMR31 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Alpha-ketoglutarate dehydrogenase subunit 4, mitochondrial (alpha-KGDH subunit 4) (2-oxoglutarate dehydrogenase complex component 4) (OGDHC subunit 4) Was originally identified in the small subunit (28S) of mitochondrial ribosomes that were purified on sucrose gradients (PubMed:2693936). This observation has been challenged by experiments showing YMR31 copurification with the oxoglutarate dehydrogenase complex (OGDC), also called alpha-ketoglutarate dehydrogenase complex (KGDH). Both mitochondrial ribosome 28S subunit and OGDC have a similar size and OGDC is highly abundant, therefore OGDC has been found to contaminate ribosomal preparations performed by sequential centrifugation steps (PubMed:25165143). In addition, YMR31 could not be located in the structure of the yeast mitochondrial ribosome, supporting the hypothesis that it is not a mitoribosomal protein. {ECO:0000269|PubMed:25165143, ECO:0000269|PubMed:2693936, ECO:0000305}. reclassified-function P43587 YPI1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Type 1 phosphatases regulator YPI1 Was originally (PubMed:14506263) thought to be an inhibitor of type 1 phosphatases using in vitro experiments, but further in vivo experiments (PubMed:18172024) showed that it was rather an activator of these phosphatases. {ECO:0000305|PubMed:14506263, ECO:0000305|PubMed:18172024}. reclassified-function Q21HE7 dapA Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) 203122 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q21H39 dapB Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) 203122 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q01040 68 Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri) 10383 Packaging protein UL32 Was originally thought to be an envelope glycoprotein. {ECO:0000305}. reclassified-function Q2S3M1 dapA Salinibacter ruber (strain DSM 13855 / M31) 309807 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B5F744 dapB Salmonella agona (strain SL483) 454166 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A9MHQ2 dapA Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980) 41514 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A9MR41 dapB Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980) 41514 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q57TJ7 dapB Salmonella choleraesuis (strain SC-B67) 321314 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B5FHF8 dapB Salmonella dublin (strain CT_02021853) 439851 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B5R1Q4 dapB Salmonella enteritidis PT4 (strain P125109) 550537 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B5RG99 dapB Salmonella gallinarum (strain 287/91 / NCTC 13346) 550538 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B4TIG4 dapB Salmonella heidelberg (strain SL476) 454169 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B4T6J1 dapB Salmonella newport (strain SL254) 423368 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B5BB16 dapA Salmonella paratyphi A (strain AKU_12601) 554290 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B5BL41 dapB Salmonella paratyphi A (strain AKU_12601) 554290 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5PLS1 dapA Salmonella paratyphi A (strain ATCC 9150 / SARB42) 295319 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5PIL9 dapB Salmonella paratyphi A (strain ATCC 9150 / SARB42) 295319 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A9MYI6 dapB Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) 1016998 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C0Q4K5 dapB Salmonella paratyphi C (strain RKS4594) 476213 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B4TR62 dapA Salmonella schwarzengrund (strain CVM19633) 439843 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B4TWQ6 dapB Salmonella schwarzengrund (strain CVM19633) 439843 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8Z4R8 dapA Salmonella typhi 90370 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8Z9L9 dapB Salmonella typhi 90370 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P41780 apbE Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 FAD:protein FMN transferase (EC 2.7.1.180) (Flavin transferase) Was originally thought to be involved in synthesis of the pyrimidine moiety of thiamine and/or in metabolism of Fe-S clusters. {ECO:0000303|PubMed:12486045, ECO:0000303|PubMed:21148731, ECO:0000303|PubMed:9473043}. reclassified-function Q05632 cbiT Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (EC 2.1.1.196) Was originally thought to be a precorrin-8w decarboxylase. {ECO:0000305}. reclassified-function P26219 cdh Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 CDP-diacylglycerol pyrophosphatase (EC 3.6.1.26) (CDP-diacylglycerol phosphatidylhydrolase) (CDP-diglyceride hydrolase) Was originally thought to be a UDP-sugar hydrolase. {ECO:0000305|PubMed:2548058}. reclassified-function Q7CQC4 cmoA Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Carboxy-S-adenosyl-L-methionine synthase (Cx-SAM synthase) (EC 2.1.3.-) Was originally thought to be a transferase that mediates the conversion of mo5U(34) to cmo5U(34) in tRNAs. {ECO:0000305|PubMed:15383682}. reclassified-function Q8ZN71 dapA Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8ZRX8 dapB Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P0A1H1 dsbI Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Protein-disulfide oxidoreductase DsbI Was originally given the gene name dsbB; however another gene encoding a dsbB more closely related to that of the characterized E.coli protein bears this gene name (DSBB_SALTY, AC Q8XG65). {ECO:0000305}. reclassified-function P30752 lolB Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Outer-membrane lipoprotein LolB Was originally thought to be involved in delta-aminolevulinic acid biosynthesis. {ECO:0000305}. reclassified-function P0A1X4 lpxD Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (UDP-3-O-(3-OHC14)-GlcN N-acyltransferase) (EC 2.3.1.191) (UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase) Was originally thought to be involved in transcription. {ECO:0000305}. reclassified-function P37169 murJ Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Probable lipid II flippase MurJ Was originally (PubMed:2680969) thought to be involved in mouse virulence. It was later shown that the mutation responsible for the virulence phenotype maps to nearby genes (PubMed:8288531). {ECO:0000305|PubMed:2680969, ECO:0000305|PubMed:8288531}. reclassified-function P74879 pduW Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Propionate kinase PduW (EC 2.7.2.15) Was originally (Ref.1) thought to be AckA. {ECO:0000305}. reclassified-function P40676 slyA Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Transcriptional regulator SlyA (Cytolysin SlyA) (Salmolysin) Was originally thought to be a toxin with hemolytic and cytolytic activity but this was later refuted. {ECO:0000305|PubMed:8290552, ECO:0000305|PubMed:8544813}. reclassified-function Q7CQM5 ssrB Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Response regulator SsrB The Glu-56 mutant was reported as constitutively active (PubMed:28704543, PubMed:30355489). However the mutant was found to be defective in DNA-binding by a later study and it was argued that plasmid-expression of Glu-56 leads to inappropriate regulation (PubMed:31033442). {ECO:0000269|PubMed:28704543, ECO:0000269|PubMed:30355489, ECO:0000269|PubMed:31033442}. reclassified-function P37458 wzyE Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Probable ECA polymerase Was originally thought to be WecF, the 4-alpha-L-fucosyltransferase. {ECO:0000305}. reclassified-function P37168 yceM Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Putative oxidoreductase YceM (EC 1.-.-.-) Was originally (PubMed:2680969) thought to be involved in mouse virulence. It was later shown that the mutation responsible for the virulence phenotype maps to nearby genes (PubMed:8288531). {ECO:0000305|PubMed:2680969, ECO:0000305|PubMed:8288531}. reclassified-function P25852 zraR Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Transcriptional regulatory protein ZraR Was originally thought to be involved in the regulation of the labile hydrogenase activity. {ECO:0000305|PubMed:1756170}. reclassified-function P37461 zraS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 99287 Sensor histidine kinase ZraS (EC 2.7.13.3) Was originally thought to be involved in the regulation of the labile hydrogenase activity. {ECO:0000305|PubMed:1756170}. reclassified-function E1WAB5 orgA Salmonella typhimurium (strain SL1344) 216597 Oxygen-regulated invasion protein OrgA Was originally thought to be a longer protein that encodes what is now known to be OrgA and OrgB. {ECO:0000305|PubMed:8063389}. reclassified-function E1WAB4 sctL1 Salmonella typhimurium (strain SL1344) 216597 SPI-1 type 3 secretion system stator protein (T3SS-1 stator protein) (Oxygen-regulated invasion protein OrgB) Was originally thought to be a longer protein that encodes what is now known to be OrgA and OrgB. {ECO:0000305|PubMed:10816487, ECO:0000305|PubMed:8063389}. reclassified-function P79912 LDHA Sceloporus woodi (Florida scrub lizard) 59726 L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) Was originally thought to originate from S.undulatus. {ECO:0000305|PubMed:8666293}. reclassified-function P79913 LDHB Sceloporus woodi (Florida scrub lizard) 59726 L-lactate dehydrogenase B chain (LDH-B) (EC 1.1.1.27) Was originally thought to originate from S.undulatus. {ECO:0000305|PubMed:8666293}. reclassified-function C1L7Y4 Schistosoma japonicum (Blood fluke) 6182 Annexin A13 (Annexin) (Annexin XIII) (SjANX A13) The nomenclature classifies invertebrate (including schistosomes) annexins as group B. However, there are inconsistencies to this naming system including this protein. It was originally named as group A (vertebrates) annexin, the name which is still currently maintained. {ECO:0000305|PubMed:38049816}. reclassified-function P38658 Schistosoma mansoni (Blood fluke) 6183 Probable protein disulfide-isomerase ER-60 (EC 5.3.4.1) (ERP60) Was originally thought to be a phosphatidylinositol 4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha). {ECO:0000305}. reclassified-function O01374 Schistosoma mansoni (Blood fluke) 6183 Cytochrome b-c1 complex subunit 7 (Complex III subunit 7) (Complex III subunit VII) (Ubiquinol-cytochrome c reductase complex 14 kDa protein) Was originally thought to be the ubiquinone-binding protein (QP-C). {ECO:0000305}. reclassified-function Q10217 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Putative acyl carrier protein, mitochondrial (ACP) Was previously considered as a subunit of the NADH dehydrogenase of the mitochondrial respiratory chain complex I. Due to lack of 38 of the other 40 subunits that are present in that complex in mammals, this attribution is unlikely (PubMed:1518044). {ECO:0000305}. reclassified-function O94500 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 NADH-ubiquinone oxidoreductase 51 kDa subunit homolog SPBC18E5.10, mitochondrial (EC 1.6.-.-) Was previously considered as a subunit of the NADH dehydrogenase of the mitochondrial respiratory chain complex I. Due to lack of 38 of the other 40 subunits that are present in that complex in mammals, this attribution is unlikely. {ECO:0000305}. reclassified-function O13691 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 NADH-ubiquinone oxidoreductase 24 kDa subunit homolog C11E3.12, mitochondrial (EC 1.6.-.-) Was previously considered as a subunit of the NADH dehydrogenase of the mitochondrial respiratory chain complex I. Due to lack of 38 of the other 40 subunits that are present in that complex in mammals, this attribution is unlikely. {ECO:0000305}. reclassified-function Q09840 aah2 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 4-alpha-glucanotransferase aah2 (EC 2.4.1.25) Was originally thought to exhibit alpha-amylase activity, but this activity is not detectable in S.pombe cell lysates or culture media. {ECO:0000305}. reclassified-function Q9Y7S9 aah3 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 4-alpha-glucanotransferase aah3 (EC 2.4.1.25) Was originally thought to exhibit alpha-amylase activity, but this activity is not detectable in S.pombe cell lysates or culture media. {ECO:0000305|PubMed:16751704}. reclassified-function Q10315 bur6 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Transcription regulator complex subunit bur6 SPAC17G8.03c was previously identified as the homolog of budding yeast DBP3 in fission yeast (PubMed:15388803). However, it was further demonstrated that SPCC16C4.22 is the true ortholog of DBP3 (PubMed:29109278). {ECO:0000269|PubMed:15388803, ECO:0000269|PubMed:29109278}. reclassified-function P22189 cta3 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Sodium/potassium exporting P-type ATPase cta3 (EC 7.2.2.3) (Cation translocating ATPase 3) Was originally thought to be a calcium transporter (PubMed:2145281). However later studies indicate that it functions as a sodium/potassium exporter (PubMed:11932440, PubMed:19757095). {ECO:0000269|PubMed:11932440, ECO:0000269|PubMed:19757095, ECO:0000269|PubMed:2145281}. reclassified-function C6Y4D0 dpb3 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 DNA polymerase epsilon subunit C (DNA polymerase II subunit C) SPAC17G8.03c was previously identified as the homolog of budding yeast DBP3 in fission yeast. However, it was further demonstrated that SPCC16C4.22 is the true ortholog of DBP3. {ECO:0000269|PubMed:29109278}. reclassified-function O59704 elp1 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Elongator complex protein 1 The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:O95163}. reclassified-function O94533 elp2 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Elongator complex protein 2 The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q6IA86}. reclassified-function O14023 elp3 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function Q9USP1 elp4 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Elongator complex protein 4 The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}. reclassified-function O74385 elp6 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Elongator complex protein 6 homolog The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:29332244}. reclassified-function Q9URU6 exg1 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Glucan endo-1,6-beta-glucosidase exg1 (EC 3.2.1.75) Was previously annotated as a exo-1,3-beta-glucanase, however S.pombe does not exhibit this activity. {ECO:0000305|PubMed:20852022}. reclassified-function O59858 gpx1 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Glutathione peroxidase-like peroxiredoxin gpx1 (EC 1.11.1.24) (Glutathione peroxidase homolog) (GPx) (Thioredoxin peroxidase gpx1) Was originally thought to be a glutathione peroxidase (PubMed:10455235), but functions as an atypical 2-Cys peroxiredoxin using thioredoxin as reducing power instead (PubMed:18162174). {ECO:0000305|PubMed:10455235, ECO:0000305|PubMed:18162174}. reclassified-function O94495 iki1 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Elongator complex protein 5 (Protein iki1) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000305|PubMed:29332244}. reclassified-function O14154 mde5 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Putative cell wall assembly protein mde5 (Mei4-dependent protein 5) (Meiotic expression up-regulated protein 30) Was originally thought to exhibit alpha-amylase activity, but this activity is not detectable in S.pombe cell lysates or culture media. {ECO:0000305}. reclassified-function O42918 meu7 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Putative cell wall assembly protein meu7 (Meiotic expression up-regulated protein 7) Was originally thought to exhibit alpha-amylase activity, but this activity is not detectable in S.pombe cell lysates or culture media. {ECO:0000305|PubMed:16751704}. reclassified-function Q92344 pfl8 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Putative cell agglutination protein pfl8 (Adhesin pfl8) (Pombe flocculin 8) (Sim4-mal2-associated protein 5) Was originally thought to be a kinetochore protein, but co-localization has not been confirmed (PubMed:16079914). A more recent study identified it as a secreted protein (PubMed:16823372). {ECO:0000305|PubMed:16079914, ECO:0000305|PubMed:16823372}. reclassified-function P40999 pmt1 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 tRNA (cytosine(38)-C(5))-methyltransferase (EC 2.1.1.204) (DNA (cytosine-5)-methyltransferase-like protein 2) (Dnmt2) (M.SpomI) (SpIM.SpoI) Was originally thought not to have cytosine-5 methyltransferase activity, and this was attributed to the insertion of a Ser residue between the Pro-Cys motif found at the active site of C5 MTases (PubMed:8636983). When this serine is deleted it becomes catalytically active and recognizes and methylates the sequence CC[AT]GG. This was in agreement with S.pombe lacking m5C DNA-methylation. However, it has later been shown that it has tRNA-methyltransferase activity despite this sequence variation (PubMed:23074192). {ECO:0000305|PubMed:23074192, ECO:0000305|PubMed:8636983}. reclassified-function O13795 pof8 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 La-related protein 7 homolog Was initially thought to contain a F-box domain (PubMed:15147268). However, such a domain is not detectable by any prediction tool. {ECO:0000269|PubMed:15147268, ECO:0000305}. reclassified-function Q9P380 ptr2 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Probable peptide transporter ptr2 (Peptide permease ptr2) Was originally (PubMed:7919993) reported to be isolated from an A.thaliana cv. Landsberg erecta cDNA library. {ECO:0000305|PubMed:7919993}. reclassified-function Q09127 rpl1001 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Large ribosomal subunit protein uL16A (60S ribosomal protein L10-A) (QM protein homolog) (SpQM) Was originally thought to be a transcription factor that may bind Jun homologs such as GCN4 and YAP-1, and which may inhibit DNA binding and transactivation by Jun homologs. {ECO:0000305|PubMed:8621081}. reclassified-function P40389 rrg1 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Protein-lysine N-methyltransferase rrg1 (EC 2.1.1.-) (Elongation factor methyltransferase 2) (Rapid response to glucose protein 1) Was originally (PubMed:8048925) thought to be induced by UV light and alkylating agents. The authors from PubMed:11861905 have found from further investigation that it is induced and regulated by glucose. {ECO:0000305|PubMed:11861905, ECO:0000305|PubMed:8048925}. reclassified-function P27638 spk1 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Mitogen-activated protein kinase spk1 (MAP kinase spk1) (MAPK) (EC 2.7.11.24) Was originally thought to confer resistance to staurosporine. {ECO:0000305|PubMed:1899230}. reclassified-function Q10274 teb1 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Telobox protein 1 (Meiotically up-regulated gene 152 protein) Was initially reported as a potential telomeric factor as it harbors two helix-loop-helix dsDNA binding domains which are recurrently found in telomeric proteins. However, teb1 was shown to have higher affinity for the vertebrate telomere repeat, TTAGGG, than to fission yeast telomere repeats in vitro. {ECO:0000269|PubMed:10572167, ECO:0000269|PubMed:10606652}. reclassified-function Q42598 thrc Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 Threonine synthase (TS) (EC 4.2.3.1) Was originally (Ref.1) thought to originate from A.thaliana. {ECO:0000305}. reclassified-function P48012 BUD3 Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis) 27300 Bud site selection protein 3 Was originally thought to be 3-isopropylmalate dehydrogenase (LEU2). {ECO:0000305|PubMed:7597851}. reclassified-function A8G9M8 dapB Serratia proteamaculans (strain 568) 399741 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1S8K1 dapB Shewanella amazonensis (strain ATCC BAA-1098 / SB2B) 326297 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3D5N2 dapA Shewanella baltica (strain OS155 / ATCC BAA-1091) 325240 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A3D7S3 dapB Shewanella baltica (strain OS155 / ATCC BAA-1091) 325240 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6WPI6 dapA Shewanella baltica (strain OS185) 402882 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6WRU0 dapB Shewanella baltica (strain OS185) 402882 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A9L573 dapA Shewanella baltica (strain OS195) 399599 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A9L0Q8 dapB Shewanella baltica (strain OS195) 399599 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8E724 dapA Shewanella baltica (strain OS223) 407976 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8E4S9 dapB Shewanella baltica (strain OS223) 407976 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q12NF7 dapA Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) 318161 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q12QJ4 dapB Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) 318161 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q082V3 dapA Shewanella frigidimarina (strain NCIMB 400) 318167 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q086I8 dapB Shewanella frigidimarina (strain NCIMB 400) 318167 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0TQB8 dapB Shewanella halifaxensis (strain HAW-EB4) 458817 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A3QGV8 dapB Shewanella loihica (strain ATCC BAA-1088 / PV-4) 323850 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8EFT7 dapA Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1) 211586 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8EHS7 dapB Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1) 211586 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8H415 dapA Shewanella pealeana (strain ATCC 700345 / ANG-SQ1) 398579 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8H756 dapB Shewanella pealeana (strain ATCC 700345 / ANG-SQ1) 398579 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8CMS5 dapA Shewanella piezotolerans (strain WP3 / JCM 13877) 225849 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8CKF7 dapB Shewanella piezotolerans (strain WP3 / JCM 13877) 225849 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A4Y644 dapA Shewanella putrefaciens (strain CN-32 / ATCC BAA-453) 319224 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4Y9M3 dapB Shewanella putrefaciens (strain CN-32 / ATCC BAA-453) 319224 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8FYT6 dapB Shewanella sediminis (strain HAW-EB3) 425104 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A0KVS0 dapA Shewanella sp. (strain ANA-3) 94122 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0KTT2 dapB Shewanella sp. (strain ANA-3) 94122 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0HHQ6 dapA Shewanella sp. (strain MR-4) 60480 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q0HLM3 dapB Shewanella sp. (strain MR-4) 60480 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0HU08 dapA Shewanella sp. (strain MR-7) 60481 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q0HY04 dapB Shewanella sp. (strain MR-7) 60481 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1RKF2 dapA Shewanella sp. (strain W3-18-1) 351745 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1RGQ6 dapB Shewanella sp. (strain W3-18-1) 351745 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1KRS8 dapB Shewanella woodyi (strain ATCC 51908 / MS32) 392500 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2TXQ4 dapA Shigella boydii serotype 18 (strain CDC 3083-94 / BS512) 344609 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B2U250 dapB Shigella boydii serotype 18 (strain CDC 3083-94 / BS512) 344609 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q31Y13 dapA Shigella boydii serotype 4 (strain Sb227) 300268 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q326J2 dapB Shigella boydii serotype 4 (strain Sb227) 300268 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q32D87 dapA Shigella dysenteriae serotype 1 (strain Sd197) 300267 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q32K66 dapB Shigella dysenteriae serotype 1 (strain Sd197) 300267 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P0A6L3 dapA Shigella flexneri 623 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q83SQ9 dapB Shigella flexneri 623 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0T239 dapA Shigella flexneri serotype 5b (strain 8401) 373384 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3YZ74 dapA Shigella sonnei (strain Ss046) 300269 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3Z5X9 dapB Shigella sonnei (strain Ss046) 300269 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5WGQ4 dapB Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii) 66692 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P26780 Sinapis alba (White mustard) (Brassica hirta) 3728 Defensin-like protein 2 (MTI-2) (Trypsin inhibitor 2) Was initially thought (PubMed:7750566, PubMed:1451776) to be a protease inhibitor. {ECO:0000305}. reclassified-function P40115 PHR1 Sinapis alba (White mustard) (Brassica hirta) 3728 Cryptochrome-1 (Blue light photoreceptor) Was originally thought to be a DNA photolyase. {ECO:0000305|PubMed:8252071}. reclassified-function C3MBY7 dapB Sinorhizobium fredii (strain NBRC 101917 / NGR234) 394 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6UEW2 dapB Sinorhizobium medicae (strain WSM419) (Ensifer medicae) 366394 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P29938 Sinorhizobium sp 42445 Uncharacterized protein in cobV 5'region (ORF1) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29939 Sinorhizobium sp 42445 Uncharacterized transporter in cobO 3'region (ORF6) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29942 Sinorhizobium sp 42445 Probable membrane transporter protein ORF9 (ORF9) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29941 Sinorhizobium sp 42445 Uncharacterized 19.2 kDa protein in cobO 3'region (ORF8) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29940 Sinorhizobium sp 42445 PEMT/PEM2 methyltransferase family protein (EC 2.1.1.-) (ORF7) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29944 Sinorhizobium sp 42445 Uncharacterized 19.0 kDa protein in cobS 5'region (ORF2) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29943 Sinorhizobium sp 42445 Uncharacterized protein in cobS 5'region (ORF1) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21631 cobA Sinorhizobium sp 42445 Uroporphyrinogen-III C-methyltransferase (Urogen III methylase) (EC 2.1.1.107) (S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase) (SUMT) (Uroporphyrinogen III methylase) (UROM) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21632 cobB Sinorhizobium sp 42445 Hydrogenobyrinate a,c-diamide synthase (EC 6.3.5.9) (Hydrogenobyrinic acid a,c-diamide synthase) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21633 cobC Sinorhizobium sp 42445 Threonine-phosphate decarboxylase (EC 4.1.1.81) (L-threonine-O-3-phosphate decarboxylase) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21634 cobD Sinorhizobium sp 42445 Cobalamin biosynthesis protein CobD Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21635 cobE Sinorhizobium sp 42445 Protein CobE Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21636 cobF Sinorhizobium sp 42445 Precorrin-6A synthase [deacetylating] (EC 2.1.1.152) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21637 cobG Sinorhizobium sp 42445 Precorrin-3B synthase (EC 1.14.13.83) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21638 cobH Sinorhizobium sp 42445 Precorrin-8X methylmutase (EC 5.4.99.61) (HBA synthase) (Precorrin isomerase) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21639 cobI Sinorhizobium sp 42445 Precorrin-2 C(20)-methyltransferase (EC 2.1.1.130) (S-adenosyl-L-methionine--precorrin-2 methyltransferase) (SP2MT) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21640 cobJ Sinorhizobium sp 42445 Precorrin-3B C(17)-methyltransferase (Precorrin-3 methylase) (Precorrin-3 methyltransferase) (EC 2.1.1.131) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21920 cobK Sinorhizobium sp 42445 Precorrin-6A reductase (EC 1.3.1.54) (Precorrin-6X reductase) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21921 cobL Sinorhizobium sp 42445 Precorrin-6Y C(5,15)-methyltransferase [decarboxylating] (Precorrin-6 methyltransferase) (Precorrin-6Y methylase) (EC 2.1.1.132) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P21922 cobM Sinorhizobium sp 42445 Precorrin-4 C(11)-methyltransferase (EC 2.1.1.133) (Precorrin-3 methylase) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29929 cobN Sinorhizobium sp 42445 Aerobic cobaltochelatase subunit CobN (EC 6.6.1.2) (Hydrogenobyrinic acid a,c-diamide cobaltochelatase subunit CobN) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29930 cobO Sinorhizobium sp 42445 Corrinoid adenosyltransferase (EC 2.5.1.17) (Cob(II)alamin adenosyltransferase) (Cob(II)yrinic acid a,c-diamide adenosyltransferase) (Cobinamide/cobalamin adenosyltransferase) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29931 cobP Sinorhizobium sp 42445 Bifunctional adenosylcobalamin biosynthesis protein CobP (Adenosylcobinamide kinase) (EC 2.7.1.156) (Adenosylcobinamide-phosphate guanylyltransferase) (EC 2.7.7.62) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29932 cobQ Sinorhizobium sp 42445 Cobyric acid synthase Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29933 cobS Sinorhizobium sp 42445 Aerobic cobaltochelatase subunit CobS (EC 6.6.1.2) (Hydrogenobyrinic acid a,c-diamide cobaltochelatase subunit CobS) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29934 cobT Sinorhizobium sp 42445 Aerobic cobaltochelatase subunit CobT (EC 6.6.1.2) (Hydrogenobyrinic acid a,c-diamide cobaltochelatase subunit CobT) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29935 cobU Sinorhizobium sp 42445 Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase (NN:DBI PRT) (EC 2.4.2.21) (N(1)-alpha-phosphoribosyltransferase) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29936 cobV Sinorhizobium sp 42445 Adenosylcobinamide-GDP ribazoletransferase (EC 2.7.8.26) (Cobalamin synthase) (Cobalamin-5'-phosphate synthase) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29945 dgkA Sinorhizobium sp 42445 Diacylglycerol kinase (DAGK) (EC 2.7.1.107) (Diglyceride kinase) (DGK) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function P29950 ung Sinorhizobium sp 42445 Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed. {ECO:0000305}. reclassified-function Q2NS74 dapA Sodalis glossinidius (strain morsitans) 343509 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2NVY2 dapB Sodalis glossinidius (strain morsitans) 343509 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P80269 Solanum tuberosum (Potato) 4113 NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial (EC 7.1.1.2) (Complex I-28.5kD) (CI-28.5kD) (NADH-ubiquinone oxidoreductase 28.5 kDa subunit) Was originally reported that TYKY1 and TYKY2 were two different genes. {ECO:0000305|PubMed:9037104}. reclassified-function P30941 Solanum tuberosum (Potato) 4113 Serine protease inhibitor 7 (PIGEN1) (PIG) (STPIA) (STPIB) (pF4) (pKEN14-28) (allergen Sola t 4) Was originally thought to be an aspartic proteinase inhibitor (PubMed:1391774, PubMed:1515078). {ECO:0000305}. reclassified-function P20346 Solanum tuberosum (Potato) 4113 Defensin-like protein P322 (Probable protease inhibitor P322) Was initially thought (Ref.1) to be a protease inhibitor. {ECO:0000305}. reclassified-function A9FHA5 dapA Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56)) 448385 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P21923 Sorghum bicolor (Sorghum) (Sorghum vulgare) 4558 Defensin-like protein 1 (Small protein inhibitor of insect alpha-amylases 1) (SI alpha-1) Was initially thought (PubMed:1995329, PubMed:7705336, PubMed:9715910) to be a protease inhibitor. {ECO:0000305}. reclassified-function Q09198 Sorghum bicolor (Sorghum) (Sorghum vulgare) 4558 Defensin-like protein 21 (Small protein inhibitor of insect alpha-amylases 2.1) (SI alpha-2.1) Was initially thought to be a protease inhibitor. {ECO:0000305|PubMed:7705336}. reclassified-function P21924 Sorghum bicolor (Sorghum) (Sorghum vulgare) 4558 Defensin-like protein 2 (Small protein inhibitor of insect alpha-amylases 2) (SI alpha-2) Was initially thought to be a protease inhibitor. {ECO:0000305|PubMed:1995329}. reclassified-function P21925 Sorghum bicolor (Sorghum) (Sorghum vulgare) 4558 Defensin-like protein 3 (Small protein inhibitor of insect alpha-amylases 3) (SI alpha-3) Was initially thought (PubMed:1995329, PubMed:7705336) to be a protease inhibitor. {ECO:0000305}. reclassified-function Q93CA6 mlrC Sphingomonas sp 28214 Microcystinase C (MlrC) MC degradation was originally described as sequential, three-step process catalyzed by enzymes subsequently named as MlrA, MlrB and MlrC, where MlrC catalyzes hydrolysis of tetrapeptides generated by MlrB (PubMed:8899999). It is shown later that purified MlrC hydrolyzes also linear MC (PubMed:11769251, PubMed:22591122) so it is not clear if MlrB is indispensable in this pathway. {ECO:0000269|PubMed:11769251, ECO:0000269|PubMed:22591122, ECO:0000269|PubMed:8899999}. reclassified-function Q1GSC8 dapA Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) (Sphingomonas alaskensis) 317655 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P11869 Spinacia oleracea (Spinach) 3562 Triose phosphate/phosphate translocator, chloroplastic (cTPT) (E29) (p36) Was originally thought to function as a chloroplast protein import receptor. {ECO:0000305}. reclassified-function P80470 PSBY Spinacia oleracea (Spinach) 3562 Photosystem II reaction center proteins PsbY, chloroplastic (L-arginine-metabolizing enzyme) (L-AME) [Cleaved into: Photosystem II reaction center protein PsbY-1, chloroplastic (PsbY-A1); Photosystem II reaction center protein PsbY-2, chloroplastic (PsbY-A2)] Was originally thought to be a manganese-binding polypeptide with L-arginine metabolizing activity, with a possible role in the function of the CaMn4O5-cluster in oxygen-evolving PSII (PubMed:9829828). However it is not essential for PSII activity in cyanobacteria and does not furnish ligands for the CaMn4O5 cluster (By similarity). {ECO:0000250|UniProtKB:P73676, ECO:0000305|PubMed:9829828}. reclassified-function P19954 PSRP1 Spinacia oleracea (Spinach) 3562 Ribosome-binding factor PSRP1, chloroplastic (30S ribosomal protein 1) (CS-S5) (CS5) (Plastid-specific 30S ribosomal protein 1) (PSrp-1) (Ribosomal protein 1) (S22) (Translation factor pY) Was originally (PubMed:2693942, PubMed:2259340, PubMed:2376575, PubMed:1731992, PubMed:10874039, PubMed:18042701) thought to be a ribosomal protein. {ECO:0000305|PubMed:10874039, ECO:0000305|PubMed:1731992, ECO:0000305|PubMed:18042701, ECO:0000305|PubMed:2259340, ECO:0000305|PubMed:2376575, ECO:0000305|PubMed:2693942}. reclassified-function Q5HG25 dapA Staphylococcus aureus (strain COL) 93062 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5HG24 dapB Staphylococcus aureus (strain COL) 93062 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6U1L6 dapA Staphylococcus aureus (strain JH1) 359787 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6U1L7 dapB Staphylococcus aureus (strain JH1) 359787 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5ISS7 dapA Staphylococcus aureus (strain JH9) 359786 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5ISS8 dapB Staphylococcus aureus (strain JH9) 359786 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6GH13 dapA Staphylococcus aureus (strain MRSA252) 282458 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6GH12 dapB Staphylococcus aureus (strain MRSA252) 282458 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q6G9G6 dapA Staphylococcus aureus (strain MSSA476) 282459 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q6G9G5 dapB Staphylococcus aureus (strain MSSA476) 282459 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8NWS5 dapA Staphylococcus aureus (strain MW2) 196620 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8NWS4 dapB Staphylococcus aureus (strain MW2) 196620 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7X271 dapA Staphylococcus aureus (strain Mu3 / ATCC 700698) 418127 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7X273 dapB Staphylococcus aureus (strain Mu3 / ATCC 700698) 418127 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P63947 dapA Staphylococcus aureus (strain Mu50 / ATCC 700699) 158878 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P63893 dapB Staphylococcus aureus (strain Mu50 / ATCC 700699) 158878 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P63948 dapA Staphylococcus aureus (strain N315) 158879 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P63894 dapB Staphylococcus aureus (strain N315) 158879 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9EZ12 dapA Staphylococcus aureus (strain NCTC 8325 / PS 47) 93061 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9EZ11 dapB Staphylococcus aureus (strain NCTC 8325 / PS 47) 93061 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6QGU6 dapA Staphylococcus aureus (strain Newman) 426430 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6QGU7 dapB Staphylococcus aureus (strain Newman) 426430 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A8Z3X3 dapA Staphylococcus aureus (strain USA300 / TCH1516) 451516 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8Z3X4 dapB Staphylococcus aureus (strain USA300 / TCH1516) 451516 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2FH43 dapA Staphylococcus aureus (strain USA300) 367830 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2FH42 dapB Staphylococcus aureus (strain USA300) 367830 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2YXX4 dapA Staphylococcus aureus (strain bovine RF122 / ET3-1) 273036 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2YXX3 dapB Staphylococcus aureus (strain bovine RF122 / ET3-1) 273036 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B9DP23 dapA Staphylococcus carnosus (strain TM300) 396513 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B9DP24 dapB Staphylococcus carnosus (strain TM300) 396513 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8CP96 dapA Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) 176280 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8CP95 dapB Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) 176280 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5HPE7 dapA Staphylococcus epidermidis (strain ATCC 35984 / DSM 28319 / BCRC 17069 / CCUG 31568 / BM 3577 / RP62A) 176279 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5HPE6 dapB Staphylococcus epidermidis (strain ATCC 35984 / DSM 28319 / BCRC 17069 / CCUG 31568 / BM 3577 / RP62A) 176279 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q4L6A0 dapA Staphylococcus haemolyticus (strain JCSC1435) 279808 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q4L6A1 dapB Staphylococcus haemolyticus (strain JCSC1435) 279808 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q49XJ7 dapA Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) 342451 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q49XJ8 dapB Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) 342451 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q45486 gatB Staphylococcus sp 29387 Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Asp/Glu-ADT subunit B) (EC 6.3.5.-) Was originally thought to originate from B.subtilis. {ECO:0000305}. reclassified-function Q9S1H5 hprK Staphylococcus xylosus 1288 HPr kinase/phosphorylase (HPrK/P) (EC 2.7.11.-) (EC 2.7.4.-) (HPr kinase/phosphatase) (HPr(Ser) kinase/phosphorylase) Was originally (PubMed:10714994, PubMed:11904409) called HPr kinase/phosphatase, but P-Ser-HPr dephosphorylation was shown (PubMed:12359880) to follow a quite unique mechanism, in which Pi instead of H(2)O is used for the nucleophilic attack on the phosphoryl group. P-Ser-HPr dephosphorylation is therefore not a phosphohydrolysis but a phospho-phosphorolysis reaction, and the bifunctional enzyme was dubbed HPr kinase/phosphorylase. {ECO:0000305|PubMed:12359880}. reclassified-function G0YF19 at Starmerella bombicola (Yeast) (Candida bombicola) 75736 Sophorolipid acetyltransferase (EC 2.3.1.-) (Carboxyhydrate transacetylase) Was originally thought to be solely responsible for the acetylation of acidic SLs (PubMed:23516968, PubMed:26298016). However, new evidence supports the presence of up to 2 degrees of acetylation in bolaform, acidic and lactonic SLs obtained from knockout mutant, supporting the existence of other sophorolipid acetyltransferases (PubMed:39143561). {ECO:0000269|PubMed:23516968, ECO:0000269|PubMed:26298016, ECO:0000269|PubMed:39143561}. reclassified-function S5ZJC7 sble Starmerella bombicola (Yeast) (Candida bombicola) 75736 Sophorolipid transesterase (SBLE) (EC 3.1.1.-) (Lactonase) (Lactone transesterase) (Lipase-like enzyme SBLE) Was originally thought to catalyze the lactonization of acidic SLs via intramolecular esterification between the hydroxyl group at the sophorose head of the SLs and the carboxylate tail (PubMed:27251547). However, evidence has shown that it is a transesterase and inactive towards acidic SLs; instead, the substrate is bolaform SLs, which were not well characterized in previous studies (PubMed:27317616, PubMed:38937850, PubMed:39143561). {ECO:0000269|PubMed:27251547, ECO:0000269|PubMed:27317616, ECO:0000269|PubMed:38937850, ECO:0000269|PubMed:39143561}. reclassified-function P37125 Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia) 40324 Chorionicgonadotropic hormone-like receptor (CGH-R) Was originally reported to be highly similar to the mammalian chorionicgonadotropic hormone receptor, but is not significantly related. {ECO:0000305|PubMed:8427582}. reclassified-function B2FL61 dapA Stenotrophomonas maltophilia (strain K279a) 522373 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B2FQ70 dapB Stenotrophomonas maltophilia (strain K279a) 522373 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B4SRX7 dapA Stenotrophomonas maltophilia (strain R551-3) 391008 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B4SHT7 dapB Stenotrophomonas maltophilia (strain R551-3) 391008 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q04661 cpsB Streptococcus agalactiae serotype III (strain NEM316) 211110 Tyrosine-protein phosphatase CpsB (EC 3.1.3.48) Was originally called CpsA. {ECO:0000305|PubMed:8355611}. reclassified-function Q04662 cpsC Streptococcus agalactiae serotype III (strain NEM316) 211110 Capsular polysaccharide biosynthesis protein CpsC Was originally called CpsB. {ECO:0000305|PubMed:8355611}. reclassified-function Q04663 cpsD Streptococcus agalactiae serotype III (strain NEM316) 211110 Tyrosine-protein kinase CpsD (EC 2.7.10.2) Was originally called CpsC. {ECO:0000305|PubMed:8355611}. reclassified-function Q04664 cpsE Streptococcus agalactiae serotype III (strain NEM316) 211110 Galactosyl transferase CpsE (EC 2.7.8.-) Was originally called CpsD. {ECO:0000305|PubMed:8355611}. reclassified-function P0A4V0 neuA Streptococcus agalactiae serotype III (strain NEM316) 211110 N-acylneuraminate cytidylyltransferase (EC 2.7.7.43) (CMP-N-acetylneuraminic acid synthase) (CMP-NeuNAc synthase) (CMP-sialic acid synthase) Was originally called CpsF. {ECO:0000305|PubMed:8830246}. reclassified-function A8AXI2 dapA Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288) 467705 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A8AX95 dapB Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288) 467705 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8DUE5 dapA Streptococcus mutans serotype c (strain ATCC 700610 / UA159) 210007 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8DUL9 dapB Streptococcus mutans serotype c (strain ATCC 700610 / UA159) 210007 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8DS90 der Streptococcus mutans serotype c (strain ATCC 700610 / UA159) 210007 GTPase Der (GTP-binding protein EngA) Was originally thought to be a D-3-phosphoglycerate dehydrogenase. {ECO:0000305|PubMed:11155166}. reclassified-function P31305 fimA Streptococcus parasanguinis 1318 Metal ABC transporter substrate-binding lipoprotein FimA (Adhesin B) (FimA) (Saliva-binding protein) Was originally thought to be a fimbrial subunit. {ECO:0000305|PubMed:2572555}. reclassified-function C1C6Z0 dapA Streptococcus pneumoniae (strain 70585) 488221 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C1C8E8 dapB Streptococcus pneumoniae (strain 70585) 488221 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B8ZPG7 dapA Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1) 561276 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8ZLL9 dapB Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1) 561276 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8DPU7 Streptococcus pneumoniae (strain ATCC BAA-255 / R6) 171101 UPF0758 protein spr0996 Was originally thought to be the site of the radC102 mutation, but it was subsequently shown that it is not the case. {ECO:0000305|PubMed:18556794}. reclassified-function Q8DPZ9 dapA Streptococcus pneumoniae (strain ATCC BAA-255 / R6) 171101 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P63896 dapB Streptococcus pneumoniae (strain ATCC BAA-255 / R6) 171101 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2IPH2 dapA Streptococcus pneumoniae (strain CGSP14) 516950 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B2IR75 dapB Streptococcus pneumoniae (strain CGSP14) 516950 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1IBH4 dapA Streptococcus pneumoniae (strain Hungary19A-6) 487214 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1ICX7 dapB Streptococcus pneumoniae (strain Hungary19A-6) 487214 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C1CE08 dapA Streptococcus pneumoniae (strain JJA) 488222 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C1CFE0 dapB Streptococcus pneumoniae (strain JJA) 488222 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C1CK93 dapA Streptococcus pneumoniae (strain P1031) 488223 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C1CLQ6 dapB Streptococcus pneumoniae (strain P1031) 488223 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C1CRD6 dapA Streptococcus pneumoniae (strain Taiwan19F-14) 487213 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C1CSH7 dapB Streptococcus pneumoniae (strain Taiwan19F-14) 487213 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B5E4D5 dapA Streptococcus pneumoniae serotype 19F (strain G54) 512566 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B5E6K0 dapB Streptococcus pneumoniae serotype 19F (strain G54) 512566 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q04KR9 dapA Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) 373153 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q04JJ1 dapB Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) 373153 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P18791 amiA Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) 170187 Oligopeptide-binding protein AmiA The revised sequence of AmiA now includes, in the C-terminal section, the sequence of an ORF which was previously known as AmiB. {ECO:0000305}. reclassified-function Q97R25 dapA Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) 170187 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P63895 dapB Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) 170187 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O07874 rnhC Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) 170187 Ribonuclease HIII (RNase HIII) (EC 3.1.26.4) Was originally defined as a RNase HII; but belongs to the RNase HIII subfamily. {ECO:0000305|PubMed:9190796}. reclassified-function Q9L7Q2 zmpB Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) 170187 Zinc metalloprotease ZmpB (EC 3.4.24.-) Was originally (PubMed:10792723) thought to control translocation of choline-binding proteins to the cell surface but PubMed:11260480 failed to confirm this observation. The conflicting observations could be explained by the fact that the mutant strain used in PubMed:10792723 lacked capsule. {ECO:0000305|PubMed:10792723}. reclassified-function P0C0J0 speB Streptococcus pyogenes 1314 Streptopain (EC 3.4.22.10) (Exotoxin type B) (Group A streptococcal cysteine protease) (Streptococcal cysteine proteinase) (SPE B) (Streptococcus peptidase A) (SPP) Was initially thought to form a homodimer (PubMed:19712682). However, it was later shown to act as a monomer (PubMed:22645124). {ECO:0000269|PubMed:19712682, ECO:0000269|PubMed:22645124}. reclassified-function A3CN43 dapA Streptococcus sanguinis (strain SK36) 388919 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A3CMU3 dapB Streptococcus sanguinis (strain SK36) 388919 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A4VU96 dapA Streptococcus suis (strain 05ZYH33) 391295 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4VUK5 dapB Streptococcus suis (strain 05ZYH33) 391295 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A4W0I7 dapA Streptococcus suis (strain 98HAH33) 391296 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4W0U7 dapB Streptococcus suis (strain 98HAH33) 391296 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P48956 rplU Streptococcus thermophilus 1308 Large ribosomal subunit protein bL21 (50S ribosomal protein L21) Was originally thought to be ribosomal protein L20. {ECO:0000305|PubMed:7958782}. reclassified-function Q5M5P2 dapB Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) 264199 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q03K16 dapA Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9) 322159 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q03M29 dapB Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9) 322159 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5M154 dapB Streptococcus thermophilus (strain CNRZ 1066) 299768 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B9DS79 dapA Streptococcus uberis (strain ATCC BAA-854 / 0140J) 218495 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B9DRX8 dapB Streptococcus uberis (strain ATCC BAA-854 / 0140J) 218495 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P83221 cyp18 Streptomyces antibioticus 1890 Peptidyl-prolyl cis-trans isomerase cyp18 (PPIase cyp18) (SanCyp18) (EC 5.2.1.8) (Rotamase cyp18) Was originally thought to have an endonuclease activity. {ECO:0000305|PubMed:10400660}. reclassified-function Q82K82 dapB Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) 227882 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9X9W0 dapA1 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) 100226 4-hydroxy-tetrahydrodipicolinate synthase 1 (HTPA synthase 1) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function O86841 dapA2 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) 100226 4-hydroxy-tetrahydrodipicolinate synthase 2 (HTPA synthase 2) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function O86836 dapB Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) 100226 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function O08333 pfkA1 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) 100226 Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-dependent phosphofructokinase) (PPi-PFK) (Pyrophosphate-dependent 6-phosphofructose-1-kinase) Was originally characterized as ATP-dependent phosphofructokinase (PubMed:9055413). However, inspection of the original N-terminal sequence showed that the characterized enzyme was not pfkA1 (SCO2119), but pfkA2 (SCO5426) instead, another isozyme in S.coelicolor (PubMed:18606812). {ECO:0000305|PubMed:18606812, ECO:0000305|PubMed:9055413}. reclassified-function A0A3B6UEU3 ScoE Streptomyces coeruleorubidus 116188 (3R)-3-[(carboxymethyl)amino]fatty acid oxygenase/decarboxylase (EC 1.14.11.78) Was originally thought to function on an ACP-bound intermediate, but ScoE was later shown to act only on a free acid substrate. {ECO:0000269|PubMed:29906336, ECO:0000305|PubMed:28634299}. reclassified-function P0DX13 scoD Streptomyces coeruleorubidus 116188 (2E)-enoyl-[ACP] glycyltransferase (EC 4.3.2.11) ((2E)-unsaturated fatty acyl-[ACP] glycyltransferase) Was originally thought to produce an ACP-bound intermediate, but the next enzyme in the pathway (ScoE) was later shown to act only on a free acid substrate. That means the thioesterase activity of ScoD releases the product from the acyl-carrier protein after Michael addition. {ECO:0000269|PubMed:28634299, ECO:0000269|PubMed:29906336}. reclassified-function B1VXZ4 dapB Streptomyces griseus subsp. griseus (strain JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235) 455632 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q15JG4 vldB Streptomyces hygroscopicus subsp. limoneus 264445 Valienol-1-phosphate guanylyltransferase (EC 2.7.7.91) (Cyclitol nucleotidyltransferase) Was originally thought to be a glucose 1-phosphate uridylyltransferase. {ECO:0000305|Ref.3}. reclassified-function Q9L9E5 novW Streptomyces niveus (Streptomyces spheroides) 193462 dTDP-4-dehydrorhamnose 3-epimerase (EC 5.1.3.-) (Novobiocin biosynthesis protein W) (dTDP-6-deoxy-D-xylo-4-hexulose 3-epimerase) Was initially characterized as a 3,5-epimerase in vitro (PubMed:15752721). However, it was later shown that it acts as a dTDP-6-deoxy-D-xylo-4-hexulose 3-epimerase in vivo (PubMed:16514445). {ECO:0000305|PubMed:15752721, ECO:0000305|PubMed:16514445}. reclassified-function O24738 barX Streptomyces virginiae (Streptomyces cinnamonensis) 1961 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase (EC 2.3.1.277) It was originally suggested that BarX is likely to participate in the regulatory pathway for the production of VB, rather than in the biosynthetic pathway of VB itself. {ECO:0000305|PubMed:10792718}. reclassified-function Q06068 Strongylocentrotus purpuratus (Purple sea urchin) 7668 97 kDa heat shock protein (Egg sperm receptor) Was originally (PubMed:8383878) thought to have a N-terminal sequence signal and a C-terminal transmembrane region. Both domains do not exist in the revised sequence. {ECO:0000305|PubMed:8383878}. reclassified-function P38099 carA Stutzerimonas stutzeri (Pseudomonas stutzeri) 316 Carbamoyl phosphate synthase small chain (EC 6.3.5.5) (Carbamoyl phosphate synthetase glutamine chain) PubMed:2153657 sequence was originally thought to originate from Pseudomonas aeruginosa. {ECO:0000305}. reclassified-function A4VN86 dapA Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri) 379731 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4VPQ3 dapB Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri) 379731 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q43137 CAD1 Stylosanthes humilis (Townsville stylo) (Astyposanthes humilis) 35628 Probable mannitol dehydrogenase 1 (EC 1.1.1.255) (NAD-dependent mannitol dehydrogenase 1) Was originally (Ref.1) thought to be a cinnamyl-alcohol dehydrogenase. {ECO:0000305}. reclassified-function Q43138 CAD3 Stylosanthes humilis (Townsville stylo) (Astyposanthes humilis) 35628 Probable mannitol dehydrogenase 3 (EC 1.1.1.255) (NAD-dependent mannitol dehydrogenase 3) Was originally (Ref.1) thought to be a cinnamyl-alcohol dehydrogenase. {ECO:0000305}. reclassified-function P46218 Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Uncharacterized protein Saci_1674 Was originally (Ref.1) thought to be an RNA polymerase subunit. {ECO:0000305}. reclassified-function P14288 bgaS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Beta-galactosidase (Lactase) (EC 3.2.1.23) Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius. {ECO:0000305|PubMed:2508066}. reclassified-function Q55080 cyp119 Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Cytochrome P450 119 (EC 1.14.-.-) (Peroxidase) (EC 1.11.1.7) Was originally (PubMed:8617361) thought to originate from Sulfolobus solfataricus, but was shown (PubMed:18157853) to stem from Sulfolobus acidocaldarius. This was due to a contamination of the S.solfataricus P1 strain isolate used for the initial cloning with the S.acidocaldarius species. {ECO:0000305|PubMed:18157853, ECO:0000305|PubMed:8617361}. reclassified-function P38617 pfdA Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Prefoldin subunit alpha (GimC subunit alpha) Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius. {ECO:0000305|PubMed:1658539}. reclassified-function P35024 rpl1 Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Large ribosomal subunit protein uL1 (50S ribosomal protein L1p) Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius. {ECO:0000305|PubMed:2497941}. reclassified-function P35023 rpl10 Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Large ribosomal subunit protein uL10 (50S ribosomal protein L10) (50S ribosomal protein P0) (Acidic ribosomal protein P0 homolog) (L10e) Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius. {ECO:0000305|PubMed:2497941, ECO:0000305|PubMed:7966335}. reclassified-function P35025 rpl11 Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Large ribosomal subunit protein uL11 (50S ribosomal protein L11p) Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius. {ECO:0000305|PubMed:2497941, ECO:0000305|PubMed:7966335}. reclassified-function P08055 rpl12 Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Large ribosomal subunit protein P1 (50S ribosomal protein L12p) (Ribosomal protein A) Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius. {ECO:0000305|PubMed:2497941}. reclassified-function P38613 rpl18a Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Large ribosomal subunit protein eL20 (50S ribosomal protein L18Ae) (50S ribosomal protein L20e) (50S ribosomal protein LX) Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius. {ECO:0000305|PubMed:1711982}. reclassified-function P13005 rpl39e Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Large ribosomal subunit protein eL39 (50S ribosomal protein L39e) (L46e) Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius. {ECO:0000305|PubMed:2502431}. reclassified-function P27340 secE Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Protein translocase subunit SecE (Protein transport protein Sec61 gamma subunit homolog) Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius. {ECO:0000305|PubMed:1658539}. reclassified-function P27341 spt5 Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) 330779 Transcription elongation factor Spt5 Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius. {ECO:0000305|PubMed:1658539}. reclassified-function B2V6F1 dapA Sulfurihydrogenibium sp. (strain YO3AOP1) 436114 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q30R77 dapA Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)) 326298 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q30PD7 dapB Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)) 326298 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q971B7 atpA Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) 273063 A-type ATP synthase subunit A (EC 7.1.2.2) Was originally reported as originating from S.acidocaldarius. {ECO:0000305|PubMed:2896191}. reclassified-function Q971B6 atpB Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) 273063 A-type ATP synthase subunit B (ATP synthase beta subunit) Was originally reported as originating from S.acidocaldarius. {ECO:0000305|PubMed:2903160}. reclassified-function P62017 atpD Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) 273063 A-type ATP synthase subunit D Was originally reported as originating from S.acidocaldarius. {ECO:0000305|PubMed:2147683}. reclassified-function Q971B8 atpE Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) 273063 A-type ATP synthase subunit E Was originally reported as originating from S.acidocaldarius. {ECO:0000305|PubMed:2147683}. reclassified-function P62019 atpE Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) 273063 Membrane-associated ATPase epsilon chain (EC 7.1.2.2) (Sul-ATPase epsilon chain) Was originally reported as originating from S.acidocaldarius. {ECO:0000305|PubMed:2147683}. reclassified-function P62021 atpK Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) 273063 A-type ATP synthase subunit K (ATP synthase P subunit) (ATPase proteolipid subunit) Was originally reported as originating from S.acidocaldarius. {ECO:0000305|PubMed:2523390}. reclassified-function A6Q8F8 dapA Sulfurovum sp. (strain NBC37-1) 387093 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6Q6T6 dapB Sulfurovum sp. (strain NBC37-1) 387093 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P15175 Sus scrofa (Pig) 9823 Cathelin Was originally (PubMed:2792375) thought to be a thiol protease inhibitor. The inhibitory activity was due to the presence of leukocyte cysteine proteinase inhibitor and not to cathelin itself. {ECO:0000305|PubMed:2792375}. reclassified-function O62697 DEFB4A Sus scrofa (Pig) 9823 Defensin beta 4A (Beta-defensin 2) (BD-2) (Defensin, beta 2) Was originally annotated as a DEFB1/Beta-defensin 1 ortholog. {ECO:0000305}. reclassified-function Q58D68 ENPP6 Sus scrofa (Pig) 9823 Glycerophosphocholine cholinephosphodiesterase ENPP6 (GPC-Cpde) (EC 3.1.4.-) (EC 3.1.4.38) (Choline-specific glycerophosphodiester phosphodiesterase) (Ectonucleotide pyrophosphatase/phosphodiesterase family member 6) (E-NPP 6) (NPP-6) This sequence was originally thought to derive from Bos taurus (PubMed:16305752). In fact it derives from Sus scrofa (PubMed:15679890, PubMed:17145712). {ECO:0000305|PubMed:16305752}. reclassified-function Q58DD9 GPN2 Sus scrofa (Pig) 9823 GPN-loop GTPase 2 (EC 3.6.5.-) (ATP-binding domain 1 family member B) Was originally thought to originate from Bos taurus. {ECO:0000305}. reclassified-function O02826 MSMB Sus scrofa (Pig) 9823 Beta-microseminoprotein (Prostate secreted seminal plasma protein) (Prostate secretory protein of 94 amino acids) (PSP-94) (PSP94) (TS507) Was originally thought to inhibit the secretion of FSH by pituitary cells. {ECO:0000305}. reclassified-function Q29081 PMVK Sus scrofa (Pig) 9823 Phosphomevalonate kinase (PMKase) (EC 2.7.4.2) Was originally thought to be located in the peroxisome. However, was later shown to be cytosolic. {ECO:0000250|UniProtKB:Q15126}. reclassified-function P31636 SLC5A4 Sus scrofa (Pig) 9823 Solute carrier family 5 member 4 (Low affinity sodium-glucose cotransporter) Was originally thought to be a sodium/neutral amino acid cotransporter (system a neutral amino acid transporter) responsible for the sodium-dependent intake of neutral amino acids such as alanine, glycine, serine, cysteine, and proline. {ECO:0000305|PubMed:8420925}. reclassified-function O97562 UCP2 Sus scrofa (Pig) 9823 Dicarboxylate carrier UCP2 (Mitochondrial uncoupling protein 2) (UCP 2) (Solute carrier family 25 member 8) The role of UCP2/SLC25A8 in mitochondrial proton conductance is a matter of debate. It was initially suggested that it mediates proton leak that increases net proton conductance in response to ROS such as reactive alkenals generated during fatty acid oxidation in mitochondria. By lowering the proton motive force, it would provide for feedback control of mitochondrial ROS metabolism limiting extensive ROS production and protecting cells against oxidative stress. This activity and its potential regulation by ubiquinones and nucleotides was disputed by later studies, which failed to reproduce the effect on proton conductance under physiological conditions. Rather than 'uncoupling' the link between electron transfer and ATP synthesis, it may couple metabolite transport to proton flux to allow for optimal ATP turnover. {ECO:0000250|UniProtKB:P55851, ECO:0000250|UniProtKB:P70406}. reclassified-function Q6R2V0 WNK1 Sus scrofa (Pig) 9823 Serine/threonine-protein kinase WNK1 (EC 2.7.11.1) HSN2 was originally thought to be an intronless gene lying within a WNK1 gene intron. However, it is most probably an alternative exon which has been also described in alternative splicing products of the human and mouse WNK1 genes. Isoforms bearing this exon are specifically expressed in the nervous system in these species. {ECO:0000305|PubMed:15060842}. reclassified-function P32208 DUT Swinepox virus (strain Kasza) (SWPV) 10277 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) Was originally thought to be a protease-like protein (pseudoprotease). {ECO:0000305}. reclassified-function Q67P59 dapA Symbiobacterium thermophilum (strain DSM 24528 / JCM 14929 / IAM 14863 / T) 292459 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q67P64 dapB Symbiobacterium thermophilum (strain DSM 24528 / JCM 14929 / IAM 14863 / T) 292459 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P39660 cmpA Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2) 1140 Bicarbonate-binding protein CmpA Was originally thought to be a carotenoid-binding protein. {ECO:0000305|PubMed:2498292}. reclassified-function Q31M42 dapA Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2) 1140 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q31LA3 dapB Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2) 1140 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5MZT3 dapA Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) 269084 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5N0M4 dapB Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) 269084 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0IE16 dapA Synechococcus sp. (strain CC9311) 64471 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3ANI5 dapA Synechococcus sp. (strain CC9605) 110662 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3AIK8 dapB Synechococcus sp. (strain CC9605) 110662 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3B0T8 dapA Synechococcus sp. (strain CC9902) 316279 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3AYN5 dapB Synechococcus sp. (strain CC9902) 316279 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2JQ67 dapA Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) 321332 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2JWL7 dapA Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime) 321327 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5GQ13 dapA Synechococcus sp. (strain RCC307) 316278 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5GSL5 dapB Synechococcus sp. (strain RCC307) 316278 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5GHT4 dapA Synechococcus sp. (strain WH7803) 32051 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q55513 dapA Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) 1111708 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P72642 dapB Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) 1111708 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P29107 ilvC Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) 1111708 Ketol-acid reductoisomerase (NADP(+)) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 1) (Ketol-acid reductoisomerase type I) Was originally isolated as a glutamyl-tRNA reductase. {ECO:0000305|PubMed:1903397}. reclassified-function P32422 psaC Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) 1111708 Photosystem I iron-sulfur center (EC 1.97.1.12) (9 kDa polypeptide) (PSI-C) (Photosystem I subunit VII) (PsaC) PubMed:1463835 originally thought that there were two genes for psaC in PCC 6803. However, the first one identified did not originate from PCC 6803 but from N.tabacum. The real psaC gene was therefore incorrectly termed psaC2. {ECO:0000305}. reclassified-function P80460 psbU Synechocystis sp. (strain PCC 6714) (Aphanocapsa sp. (strain PCC 6714)) 1147 Photosystem II extrinsic protein U (PSII-U) (PsbU) (Photosystem II 12 kDa extrinsic protein) (PS II complex 12 kDa extrinsic protein) Was originally (Ref.1) thought to be a malate dehydrogenase. {ECO:0000305}. reclassified-function A0LEA7 dapA Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB) 335543 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A0LEA6 dapB Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB) 335543 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q0AXH2 dapB Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen) 335541 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3A1U7 dapA Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1) (Pelobacter carbinolicus) 338963 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3A1U6 dapB Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1) (Pelobacter carbinolicus) 338963 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q2LTA1 dapA Syntrophus aciditrophicus (strain SB) 56780 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q2LTA0 dapB Syntrophus aciditrophicus (strain SB) 56780 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8WZJ4 xynA Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum) 28572 1,4-beta-D-glucan cellobiohydrolase xynA (EC 3.2.1.91) (Beta-glucancellobiohydrolase xynA) (Exocellobiohydrolase xynA) (Exoglucanase xynA) Was originally identified as a 1,4-beta-D-xylan xylanohydrolase (PubMed:12664153). However, further sequence comparisons and enzymatic studies showed that xynA was principally an 1,4-beta-D-glucan cellobiohydrolase (PubMed:22776993). {ECO:0000305|PubMed:12664153, ECO:0000305|PubMed:22776993}. reclassified-function C5BQD1 dapA Teredinibacter turnerae (strain ATCC 39867 / T7901) 377629 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C5BQ31 dapB Teredinibacter turnerae (strain ATCC 39867 / T7901) 377629 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0KAL7 dapA Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) 340099 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B0K4I3 dapA Thermoanaerobacter sp. (strain X514) 399726 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P26827 amyA Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes) 33950 Cyclomaltodextrin glucanotransferase (EC 2.4.1.19) (Cyclodextrin-glycosyltransferase) (CGTase) Was originally thought to be an alpha-amylase. {ECO:0000305|PubMed:1854207}. reclassified-function Q47RU3 dapB Thermobifida fusca (strain YX) 269800 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B5YKK4 dapA Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87) 289376 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B9KY71 dapA Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2) 309801 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B9KY70 dapB Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2) 309801 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B7IF13 dapA Thermosipho africanus (strain TCF52B) 484019 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B7IF14 dapB Thermosipho africanus (strain TCF52B) 484019 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A6LP58 dapA Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429) 391009 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A6LP59 dapB Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429) 391009 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P12313 psbT Thermostichus vulcanus (Synechococcus vulcanus) 32053 Photosystem II reaction center protein T (PSII-T) Was originally thought to be PsbN. {ECO:0000305|PubMed:2503398}. reclassified-function Q8DJK4 dapA Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1) 197221 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8DHH2 dapB Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1) 197221 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P56728 Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) 243274 Uncharacterized protein TM_0928 Was originally proposed to be fused with TM_0929. {ECO:0000305|PubMed:8168477}. reclassified-function Q9X1K9 dapA Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) 243274 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9X1K8 dapB Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) 243274 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P96112 surE Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) 243274 5'-nucleotidase SurE (EC 3.1.3.5) (Nucleoside 5'-monophosphate phosphohydrolase) Was originally annotated as an acid phosphatase (EC 3.1.3.2). {ECO:0000305}. reclassified-function B9K865 dapA Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E) 309803 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B9K866 dapB Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E) 309803 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A5IM62 dapA Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1) 390874 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5IM63 dapB Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1) 390874 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1LBR1 dapA Thermotoga sp. (strain RQ2) 126740 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B1LBR0 dapB Thermotoga sp. (strain RQ2) 126740 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5SJQ1 dapA Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) 300852 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q72K27 dapA Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) 262724 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q93R93 lysJ Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) 262724 [LysW]-aminoadipate semialdehyde transaminase (EC 2.6.1.118) Was originally thought (PubMed:11489859) to be an N(2)-acetyl-L-2-aminoadipate semialdehyde transaminase. {ECO:0000305}. reclassified-function B8GN57 dapA Thioalkalivibrio sulfidiphilus (strain HL-EbGR7) 396588 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B8GNX3 dapB Thioalkalivibrio sulfidiphilus (strain HL-EbGR7) 396588 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3SJU8 dapA Thiobacillus denitrificans (strain ATCC 25259 / T1) 292415 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q3SJS2 dapB Thiobacillus denitrificans (strain ATCC 25259 / T1) 292415 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C4LCT8 dapB Tolumonas auensis (strain DSM 9187 / NBRC 110442 / TA 4) 595494 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A0A2I6QAZ5 AA14A Trametes coccinea (strain BRFM310) (Pycnoporus coccineus) 1353009 AA14 family lytic polysaccharide monooxygenase A (LPMO AA14A) (EC 1.14.99.-) Was originally described as having strict xylanolytic activity (PubMed:29377002). However, further studies could not detect activity on any of the tested polysaccharide substrates including xylan, and no synergistic effects between AA14A and a xylanase was observed, leading to the conclusion that the substrate remains unknown (PubMed:37418595). {ECO:0000269|PubMed:29377002, ECO:0000269|PubMed:37418595}. reclassified-function P96116 troA Treponema pallidum (strain DSM 117211 / Nichols) 243276 Zinc-binding protein TroA (Tromp-1) Was originally thought to be an outer membrane protein with porin-like properties. {ECO:0000305|PubMed:7768866}. reclassified-function B3E936 dapA Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter lovleyi) 398767 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B3E935 dapB Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter lovleyi) 398767 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P07981 egl1 Trichoderma reesei (Filamentous fungus) (Hypocrea jecorina) 51453 Endoglucanase EG-1 (EC 3.2.1.4) (Cellulase) (Endo-1,4-beta-glucanase) Was originally called endoglucanase EG-II. {ECO:0000305}. reclassified-function P07982 egl2 Trichoderma reesei (Filamentous fungus) (Hypocrea jecorina) 51453 Endoglucanase EG-II (EGII) (EC 3.2.1.4) (Cellulase) (Endo-1,4-beta-glucanase) Was originally called endoglucanase EG-III. {ECO:0000305|PubMed:3384334}. reclassified-function Q8NK50 lxr1 Trichoderma reesei (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / VTT-D-86271 / Rut C-30) (Hypocrea jecorina) 1344414 NADP-dependent mannitol dehydrogenase (MtDH) (EC 1.1.1.138) (Mannitol 2-dehydrogenase [NADP(+)]) Was previously described as the first fungal L-xylulose reductase responsible for NADPH dependent reduction of L-xylulose to xylitol in L-arabinose catabolism (PubMed:12009906). However, lxr1 forms a clade with fungal D-mannitol 2-dehydrogenases, is not induced by L-arabinose, and deletion reduces D-mannitol 2-dehydrogenase activity, suggesting that lxr1 is a D-mannitol 2-dehydrogenase and that a true L-xylulose reductase is still awaiting discovery (PubMed:19303876). {ECO:0000269|PubMed:12009906, ECO:0000269|PubMed:19303876}. reclassified-function Q10YI1 dapB Trichodesmium erythraeum (strain IMS101) 203124 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3MFY8 dapB Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) 240292 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function U3KRF8 Trichosanthes anguina (Snake gourd) 50544 Seed lectin (SGSL) [Cleaved into: Seed lectin Aalpha chain; Seed lectin Abeta chain; Seed lectin B chain] Was originally thought to be a heterodimer. However, methods used then would have missed the Aalpha chain. {ECO:0000305|PubMed:8799450}.; reclassified-function P24846 Triticum aestivum (Wheat) 4565 4-hydroxy-tetrahydrodipicolinate synthase 1, chloroplastic (HTPA synthase 1) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P24847 Triticum aestivum (Wheat) 4565 4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic (HTPA synthase 2) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P20158 Triticum aestivum (Wheat) 4565 Defensin-like protein 1 (Gamma-1-purothionin) Was initially thought to be a thionin (PubMed:2226781, PubMed:8380707). {ECO:0000305}. reclassified-function P20159 Triticum aestivum (Wheat) 4565 Defensin-like protein 2 (Gamma-2-purothionin) Was initially thought to be a thionin. {ECO:0000305|PubMed:2226781}. reclassified-function P33447 Trypanosoma cruzi 5693 Tyrosine aminotransferase (TAT) (EC 2.6.1.5) (L-tyrosine:2-oxoglutarate aminotransferase) Was originally thought to have three internal disulfide bonds. {ECO:0000305|PubMed:8100416}. reclassified-function P56220 dapD Unknown prokaryotic organism 2725 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (EC 2.3.1.117) (Tetrahydrodipicolinate N-succinyltransferase) (THDP succinyltransferase) (THP succinyltransferase) (Tetrahydropicolinate succinylase) Was originally thought to originate from Mycobacterium bovis (PubMed:11910040, PubMed:8880935, PubMed:9012664, PubMed:9671504). However, there is now convincing evidence that this is incorrect (PubMed:19394346). The source is unknown, but the sequence similarity suggests the protein is of enterobacterial origin. {ECO:0000305|PubMed:19394346}. reclassified-function P35627 Unspecified eudicot DB-1992 323200 Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Cyclophilin) (Cyclosporin A-binding protein) (Rotamase) Was originally (PubMed:1623198) reported to be isolated from an A.thaliana cDNA library. PubMed:9426607 authors have assigned that the sequence has been amplified from an other contaminating organism. {ECO:0000305|PubMed:1623198}. reclassified-function Q90121 M2A Ustilago maydis P4 virus (UmV4) (UmV-P4) 11009 KP4 killer toxin (Fungal toxin KP4) (Killer protein 4) Was originally thought to be glycosylated, but this does not seem to be the case according to PubMed:8145639. {ECO:0000305|PubMed:1897946}. reclassified-function Q76RE7 OPG046 Vaccinia virus (strain Ankara) (VACV) 126794 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) Was originally thought to be a protease-like protein (pseudoprotease). {ECO:0000305}. reclassified-function P68634 OPG046 Vaccinia virus (strain Copenhagen) (VACV) 10249 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) Was originally thought to be a protease-like protein (pseudoprotease). {ECO:0000305}. reclassified-function P68635 OPG046 Vaccinia virus (strain L-IVP) (VACV) 31531 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) Was originally thought to be a protease-like protein (pseudoprotease). {ECO:0000305}. reclassified-function P17374 OPG046 Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) 10254 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) Was originally thought to be a protease-like protein (pseudoprotease). {ECO:0000305}. reclassified-function P21605 OPG065 Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) 10254 RNA-binding protein OPG065 (RNA-binding protein E3) (p25) Was reported to bind Z-DNA structures (PubMed:12777633, PubMed:14757814). However, it probably binds Z-RNA in vivo (PubMed:34192517). {ECO:0000269|PubMed:12777633, ECO:0000269|PubMed:14757814, ECO:0000269|PubMed:34192517}. reclassified-function P07240 OPG108 Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) 10254 Envelope protein OPG108 (Ag35) (Virion envelope protein p35) Was originally mixed up with the protein H5 encoded by encoded by H5R gene. {ECO:0000305|PubMed:2462305}. reclassified-function P07242 OPG110 Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) 10254 Late transcription elongation factor OPG110 (Viral late gene transcription factor 4) (VLTF-4) Was originally thought to be p35/Ag35, a membrane protein involved in the biogenesis of the viral envelope encoded by H3L gene. {ECO:0000305|PubMed:2462305}. reclassified-function Q80HV3 OPG149 Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) 10254 Resolvase OPG149 (EC 3.1.-.-) (DNA holliday junction resolvase A22) Was initially reported be palmyoylated (PubMed:11017799). However, additional data are required to confirm this result. {ECO:0000305|PubMed:11017799}. reclassified-function P09282 26 Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3) 10338 Packaging protein UL32 Was originally thought to be an envelope glycoprotein. {ECO:0000305}. reclassified-function B7VJ13 dapB Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)) 575788 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7MXR0 dapB Vibrio campbellii (strain ATCC BAA-1116) 2902295 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9KPI5 Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) 243277 UPF0126 membrane protein VC_2382 Was originally thought to be recA; but the sequence was incorrectly assigned. {ECO:0000305|PubMed:1741267}. reclassified-function Q9KPI4 Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) 243277 Uncharacterized HTH-type transcriptional regulator VC_2383 Was originally thought to be recA; but the sequence was incorrectly assigned. {ECO:0000305|PubMed:1741267}. reclassified-function Q9KQ47 dapA Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) 243277 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9KPH7 dapB Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) 243277 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P15492 hlyB Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) 243277 Methyl-accepting chemotaxis protein HlyB Was originally thought to be a pore or transmembrane transporter for hemolysin. {ECO:0000305|PubMed:2162464}. reclassified-function A5F699 dapA Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) 345073 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A5F5N9 dapB Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) 345073 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C3LPG2 dapA Vibrio cholerae serotype O1 (strain M66-2) 579112 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function C3LQT6 dapB Vibrio cholerae serotype O1 (strain M66-2) 579112 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q87SF5 dapB Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) 223926 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8DBB0 dapA Vibrio vulnificus (strain CMCP6) 216895 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8DEM0 dapB Vibrio vulnificus (strain CMCP6) 216895 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8DF91 frsA Vibrio vulnificus (strain CMCP6) 216895 Esterase FrsA (EC 3.1.1.1) Was originally reported to catalyze the cofactor-independent decarboxylation of pyruvate (PubMed:21623357). In contrast, Kellett et al. demonstrated with computational, structural, and kinetic evidence that this enzyme does not exhibit pyruvate decarboxylase activity (PubMed:23452154). {ECO:0000269|PubMed:21623357, ECO:0000269|PubMed:23452154}. reclassified-function Q7MIL2 dapA Vibrio vulnificus (strain YJ016) 196600 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7MNU2 dapB Vibrio vulnificus (strain YJ016) 196600 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P83399 Vigna unguiculata (Cowpea) 3917 Defensin-like protein 1 (Cp-thionin I) (Cp-thionin-1) (Gamma-thionin I) Was initially thought to be a thionin. {ECO:0000305|PubMed:12112698}. reclassified-function P84920 Vigna unguiculata (Cowpea) 3917 Defensin-like protein 2 (Cp-thionin II) (Cp-thionin-2) (Gamma-thionin II) Was initially thought to be a thionin. {ECO:0000305|PubMed:16824043}. reclassified-function P14420 Vipera ammodytes meridionalis (Eastern sand viper) 73841 Basic phospholipase A2 vipoxin B chain (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Vipoxin toxic component) The acidic chain was originally postulated to act as an inhibitor of the basic chain. {ECO:0000305}. reclassified-function Q8D2M3 dapA Wigglesworthia glossinidia brevipalpis 36870 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8D3H6 dapB Wigglesworthia glossinidia brevipalpis 36870 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B3CM06 dapA Wolbachia pipientis subsp. Culex pipiens (strain wPip) 570417 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function B3CN84 dapB Wolbachia pipientis subsp. Culex pipiens (strain wPip) 570417 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q73H02 dapA Wolbachia pipientis wMel 163164 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q73I13 dapB Wolbachia pipientis wMel 163164 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q5GTA6 dapB Wolbachia sp. subsp. Brugia malayi (strain TRS) 292805 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function C0R2S2 dapB Wolbachia sp. subsp. Drosophila simulans (strain wRi) 66084 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q7M7L6 dapA Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes) 273121 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q7MA63 dapB Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes) 273121 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q4UU71 dapB Xanthomonas campestris pv. campestris (strain 8004) 314565 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8P9V6 dapA Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) 190485 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8P9L3 dapB Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) 190485 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0RSP5 dapB Xanthomonas campestris pv. campestris (strain B100) 509169 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8PLN5 dapA Xanthomonas citri pv. citri (strain 306) 190486 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8PLE0 dapB Xanthomonas citri pv. citri (strain 306) 190486 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q3BUC6 dapB Xanthomonas euvesicatoria pv. vesicatoria (strain 85-10) (Xanthomonas campestris pv. vesicatoria) 316273 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q9I8S4 azin2 Xenopus laevis (African clawed frog) 8355 Antizyme inhibitor 2 (AzI2) (Ornithine decarboxylase 2) (ODC 2) (xODC2) (Ornithine decarboxylase-like protein) (ODC-like protein) (ornithine decarboxylase paralog) (ODC-p) Human ortholog was initially reported to have ornithine decarboxylase or arginine decarboxylase activities, but it was later found that the mouse ortholog does not possess either of them. {ECO:0000305}. reclassified-function Q6GN98 eef1akmt1 Xenopus laevis (African clawed frog) 8355 EEF1A lysine methyltransferase 1 (EC 2.1.1.-) (N(6)-adenine-specific DNA methyltransferase 2) (Protein-lysine N-methyltransferase n6amt2) Was originally thought to be an N(6)-adenine-specific DNA methyltransferase based on primary sequence and predicted secondary structure. {ECO:0000255|HAMAP-Rule:MF_03187}. reclassified-function Q2TAQ1 elp1 Xenopus laevis (African clawed frog) 8355 Putative elongator complex protein 1 (ELP1) (IkappaB kinase complex-associated protein) (IKK complex-associated protein) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:O95163}. reclassified-function Q5HZM6 elp3 Xenopus laevis (African clawed frog) 8355 Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function Q5XG58 elp4 Xenopus laevis (African clawed frog) 8355 Elongator complex protein 4 The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}. reclassified-function Q0IHA2 elp6 Xenopus laevis (African clawed frog) 8355 Elongator complex protein 6 (Protein TMEM103) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q0PNE2}. reclassified-function Q90WN4 foxd2 Xenopus laevis (African clawed frog) 8355 Forkhead box protein D2 (FoxD2) (xFoxD2) (Fork head domain-related protein 9) (xFD-9) (Forkhead protein 3) (FKH-3) (xFKH3) Was originally thought to be a FoxD1 protein (PubMed:11804794, PubMed:15656969). However, further sequence comparisons clearly suggests that it belongs to the FoxD2 subclass (PubMed:10702024). {ECO:0000305|PubMed:10702024, ECO:0000305|PubMed:11804794, ECO:0000305|PubMed:15656969}. reclassified-function P79942 noct Xenopus laevis (African clawed frog) 8355 Nocturnin (EC 3.1.3.-) (Carbon catabolite repression 4-like protein) (Rhythmic message 1) (RM1) Was initially shown to have low deadenylase activity that was lost when the metal-binding Glu was mutated (PubMed:12573214). Later studies showed that the purified protein lacked deadenylase activity (By similarity). Was subsequently shown to act as a phosphatase (By similarity). {ECO:0000250|UniProtKB:O35710, ECO:0000250|UniProtKB:Q9UK39, ECO:0000269|PubMed:12573214}. reclassified-function Q91822 pim3 Xenopus laevis (African clawed frog) 8355 Serine/threonine-protein kinase pim-3 (EC 2.7.11.1) (Pim-1) Was originally called Pim-1 but seems to represent the protein pim3. {ECO:0000305|PubMed:9099695}. reclassified-function O93309 smc3 Xenopus laevis (African clawed frog) 8355 Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) Was originally isolated as a proteoglycan protein. Although not excluded, such secreted function is not clear. {ECO:0000305}. reclassified-function P40650 sox11-b Xenopus laevis (African clawed frog) 8355 Transcription factor Sox-11-B (Transcription factor Sox-13) (xSox-13) (XLS13B) Was originally termed sox-13. {ECO:0000305|PubMed:1614875}. reclassified-function P40649 sox13 Xenopus laevis (African clawed frog) 8355 Transcription factor Sox-13 (Transcription factor Sox-12) (xSox-12) (xSox12) Was originally termed sox-12 (PubMed:1614875, PubMed:8597594). {ECO:0000305}. reclassified-function Q5FWM3 sox3-b Xenopus laevis (African clawed frog) 8355 Transcription factor Sox-3-B (Transcription factor Sox-11) (xSox-11) Was originally termed sox-11. {ECO:0000305|PubMed:1614875}. reclassified-function Q8AYK6 wee1-a Xenopus laevis (African clawed frog) 8355 Wee1-like protein kinase 1-A (EC 2.7.10.2) (Zygotic wee1-like protein kinase 2) (XWee2) Was initially assigned as wee2 (PubMed:12217326). However, it corresponds to the zygotic protein WEE1 in mammals. {ECO:0000305|PubMed:12217326}. reclassified-function P47817 wee2-a Xenopus laevis (African clawed frog) 8355 Wee1-like protein kinase 2-A (EC 2.7.10.2) (Maternally supplied wee1-like protein kinase 1A) (Xe-wee1A) Was initially assigned as wee1 (PubMed:7749193). However, it corresponds to the meiosis-specific protein WEE2 in mammals. {ECO:0000305|PubMed:7749193}. reclassified-function O57473 wee2-b Xenopus laevis (African clawed frog) 8355 Wee1-like protein kinase 2-B (EC 2.7.10.2) (Wee1-like protein kinase 1) (Xe-wee1) Was initially assigned as wee1 (PubMed:9486797). However, it corresponds to the meiosis-specific protein WEE2 in mammals. {ECO:0000305|PubMed:9486797}. reclassified-function A0A1L8F8I9 whr1.L Xenopus laevis (African clawed frog) 8355 Winged helix repair factor 1 (Inactive serine/threonine-protein kinase 19) Was originally reported to be a serine/threonine-protein kinase. However, later studies have shown that the protein does not have kinase activity and is involved in transcription-coupled nucleotide excision repair. {ECO:0000250|UniProtKB:P49842}. reclassified-function Q0P4M4 agbl2 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 Cytosolic carboxypeptidase 2 (EC 3.4.17.-) (ATP/GTP-binding protein-like 2) (Protein deglutamylase CCP2) Was initially shown to catalyze the removal of carboxy-terminus tyrosine from alpha-tubulin (By similarity). However, later studies did not identified any detyrosinase or deglycylase activities from the carboxy-terminus of tubulin (By similarity). {ECO:0000250|UniProtKB:Q5U5Z8, ECO:0000250|UniProtKB:Q8CDK2}.; reclassified-function Q5EBD9 elp2 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 Elongator complex protein 2 (ELP2) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q6IA86}. reclassified-function Q6NVL5 elp3 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. reclassified-function Q28CX0 elp6 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 Elongator complex protein 6 (Protein TMEM103) The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification. {ECO:0000250|UniProtKB:Q0PNE2}. reclassified-function Q7T0B0 stk40 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 Serine/threonine-protein kinase 40 (EC 2.7.11.1) (Serine/threonine-protein kinase lyk4) Was originally thought to originate from X.laevis. However, sequence identity with X.tropicalis is much higher than with X.laevis, suggesting that the sequence is from X.tropicalis. {ECO:0000305}. reclassified-function B2GUB3 ttll3 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 8364 Tubulin tyrosine ligase 3 (EC 6.3.2.-) (Tubulin--tyrosine ligase protein 3) TTLL3 and TTLL8 monoglycylase-mediated glycylation of tubulin was initially reported to play a role in ependymal motile ciliary maintenance (By similarity). However, contradictory results were later observed (By similarity). {ECO:0000250|UniProtKB:A4Q9E5}. reclassified-function Q2F7J1 env Xenotropic MuLV-related virus (isolate VP35) (XMRV) 356663 Envelope glycoprotein (Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM); R-peptide] Originally thought to be characterized from prostate tumors, the described gammaretrovirus XMRV is in fact laboratory-derived and there is no association of XMRV with prostate cancer. {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}. reclassified-function Q2F7J2 gag Xenotropic MuLV-related virus (isolate VP35) (XMRV) 356663 Gag polyprotein (Pr65gag) (Core polyprotein) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10-gag (NC-gag)] Originally thought to be characterized from prostate tumors, the described gammaretrovirus XMRV is in fact laboratory-derived and there is no association of XMRV with prostate cancer. {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}. reclassified-function Q2F7J3 gag-pol Xenotropic MuLV-related virus (isolate VP35) (XMRV) 356663 Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-pol); Protease p14 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p80 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)] Originally thought to be characterized from prostate tumors, the described gammaretrovirus XMRV is in fact laboratory-derived and there is no association of XMRV with prostate cancer. {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}. reclassified-function Q2F7I8 env Xenotropic MuLV-related virus (isolate VP42) (XMRV) 356664 Envelope glycoprotein (Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM); R-peptide] Originally thought to be characterized from prostate tumors, the described gammaretrovirus XMRV is in fact laboratory-derived and there is no association of XMRV with prostate cancer. {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}. reclassified-function Q2F7I9 gag Xenotropic MuLV-related virus (isolate VP42) (XMRV) 356664 Gag polyprotein (Pr65gag) (Core polyprotein) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10-gag (NC-gag)] Originally thought to be characterized from prostate tumors, the described gammaretrovirus XMRV is in fact laboratory-derived and there is no association of XMRV with prostate cancer. {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}. reclassified-function Q2F7J0 gag-pol Xenotropic MuLV-related virus (isolate VP42) (XMRV) 356664 Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-pol); Protease p14 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p80 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)] Originally thought to be characterized from prostate tumors, the described gammaretrovirus XMRV is in fact laboratory-derived and there is no association of XMRV with prostate cancer. {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}. reclassified-function Q27ID8 env Xenotropic MuLV-related virus (isolate VP62) (XMRV) 373193 Envelope glycoprotein (Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM); R-peptide] Originally thought to be characterized from prostate tumors, the described gammaretrovirus XMRV is in fact laboratory-derived and there is no association of XMRV with prostate cancer. {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}. reclassified-function Q27ID9 gag Xenotropic MuLV-related virus (isolate VP62) (XMRV) 373193 Gag polyprotein (Pr65gag) (Core polyprotein) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-gag)] Originally thought to be characterized from prostate tumors, the described gammaretrovirus XMRV is in fact laboratory-derived and there is no association of XMRV with prostate cancer. {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}. reclassified-function A1Z651 gag-pol Xenotropic MuLV-related virus (isolate VP62) (XMRV) 373193 Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-pol); Protease p14 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p80 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)] Originally thought to be characterized from prostate tumors, the described gammaretrovirus XMRV is in fact laboratory-derived and there is no association of XMRV with prostate cancer. {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}. reclassified-function Q9PER5 dapA Xylella fastidiosa (strain 9a5c) 160492 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q9PEC3 dapB Xylella fastidiosa (strain 9a5c) 160492 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B0U565 dapB Xylella fastidiosa (strain M12) 405440 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2I841 dapB Xylella fastidiosa (strain M23) 405441 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q87AT3 dapA Xylella fastidiosa (strain Temecula1 / ATCC 700964) 183190 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q87EC0 dapB Xylella fastidiosa (strain Temecula1 / ATCC 700964) 183190 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A1JL07 dapA Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) 393305 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A1JJE5 dapB Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) 393305 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q8ZCD0 dapA Yersinia pestis 632 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q8ZIL6 dapB Yersinia pestis 632 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A4TMN2 dapA Yersinia pestis (strain Pestoides F) 386656 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A4TQE9 dapB Yersinia pestis (strain Pestoides F) 386656 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A9R003 dapB Yersinia pestis bv. Antiqua (strain Angola) 349746 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1C0I8 dapB Yersinia pestis bv. Antiqua (strain Antiqua) 360102 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function Q1CMU5 dapB Yersinia pestis bv. Antiqua (strain Nepal516) 377628 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A0A0N9NCU6 yopJ Yersinia pseudotuberculosis 633 Serine/threonine-protein acetyltransferase YopJ (EC 2.3.1.-) (Virulence factor YopJ) Was initially thought to be a protease involved in deubiquitination because of its similarity with cysteine proteases (PubMed:11090361, PubMed:16301742). However, it was later shown that YopJ is an acetyltransferase that uses a dual substrate mechanism similar to the one used by papain-like proteases (PubMed:16728640). {ECO:0000269|PubMed:11090361, ECO:0000269|PubMed:16301742, ECO:0000269|PubMed:16728640}. reclassified-function Q668F7 dapA Yersinia pseudotuberculosis serotype I (strain IP32953) 273123 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q66ER9 dapB Yersinia pseudotuberculosis serotype I (strain IP32953) 273123 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B2K3N1 dapB Yersinia pseudotuberculosis serotype IB (strain PB1/+) 502801 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function A7FG49 dapA Yersinia pseudotuberculosis serotype O:1b (strain IP 31758) 349747 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function A7FMD2 dapB Yersinia pseudotuberculosis serotype O:1b (strain IP 31758) 349747 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function B1JKZ4 dapB Yersinia pseudotuberculosis serotype O:3 (strain YPIII) 502800 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. reclassified-function P26259 Zea mays (Maize) 4577 4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function P81008 Zea mays (Maize) 4577 Defensin-like protein 1 (Gamma-zeathionin-1) Was initially thought (Ref.1) to be a thionin. {ECO:0000305}. reclassified-function P81009 Zea mays (Maize) 4577 Defensin-like protein 2 (Gamma-zeathionin-2) Was initially thought (Ref.1) to be a thionin. {ECO:0000305}. reclassified-function Q41048 PSBQ1 Zea mays (Maize) 4577 Oxygen-evolving enhancer protein 3-1, chloroplastic (OEE3) (16 kDa subunit of oxygen evolving system of photosystem II) (OEC 16 kDa subunit) Was originally thought to originate from pea. {ECO:0000305|PubMed:16668961}. reclassified-function Q5NPL6 dapA Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) 264203 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}. reclassified-function Q5NPM9 dapB Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) 264203 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. {ECO:0000305}. retracted-reference Q8LBP4 ALB3 Arabidopsis thaliana (Mouse-ear cress) 3702 Inner membrane protein ALBINO3, chloroplastic Two articles reported an interaction with LPA2; however, these papers were later retracted. {ECO:0000305|PubMed:17601825, ECO:0000305|PubMed:20605914, ECO:0000305|PubMed:27895223, ECO:0000305|PubMed:28154118}. retracted-reference Q38912 ARAC3 Arabidopsis thaliana (Mouse-ear cress) 3702 Rac-like GTP-binding protein ARAC3 (AtRAC1) (EC 3.6.5.2) (GTPase protein ROP6) An article reported S-acylation of Cys residues that regulates localization to membranes; however, this paper was later retracted. {ECO:0000305|PubMed:17242203, ECO:0000305|PubMed:28754775}. retracted-reference Q9SUH5 AUG8 Arabidopsis thaliana (Mouse-ear cress) 3702 AUGMIN subunit 8 (QWRF motif-containing protein 8) (ROP1 enhancer 2) An article reported that this protein promotes microtubule reorientation in hypocotyls; however, this paper was later retracted. {ECO:0000305|PubMed:23735294, ECO:0000305|PubMed:28874511}. retracted-reference Q9SKA9 CHX21 Arabidopsis thaliana (Mouse-ear cress) 3702 Cation/H(+) antiporter 21 (Protein CATION/H+ EXCHANGER 21) (AtCHX21) The article by Evans et al was retracted by the editors due to concerns over image manipulation, which raised sufficient doubts regarding the credibility of the study. {ECO:0000305|PubMed:33428752}. retracted-reference Q8VYD4 CHX23 Arabidopsis thaliana (Mouse-ear cress) 3702 Cation/H(+) antiporter 23, chloroplastic (Protein CATION/H+ EXCHANGER 23) (AtCHX23) The article by Evans et al was retracted by the editors due to concerns over image manipulation, which raised sufficient doubts regarding the credibility of the study. {ECO:0000305|PubMed:33428752}. retracted-reference Q9M7X9 CITRX Arabidopsis thaliana (Mouse-ear cress) 3702 Thioredoxin-like protein CITRX, chloroplastic (EC 1.8.-.-) (Cf-9-interacting thioredoxin) (AtCiTrx) (PEP-associated protein 10) (Thioredoxin Trx p) (Thioredoxin Z) The article has been retracted, because it has become clear that the thioredoxin that interacts in yeast 2-hybrid with the Cf-9 C-terminus is in fact localized in the chloroplast, rendering a role in Cf-9 signaling unlikely. All the authors agree that this paper should be withdrawn from the scientific literature. {ECO:0000305|PubMed:31310343}. retracted-reference Q8RWY6 CLASP Arabidopsis thaliana (Mouse-ear cress) 3702 CLIP-associated protein (AtCLASP) An article reported an auxin transcription module controlling cell division plane rotation through CLASP; however, this paper was later retracted. {ECO:0000305|PubMed:22500804, ECO:0000305|PubMed:24267897}. retracted-reference P21238 CPN60A1 Arabidopsis thaliana (Mouse-ear cress) 3702 Chaperonin 60 subunit alpha 1, chloroplastic (CPN-60 alpha 1) (Protein SCHLEPPERLESS) (RuBisCO large subunit-binding protein subunit alpha 1) The Cpn60 chaperonin complex was previously shown to be required for folding of the NAD(P)H-quinone oxidoreductase subunit ndhH. However the corresponding paper has been retracted due to fraudulent image manipulation of some of the data. {ECO:0000305|PubMed:21483722, ECO:0000305|PubMed:36332167}. retracted-reference Q56XV8 CPN60A2 Arabidopsis thaliana (Mouse-ear cress) 3702 Chaperonin 60 subunit alpha 2, chloroplastic (CPN-60 alpha 2) (Protein EMBRYO DEFECTIVE 3007) The Cpn60 chaperonin complex was previously shown to be required for folding of the NAD(P)H-quinone oxidoreductase subunit ndhH. However the corresponding paper has been retracted due to fraudulent image manipulation of some of the data. {ECO:0000305|PubMed:21483722, ECO:0000305|PubMed:36332167}. retracted-reference P21240 CPN60B1 Arabidopsis thaliana (Mouse-ear cress) 3702 Chaperonin 60 subunit beta 1, chloroplastic (CPN-60 beta 1) (60 kDa chaperonin subunit beta 1) (RuBisCO large subunit-binding protein subunit beta, chloroplastic) The Cpn60 chaperonin complex was previously shown to be required for folding of the NAD(P)H-quinone oxidoreductase subunit ndhH. However the corresponding paper has been retracted due to fraudulent image manipulation of some of the data. {ECO:0000305|PubMed:21483722, ECO:0000305|PubMed:36332167}. retracted-reference Q9LJE4 CPN60B2 Arabidopsis thaliana (Mouse-ear cress) 3702 Chaperonin 60 subunit beta 2, chloroplastic (CPN-60 beta 2) The Cpn60 chaperonin complex was previously shown to be required for folding of the NAD(P)H-quinone oxidoreductase subunit ndhH. However the corresponding paper has been retracted due to fraudulent image manipulation of some of the data. {ECO:0000305|PubMed:21483722, ECO:0000305|PubMed:36332167}. retracted-reference C0Z361 CPN60B3 Arabidopsis thaliana (Mouse-ear cress) 3702 Chaperonin 60 subunit beta 3, chloroplastic (CPN-60 beta 3) The Cpn60 chaperonin complex was previously shown to be required for folding of the NAD(P)H-quinone oxidoreductase subunit ndhH. However the corresponding paper has been retracted due to fraudulent image manipulation of some of the data. {ECO:0000305|PubMed:21483722, ECO:0000305|PubMed:36332167}. retracted-reference Q9C667 CPN60B4 Arabidopsis thaliana (Mouse-ear cress) 3702 Chaperonin 60 subunit beta 4, chloroplastic (CPN-60 beta 4) Was previously thought to bind and recruit the NAD(P)H-quinone oxidoreductase subunit ndhH to the Cpn60 chaperonin complex to facilitate its correct folding. The C-terminus (568-611) was described as required for ndhH binding but not for chaperonin complex formation. However the corresponding paper has been retracted due to fraudulent image manipulation of some of the data. {ECO:0000305|PubMed:21483722, ECO:0000305|PubMed:36332167}. retracted-reference O82258 CRR6 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein CHLORORESPIRATORY REDUCTION 6, chloroplastic Was shown to be a chloroplast stromal protein that may be required for post-translational steps of NDH subcomplex A biogenesis essential for its accumulation. However, The corresponding paper has been retracted due to evidence of digital manipulation of some of the data, making the conclusions unreliable. {ECO:0000305|PubMed:20444231, ECO:0000305|PubMed:36951245}. retracted-reference Q9FL87 CRR7 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein CHLORORESPIRATORY REDUCTION 7, chloroplastic Was shown to be a chloroplast stromal protein that may be required for post-translational steps of NDH subcomplex A biogenesis essential for its accumulation. However, The corresponding paper has been retracted due to evidence of digital manipulation of some of the data, making the conclusions unreliable. {ECO:0000305|PubMed:20444231, ECO:0000305|PubMed:36951245}. retracted-reference Q9ZTP3 EIN4 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein EIN4 (AtEIN4) (EC 2.7.11.-) (Protein ETHYLENE INSENSITIVE 4) The article by Li et al was retracted by the editors after publication. Concerns were raised regarding a number of figure panels, such as partial overlap between the panels and duplication of protein gel analysis. {ECO:0000305|PubMed:35105927}. retracted-reference Q0WPQ2 ETR2 Arabidopsis thaliana (Mouse-ear cress) 3702 Ethylene receptor 2 (AtETR2) (EC 2.7.11.-) (Protein ETHYLENE RESPONSE 2) (Protein ETR2) The article by Li et al was retracted by the editors after publication. Concerns were raised regarding a number of figure panels, such as partial overlap between the panels and duplication of protein gel analysis. {ECO:0000305|PubMed:35105927}. retracted-reference P49177 GB1 Arabidopsis thaliana (Mouse-ear cress) 3702 Guanine nucleotide-binding protein subunit beta (AGB1) (transducin) An article reported a role as negative regulator of ABA during seed germination; however, this paper was later retracted. {ECO:0000305|PubMed:16581874, ECO:0000305|PubMed:31685692}. retracted-reference O04714 GCR1 Arabidopsis thaliana (Mouse-ear cress) 3702 G protein-coupled receptor 1 An article reported a role as negative regulator of ABA during seed germination; however, this paper was later retracted. {ECO:0000305|PubMed:16581874, ECO:0000305|PubMed:31685692}. retracted-reference Q94B78 GLDP1 Arabidopsis thaliana (Mouse-ear cress) 3702 Glycine dehydrogenase (decarboxylating) 1, mitochondrial (EC 1.4.4.2) (Glycine cleavage system P protein 1) (Glycine decarboxylase 1) (Glycine decarboxylase P-protein 1) (AtGLDP1) (Glycine dehydrogenase (aminomethyl-transferring) 1) This protein has also been shown to act as an inducible nitric oxide synthase (iNOS) (PubMed:12757708), but the paper has been retracted (PubMed:15599984). {ECO:0000305}. retracted-reference P18064 GPA1 Arabidopsis thaliana (Mouse-ear cress) 3702 Guanine nucleotide-binding protein alpha-1 subunit (GP-alpha-1) An article reported a role as negative regulator of ABA during seed germination; however, this paper was later retracted. {ECO:0000305|PubMed:16581874, ECO:0000305|PubMed:31685692}. retracted-reference Q9SRY4 LPA1 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein LOW PSII ACCUMULATION 1, chloroplastic An article reported a lack of interaction with LPA2; however, this paper was later retracted. {ECO:0000305|PubMed:17601825, ECO:0000305|PubMed:27895223}. retracted-reference F4KDA6 LPA2 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein LPA2 (Protein LOW PSII ACCUMULATION 2, chloroplastic) A paper reported a role in assisting chlorophyll a binding protein psbC assembly within photosystem II (PSII); however, this paper was later retracted. An article reported an interaction with LPA3; however, this paper was later retracted. {ECO:0000305|PubMed:17601825, ECO:0000305|PubMed:20605914, ECO:0000305|PubMed:27895223, ECO:0000305|PubMed:28154118}. retracted-reference Q8H0W0 LPA3 Arabidopsis thaliana (Mouse-ear cress) 3702 Protein LPA3 (Protein LOW PSII ACCUMULATION 3, chloroplastic) An article reported a role in essential for photosystem II assembly; however, this paper was later retracted. {ECO:0000305|PubMed:20605914, ECO:0000305|PubMed:28154118}. retracted-reference Q9SCU7 MYB30 Arabidopsis thaliana (Mouse-ear cress) 3702 Transcription factor MYB30 (Myb-related protein 30) (AtMYB30) An article reported regulation of transcriptional activity and hypersensitive response control by Xanthomonas type III effector XopD; however, this paper was later retracted. {ECO:0000305|PubMed:21917550, ECO:0000305|PubMed:29255113}. retracted-reference Q9SDS8 MYB8 Arabidopsis thaliana (Mouse-ear cress) 3702 Transcription factor MYB8 (Myb-related protein 8) (AtMYB8) This protein has been described as HOS10 (high expression of osmotically responsive genes 10), a coordinating factor for responses to abiotic stress and for growth and development (PubMed:15994234). However, due to a locus misidentification, the locus responsible for the HOS10 phenotypes reported in ecotype C24 remains unknown and the paper has been retracted (PubMed:20622156). {ECO:0000305}. retracted-reference Q84TD6 NAC047 Arabidopsis thaliana (Mouse-ear cress) 3702 NAC transcription factor 47 (NAC domain-containing protein 47) (ANAC047) (Protein SPEEDY HYPONASTIC GROWTH) Was originally thought as being induced by root flooding and as acting as a transcription factor binding to the promoter of ACO5 (an ACC oxidase involved in ethylene biosynthesis) to mediate waterlogging-induced hyponastic leaf movement and cell expansion in abaxial cells of the basal petiole region (PubMed:24363315). However, the corresponding article has been retracted (PubMed:40523660). {ECO:0000269|PubMed:24363315, ECO:0000269|PubMed:40523660}. retracted-reference Q56Y52 POT1A Arabidopsis thaliana (Mouse-ear cress) 3702 Protection of telomeres protein 1a (AtPOT1a) (AtPot1) (Protection of telomeres protein 1) Was originally thought to associate with TER1, the RNA molecule of the telomerase complex that provides a template for telomeric DNA synthesis (PubMed:21164032). The authentic RNA subunit of the telomerase that associates with POT1A has been recently shown to be TR and not TER1 (PubMed:31392988, PubMed:31754031). The original publication has been retracted. {ECO:0000269|PubMed:21164032, ECO:0000269|PubMed:31392988, ECO:0000269|PubMed:31754031, ECO:0000305|PubMed:31754033}. retracted-reference Q06738 RD29A Arabidopsis thaliana (Mouse-ear cress) 3702 Low-temperature-induced 78 kDa protein (Desiccation-responsive protein 29A) An article reported induction by MKK1, MKK2 and MKK3 in response to drought and salt stresses; however, this paper was later retracted. {ECO:0000305|PubMed:16913865, ECO:0000305|PubMed:17081259}. retracted-reference Q29PU2 SAUR76 Arabidopsis thaliana (Mouse-ear cress) 3702 Auxin-responsive protein SAUR76 (Protein SMALL AUXIN UP RNA 76) The article by Li et al was retracted by the editors after publication. Concerns were raised regarding a number of figure panels, such as partial overlap between the panels and duplication of protein gel analysis. {ECO:0000305|PubMed:35105927}. retracted-reference Q9LQI6 SAUR77 Arabidopsis thaliana (Mouse-ear cress) 3702 Auxin-responsive protein SAUR77 (Protein SMALL AUXIN UP RNA 77) The article by Li et al was retracted by the editors after publication. Concerns were raised regarding a number of figure panels, such as partial overlap between the panels and duplication of protein gel analysis. {ECO:0000305|PubMed:35105927}. retracted-reference Q9C9E1 SAUR78 Arabidopsis thaliana (Mouse-ear cress) 3702 Auxin-responsive protein SAUR78 (Protein SMALL AUXIN UP RNA 78) The article by Li et al was retracted by the editors after publication. Concerns were raised regarding a number of figure panels, such as partial overlap between the panels and duplication of protein gel analysis. {ECO:0000305|PubMed:35105927}. retracted-reference P56753 ndhH Arabidopsis thaliana (Mouse-ear cress) 3702 NAD(P)H-quinone oxidoreductase subunit H, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit H) (NADH-plastoquinone oxidoreductase 49 kDa subunit) (NADH-plastoquinone oxidoreductase subunit H) The folding of this protein was previously described as requiering the activity of the type I chaperonin Cpn60, possibly following recruitment by the chaperonin minor subunit CPN60B4. However the corresponding paper has been retracted due to fraudulent image manipulation of some of the data. {ECO:0000305|PubMed:21483722, ECO:0000305|PubMed:36332167}. retracted-reference P56778 psbC Arabidopsis thaliana (Mouse-ear cress) 3702 Photosystem II CP43 reaction center protein (PSII 43 kDa protein) (Protein CP-43) An article reported an interaction with LPA2; however, this paper was later retracted. An article reported an interaction with LPA3; however, this paper was later retracted. {ECO:0000305|PubMed:17601825, ECO:0000305|PubMed:20605914, ECO:0000305|PubMed:27895223, ECO:0000305|PubMed:28154118}. retracted-reference A9QXE0 Aspergillus niger 5061 Cyanide hydratase (CHT) (EC 4.2.1.66) (Cyanide-degrading nitrilase) (Formamide hydrolyase) (NitAn1) It was initially shown that the substrate specificities of the enzyme natively expressed in Aspergillus niger and the recombinant enzyme expressed in E.coli were different (PubMed:17061133), and it was hypothesized that the difference may be due to a misfolding or a post-translational modification (PubMed:21210990). However, both papers were corrected (PubMed:23455586) or retracted (PubMed:23870008), because it was shown that the 2 enzymes analyzed were different in terms of their primary structure (Ref.7). {ECO:0000305|PubMed:23455586, ECO:0000305|PubMed:23870008, ECO:0000305|Ref.7}. retracted-reference E8MGH8 hypBA1 Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) 565042 Non-reducing end beta-L-arabinofuranosidase (EC 3.2.1.185) (Beta-L-arabinofuranosidase) (Beta-AFase) The original article describing the function has been retracted because the results of E338A and E366A mutants were reversed. The authors later submitted a corrected manuscript. {ECO:0000305|PubMed:21914802, ECO:0000305|PubMed:24143008}. retracted-reference O61235 ctl-1 Caenorhabditis elegans 6239 Catalase-2 (EC 1.11.1.6) Was originally reported to play a role in determining adult lifespan. However, the paper was later retracted due to errors in the data. {ECO:0000305|PubMed:10335847, ECO:0000305|PubMed:12610632}. retracted-reference Q27487 ctl-2 Caenorhabditis elegans 6239 Peroxisomal catalase 1 (EC 1.11.1.6) (Catalase-2) Was originally reported to play a role in determining adult lifespan. However, the paper was later retracted due to errors in the data. {ECO:0000305|PubMed:10335847, ECO:0000305|PubMed:12610632}. retracted-reference A0A452E9Y6 LPO Capra hircus (Goat) 9925 Lactoperoxidase (LPO) (EC 1.11.1.7) The drug propylthiouracilin was reported to bind to the distal heme-pockets of LPO (PubMed:25760705). However, the paper was retracted as some concerns were raised about the modeling. {ECO:0000269|PubMed:25760705, ECO:0000305|PubMed:26057817}. retracted-reference P10844 botB Clostridium botulinum 1491 Botulinum neurotoxin type B (BoNT/B) (Bontoxilysin-B) [Cleaved into: Botulinum neurotoxin B light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin B heavy chain (HC)] A structure of a fragment of this protein in complex with the catalytic domain of C.botulinum neurotoxin type B (BoNT/B, botB) was reported; because of the lack of clear and continuous electron density for the VAMP2 peptide in the complex structure, the paper was retracted. One of its associated structures remains valid (PDB:1F82, light chain alone) (PubMed:10932255, PubMed:19578378). {ECO:0000269|PubMed:10932255, ECO:0000269|PubMed:19578378}. retracted-reference J9VW97 LIV4 Cryptococcus neoformans (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Cryptococcus neoformans var. grubii serotype A) 235443 DNA-binding protein LIV4 Article PMID:32391887 was retracted due undermined confidence in the construction of the deletion mutant and consequently the conclusions of the study. {ECO:0000305|PubMed:37849405}. retracted-reference Q66125 Cucumber mosaic virus (strain Q) (CMV) 12310 Suppressor of silencing 2b (Protein 2b) A paper showing a role as suppressor of RNA-mediated gene silencing has been retracted because of duplications in figures 5B and 6I of this paper. {ECO:0000305|PubMed:26286615}. retracted-reference P02283 His2B; His2B:CG17949; His2B:CG33868; His2B:CG33870; His2B:CG33872; His2B:CG33874; His2B:CG33876; His2B:CG33878; His2B:CG33880; His2B:CG33882; His2B:CG33884; His2B:CG33886; His2B:CG33888; His2B:CG33890; His2B:CG33892; His2B:CG33894; His2B:CG33896; His2B:CG33898; His2B:CG33900; His2B:CG33902; His2B:CG33904; His2B:CG33906; His2B:CG33908; His2B:CG33910 Drosophila melanogaster (Fruit fly) 7227 Histone H2B Was reported to be phosphorylated at Ser-34. However, the paper was retracted because some data, results and conclusions in the paper are not reliable. {ECO:0000305|PubMed:15143281, ECO:0000305|PubMed:24876484}. retracted-reference P51123 Taf1 Drosophila melanogaster (Fruit fly) 7227 Transcription initiation factor TFIID subunit 1 (EC 2.7.11.1) (TAFII250) (TBP-associated factor 230 kDa) (p230) (Transcription initiation factor TFIID 230 kDa subunit) (TAFII-230) The C-terminal Ser/Thr kinase domain was reported to phosphorylate histone H2B at 'Ser-34'. However, the paper was retracted because some data, results and conclusions in the paper are not reliable. {ECO:0000305|PubMed:15143281, ECO:0000305|PubMed:24876484}. retracted-reference Q9VW15 ash1 Drosophila melanogaster (Fruit fly) 7227 Histone-lysine N-methyltransferase ash1 (EC 2.1.1.354) (Absent small and homeotic disks protein 1) (Lysine N-methyltransferase 2H) Was reported to trimethylate H3 'Lys-9' and H4 'Lys-20' (PubMed:12397363). Was also reported to bind non-coding RNAs of trithorax response element (TRE) (PubMed:16497925). However, both papers were retracted because some data, results and conclusions are not reliable. {ECO:0000305|PubMed:12397363, ECO:0000305|PubMed:16497925}. retracted-reference Q9W0K7 bab1 Drosophila melanogaster (Fruit fly) 7227 Protein bric-a-brac 1 A paper showing that the protein forms homodimers via the BTB domain has been retracted by the authors, due to concerns regarding the validity of their data. However, they still consider that their main conclusions may be correct and require further testing. {ECO:0000305|PubMed:7760839}. retracted-reference P37624 rbbA Escherichia coli (strain K12) 83333 Ribosome-associated ATPase (Ribosomal bound ATPase) A deletion mutant has been described previously that shows significant loss of translation fidelity. Also previously shown to interact with yhjD. The publication was retracted due to image manipulation concerns. {ECO:0000305|PubMed:21556145, ECO:0000305|PubMed:40522897}. retracted-reference Q8X582 elfA Escherichia coli O157:H7 83334 Laminin-binding fimbrial subunit ElfA (ELF) Was shown to be required for adherence to mammalian host epithelial cells by binding specifically to laminin. However, the corresponding paper has been retracted due to evidence of digital manipulation of some of the data, making the conclusions unreliable. {ECO:0000305|PubMed:19508558, ECO:0000305|PubMed:38054536}. retracted-reference Q8XDD1 elfC Escherichia coli O157:H7 83334 Probable outer membrane usher protein ElfC Was shown to be involved in adherence to mammalian host epithelial cells by affecting the export and assembly of the ElfA fimbrial subunits across the outer membrane. However, the corresponding paper has been retracted due to evidence of digital manipulation of some of the data, making the conclusions unreliable. {ECO:0000305|PubMed:19508558, ECO:0000305|PubMed:38054536}. retracted-reference Q8X5E4 elfD Escherichia coli O157:H7 83334 Probable fimbrial chaperone protein ElfD Was shown to be involved in adherence to mammalian host epithelial cells through its role in the biogenesis of the ElfA fimbriae. However, the corresponding paper has been retracted due to evidence of digital manipulation of some of the data, making the conclusions unreliable. {ECO:0000305|PubMed:19508558, ECO:0000305|PubMed:38054536}. retracted-reference Q8XDC9 elfG Escherichia coli O157:H7 83334 Uncharacterized fimbrial-like protein ElfG Was shown to be involved in adherence to mammalian host epithelial cells. However, the corresponding paper has been retracted due to evidence of digital manipulation of some of the data, making the conclusions unreliable. {ECO:0000305|PubMed:19508558, ECO:0000305|PubMed:38054536}. retracted-reference P00362 gap Geobacillus stearothermophilus (Bacillus stearothermophilus) 1422 Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) PubMed:2684782 sequence was incorrect and retracted in PubMed:2227448. {ECO:0000305}. retracted-reference P04776 GY1 Glycine max (Soybean) (Glycine hispida) 3847 Glycinin G1 (Glycinin 11S G1) (Glycinin A1aB1b) (allergen Gly m 6) [Cleaved into: Glycinin A1a subunit (Glycinin acidic 1a subunit); Glycinin Bx subunit (Glycinin basic x subunit) (Glycinin B1b subunit) (Glycinin basic 1b subunit)] Has previously been shown to disrupt the membrane integrity and inhibit growth of L.monocytogenes, B.subtilis and S.enteritidis. The publication was retracted due to suspected image manipulation. {ECO:0000305|PubMed:22236762, ECO:0000305|PubMed:40912968}. retracted-reference P04405 GY2 Glycine max (Soybean) (Glycine hispida) 3847 Glycinin G2 (Glycinin 11S G2) (Glycinin A2B1a) (allergen Gly m 6) [Cleaved into: Glycinin A2 subunit; Glycinin B1a subunit] Has previously been shown to disrupt the membrane integrity and inhibit growth of L.monocytogenes, B.subtilis and S.enteritidis. The publication was retracted due to suspected image manipulation. {ECO:0000305|PubMed:22236762, ECO:0000305|PubMed:40912968}. retracted-reference P11828 GY3 Glycine max (Soybean) (Glycine hispida) 3847 Glycinin G3 (Glycinin 11S G3) (Glycinin A1bB2) (allergen Gly m 6) [Cleaved into: Glycinin A1b subunit (Glycinin A subunit); Glycinin B2 subunit (Glycinin B subunit)] Has previously been shown to disrupt the membrane integrity and inhibit growth of L.monocytogenes, B.subtilis and S.enteritidis. The publication was retracted due to suspected image manipulation. {ECO:0000305|PubMed:22236762, ECO:0000305|PubMed:40912968}. retracted-reference P02858 GY4 Glycine max (Soybean) (Glycine hispida) 3847 Glycinin G4 (Glycinin 11S G4) (Glycinin A5A4B3) (allergen Gly m 6) [Cleaved into: Glycinin A5 subunit; Glycinin A4 subunit; Glycinin B3 subunit] Has previously been shown to disrupt the membrane integrity and inhibit growth of L.monocytogenes, B.subtilis and S.enteritidis. The publication was retracted due to suspected image manipulation. {ECO:0000305|PubMed:22236762, ECO:0000305|PubMed:40912968}. retracted-reference P04347 GY5 Glycine max (Soybean) (Glycine hispida) 3847 Glycinin G5 (Glycinin 11S G5) (Glycinin A3B4) (allergen Gly m 6) [Cleaved into: Glycinin A3 subunit; Glycinin B4 subunit] Has previously been shown to disrupt the membrane integrity and inhibit growth of L.monocytogenes, B.subtilis and S.enteritidis. The publication was retracted due to suspected image manipulation. {ECO:0000305|PubMed:22236762, ECO:0000305|PubMed:40912968}. retracted-reference P33897 ABCD1 Homo sapiens (Human) 9606 ATP-binding cassette sub-family D member 1 (EC 3.1.2.-) (EC 7.6.2.-) (Adrenoleukodystrophy protein) (ALDP) Variants Trp-88, Cys-152, Cys-181, Ser-343, Pro-503, Arg-514 and His-554 have original been associated with ALD. However this paper was retracted due to inconsistencies in a confirmation immunoblot that could not be validated from the originally published data. {ECO:0000305|PubMed:15643618, ECO:0000305|PubMed:34337821}. retracted-reference P58397 ADAMTS12 Homo sapiens (Human) 9606 A disintegrin and metalloproteinase with thrombospondin motifs 12 (ADAM-TS 12) (ADAM-TS12) (ADAMTS-12) (EC 3.4.24.-) Was reported to be expressed in adult skeletal muscle and fat, in fetal lung, and in gastric carcinomas and cancer cells of diverse origin (PubMed:11279086). However, this paper has been retracted because data in one figure has been falsified (PubMed:30808000). {ECO:0000269|PubMed:11279086, ECO:0000269|PubMed:30808000}. retracted-reference Q400G9 AMZ1 Homo sapiens (Human) 9606 Archaemetzincin-1 (EC 3.4.-.-) (Archeobacterial metalloproteinase-like protein 1) An article reported the identification and characterization of this protein as zinc metalloprotease in different tissues; however, this paper was later retracted. {ECO:0000269|PubMed:15972818, ECO:0000305|PubMed:30808005}. retracted-reference Q86W34 AMZ2 Homo sapiens (Human) 9606 Archaemetzincin-2 (EC 3.4.-.-) (Archeobacterial metalloproteinase-like protein 2) An article reported the identification and characterization of this protein as zinc metalloprotease in different tissues; however, this paper was later retracted. {ECO:0000269|PubMed:15972818, ECO:0000305|PubMed:30808005}. retracted-reference Q6UXH0 ANGPTL8 Homo sapiens (Human) 9606 Angiopoietin-like protein 8 (Betatrophin) (Lipasin) (Refeeding-induced fat and liver protein) Initially reported to specifically promote pancreatic beta cell proliferation without insulin resistance and to promote beta cell mass expansion, thereby improving glucose tolerance (PubMed:23623304). However, this result could not be confirmed by further studies and the original paper was later retracted (PubMed:28038792). The lack of a role in beta cell proliferation was also confirmed in another study (PubMed:25417115). {ECO:0000269|PubMed:25417115, ECO:0000305|PubMed:23623304, ECO:0000305|PubMed:28038792}. retracted-reference Q8N6M6 AOPEP Homo sapiens (Human) 9606 Aminopeptidase O (AP-O) (EC 3.4.11.-) A paper describing the function, enzyme activity and expression patterns of this protein has been retracted due to concerns of image manipulation. {ECO:0000305|PubMed:15687497, ECO:0000305|PubMed:30808004}. retracted-reference P02652 APOA2 Homo sapiens (Human) 9606 Apolipoprotein A-II (Apo-AII) (ApoA-II) (Apolipoprotein A2) [Cleaved into: Proapolipoprotein A-II (ProapoA-II); Truncated apolipoprotein A-II (Apolipoprotein A-II(1-76))] A paper describing the crystal structure of this protein has been retracted due to evidence of fabricated data (see also US Office of Research Integrity Notice 2018-07782). {ECO:0000305|PubMed:12269810, ECO:0000305|PubMed:30278611}. retracted-reference P10275 AR Homo sapiens (Human) 9606 Androgen receptor (Dihydrotestosterone receptor) (Nuclear receptor subfamily 3 group C member 4) Had previously been shown to interact with PELP1. However this paper was retracted as cell-based data was viewed as unreliable. {ECO:0000305|PubMed:12415108, ECO:0000305|PubMed:19666546}. retracted-reference Q8IXJ9 ASXL1 Homo sapiens (Human) 9606 Polycomb group protein ASXL1 (Additional sex combs-like protein 1) Was previously reported to interact with KDM1A, CBX1, CBX3 and CBX5. However, this publication has been retracted. {ECO:0000305|PubMed:19880879, ECO:0000305|PubMed:25750265}. retracted-reference Q8WYN0 ATG4A Homo sapiens (Human) 9606 Cysteine protease ATG4A (EC 3.4.22.-) (AUT-like 2 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 2) (Autophagin-2) (Autophagy-related protein 4 homolog A) (HsAPG4A) (hAPG4A) A paper describing ATG4D tissue expression has been retracted, due to concerns of image duplication in some of the figures. {ECO:0000269|PubMed:12446702, ECO:0000305|PubMed:30808002}. retracted-reference Q9Y4P1 ATG4B Homo sapiens (Human) 9606 Cysteine protease ATG4B (EC 3.4.22.-) (AUT-like 1 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 1) (Autophagin-1) (Autophagy-related protein 4 homolog B) (HsAPG4B) (hAPG4B) A paper describing ATG4B tissue expression has been retracted, due to concerns of image duplication in some of the figures. {ECO:0000269|PubMed:12446702, ECO:0000305|PubMed:30808002}. retracted-reference Q96DT6 ATG4C Homo sapiens (Human) 9606 Cysteine protease ATG4C (EC 3.4.22.-) (AUT-like 3 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 3) (Autophagin-3) (Autophagy-related protein 4 homolog C) (HsAPG4C) A paper describing ATG4C tissue expression and activity has been retracted, due to concerns of image duplication in some of the figures. {ECO:0000269|PubMed:12446702, ECO:0000305|PubMed:30808002}. retracted-reference Q9UIG0 BAZ1B Homo sapiens (Human) 9606 Tyrosine-protein kinase BAZ1B (EC 2.7.10.2) (Bromodomain adjacent to zinc finger domain protein 1B) (Williams syndrome transcription factor) (Williams-Beuren syndrome chromosomal region 10 protein) (Williams-Beuren syndrome chromosomal region 9 protein) (hWALp2) Was shown to interact with VDR and with acetylated histones via its Bromo domain, but this work has later been retracted. {ECO:0000305|PubMed:16252006, ECO:0000305|PubMed:25452584}. retracted-reference Q9UL45 BLOC1S6 Homo sapiens (Human) 9606 Biogenesis of lysosome-related organelles complex 1 subunit 6 (BLOC-1 subunit 6) (Pallid protein homolog) (Pallidin) (Syntaxin 13-interacting protein) A paper showing involvement in Hermansky-Pudlak syndrome 9 was retracted due to image duplication. {ECO:0000269|PubMed:21665000, ECO:0000305|PubMed:28475864}. retracted-reference Q9NYX4 CALY Homo sapiens (Human) 9606 Neuron-specific vesicular protein calcyon Was originally thought to interact with the D1 dopamine receptor (DRD1) and to play a role in potentiating calcium ion-dependent signaling but this work was later retracted. {ECO:0000305|PubMed:10698743}.; retracted-reference Q7Z7J9 CAMK2N1 Homo sapiens (Human) 9606 Calcium/calmodulin-dependent protein kinase II inhibitor 1 (CaMKII inhibitory protein alpha) (CaMKIIN-alpha) There was previous evidence showing expression across a broad range of tissues. However this paper was retracted as immunoblot data was viewed as unreliable. {ECO:0000305|PubMed:18305109, ECO:0000305|PubMed:34237910}. retracted-reference P83916 CBX1 Homo sapiens (Human) 9606 Chromobox protein homolog 1 (HP1Hsbeta) (Heterochromatin protein 1 homolog beta) (HP1 beta) (Heterochromatin protein p25) (M31) (Modifier 1 protein) (p25beta) Was previously reported to interact with ASXL1. However, this publication has been retracted. {ECO:0000305|PubMed:19880879, ECO:0000305|PubMed:25750265}. retracted-reference Q13185 CBX3 Homo sapiens (Human) 9606 Chromobox protein homolog 3 (HECH) (Heterochromatin protein 1 homolog gamma) (HP1 gamma) (Modifier 2 protein) Was previously reported to interact with ASXL1. However, this publication has been retracted. {ECO:0000305|PubMed:19880879, ECO:0000305|PubMed:25750265}. retracted-reference P45973 CBX5 Homo sapiens (Human) 9606 Chromobox protein homolog 5 (Antigen p25) (Heterochromatin protein 1 homolog alpha) (HP1 alpha) Was previously reported to interact with ASXL1. However, this publication has been retracted. {ECO:0000305|PubMed:19880879, ECO:0000305|PubMed:25750265}. retracted-reference Q96S94 CCNL2 Homo sapiens (Human) 9606 Cyclin-L2 (Paneth cell-enhanced expression protein) The article reporting the nucleotide sequence of isoforms 1 and 2 with PMID:14684736 was retracted due to suspected data duplication affecting data regarding its function and physical interactions; the nucleotide sequence of the protein remains unchanged but its proposed role in the processing of apoptosis-related factors and interactions with POLR2A, SRSF2 and SRSF7 has been removed. {ECO:0000305|PubMed:14684736, ECO:0000305|PubMed:34237909}. retracted-reference Q12834 CDC20 Homo sapiens (Human) 9606 Cell division cycle protein 20 homolog (p55CDC) Originally thought to be phosphorylated by MPF during mitosis. However this paper was retracted due to falsification of data. {ECO:0000305|PubMed:10459014, ECO:0000305|PubMed:15824138}. retracted-reference P40199 CEACAM6 Homo sapiens (Human) 9606 Cell adhesion molecule CEACAM6 (Carcinoembryonic antigen-related cell adhesion molecule 6) (CEA cell adhesion molecule 6) (Non-specific crossreacting antigen) (Normal cross-reacting antigen) (CD antigen CD66c) Described to function in anoikis resistance and to be up-regulated in anoikis-resistant pancreatic adenocarcinoma cells in an article that was finally retracted. {ECO:0000269|PubMed:14724575, ECO:0000269|PubMed:36765147}. retracted-reference Q3ZCV2 CIMAP2 Homo sapiens (Human) 9606 Ciliary microtubule-associated protein 2 (Lymphocyte expansion molecule) Was reported to promote CD8+ T cell immunity through effects on mitochondrial respiration (PubMed:25883318). However, the corresponding article has been retracted (PubMed:27980177). retracted-reference P02462 COL4A1 Homo sapiens (Human) 9606 Collagen alpha-1(IV) chain [Cleaved into: Arresten] Was shown to inhibit expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation, and to function as a ligand for alpha1/beta1 integrin. However, this study was later retracted. {ECO:0000305|PubMed:16151532, ECO:0000305|PubMed:31895054}. retracted-reference P16870 CPE Homo sapiens (Human) 9606 Carboxypeptidase E (CPE) (EC 3.4.17.10) (Carboxypeptidase H) (CPH) (Enkephalin convertase) (Prohormone-processing carboxypeptidase) Isoform 2 was reported to be located in the nucleus and to interact with HDAC1 and HDAC2 (PubMed:21285511). However, this work was later retracted (PubMed:30882370). {ECO:0000305|PubMed:21285511, ECO:0000305|PubMed:30882370}. retracted-reference P35222 CTNNB1 Homo sapiens (Human) 9606 Catenin beta-1 (Beta-catenin) A paper showing an interaction with TBP and phosphorylation at Tyr-86 and Tyr-654 has been retracted due to panel duplication in several figures. {ECO:0000269|PubMed:11279024, ECO:0000305|PubMed:27226643}. retracted-reference Q92841 DDX17 Homo sapiens (Human) 9606 Probable ATP-dependent RNA helicase DDX17 (EC 3.6.4.13) (DEAD box protein 17) (DEAD box protein p72) (DEAD box protein p82) (RNA-dependent helicase p72) Was reported to act as a transcriptional coactivator for estrogen receptor ESR1 (PubMed:11250900). Although this publication was retracted because of aberrations in some figures, this function was also described in other publications by different groups and may be real (PubMed:19995069, PubMed:20406972, PubMed:20663877, PubMed:24275493). {ECO:0000269|PubMed:11250900, ECO:0000269|PubMed:19995069, ECO:0000269|PubMed:20406972, ECO:0000269|PubMed:20663877, ECO:0000269|PubMed:24275493}. retracted-reference P17844 DDX5 Homo sapiens (Human) 9606 Probable ATP-dependent RNA helicase DDX5 (EC 3.6.4.13) (DEAD box protein 5) (RNA helicase p68) DDX5 was reported to be a transcriptional coactivator of ESR1. However, this study has been retracted due to concerns of image manipulation. {ECO:0000305|PubMed:10409727, ECO:0000305|PubMed:11250900, ECO:0000305|PubMed:24509260, ECO:0000305|PubMed:25452582}. retracted-reference Q9BQI3 EIF2AK1 Homo sapiens (Human) 9606 Eukaryotic translation initiation factor 2-alpha kinase 1 (EC 2.7.11.1) (Heme-controlled repressor) (HCR) (Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase) (Heme-regulated inhibitor) (hHRI) (Hemin-sensitive initiation factor 2-alpha kinase) Was reported to be expressed predominantly in erythroid cells and at much lower levels in hepatocytes. However, this paper has been retracted because there was improper manipulation, reuse and analyses. {ECO:0000305|PubMed:20071449, ECO:0000305|PubMed:34404736}. retracted-reference P54851 EMP2 Homo sapiens (Human) 9606 Epithelial membrane protein 2 (EMP-2) (Protein XMP) Previously thought to be involved in cell migration via Src activation. The publication was retracted due to image manipulation. {ECO:0000305|PubMed:21637765, ECO:0000305|PubMed:36219627}. retracted-reference P28715 ERCC5 Homo sapiens (Human) 9606 DNA excision repair protein ERCC-5 (EC 3.1.-.-) (DNA repair protein complementing XP-G cells) (XPG) (Xeroderma pigmentosum group G-complementing protein) A paper describing an additional role for this protein in a base excision repair pathway that is not coupled to transcription has been retracted, because some of the experimental data were incorrect. {ECO:0000269|PubMed:9096355, ECO:0000305|PubMed:17179216}. retracted-reference Q03468 ERCC6 Homo sapiens (Human) 9606 DNA excision repair protein ERCC-6 (EC 3.6.4.-) (ATP-dependent helicase ERCC6) (Cockayne syndrome protein CSB) PubMed:16916636 was retracted due to image manipulations. {ECO:0000305|PubMed:34919821}. retracted-reference Q13216 ERCC8 Homo sapiens (Human) 9606 DNA excision repair protein ERCC-8 (Cockayne syndrome WD repeat protein CSA) PubMed:16916636 was retracted due to image manipulations. {ECO:0000305|PubMed:34919821}. retracted-reference P03372 ESR1 Homo sapiens (Human) 9606 Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) Was originally reported to be phosphorylated by CSNK1D/CK1. However, the corresponding article has been retracted. {ECO:0000305|PubMed:19339517, ECO:0000305|PubMed:34718754}.; retracted-reference Q92731 ESR2 Homo sapiens (Human) 9606 Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2) Had previously been shown to interact with PELP1. However this paper was retracted as cell-based data was viewed as unreliable. {ECO:0000305|PubMed:12415108, ECO:0000305|PubMed:19666546}. retracted-reference P22455 FGFR4 Homo sapiens (Human) 9606 Fibroblast growth factor receptor 4 (FGFR-4) (EC 2.7.10.1) (CD antigen CD334) An additional N-terminally truncated cytoplasmic isoform was previously reported to exist. However, the paper was subsequently retracted due to concerns regarding duplication of panels in some figures. {ECO:0000305|PubMed:11781352, ECO:0000305|PubMed:26237043}. retracted-reference Q9UM11 FZR1 Homo sapiens (Human) 9606 Fizzy-related protein homolog (Fzr) (CDC20-like protein 1) (Cdh1/Hct1 homolog) (hCDH1) Originally thought to be phosphorylated by MPF during mitosis. However this paper was retracted due to falsification of data. {ECO:0000305|PubMed:10459014, ECO:0000305|PubMed:15824138}. retracted-reference Q9UNW8 GPR132 Homo sapiens (Human) 9606 Probable G protein-coupled receptor 132 (G2 accumulation protein) Was originally thought to be a receptor for lysophosphatidylcholine (LPC) and sphingosylphosphorylcholine (SPC), However, this work has been retracted. {ECO:0000305|PubMed:11474113}. retracted-reference P46093 GPR4 Homo sapiens (Human) 9606 G protein-coupled receptor 4 (hGPR4) (G protein-coupled receptor 6C.l) (GPR6C.l) Was originally thought to be a receptor for sphingosylphosphorylcholine and lysophosphatidylcholine (PubMed:11535583). However, this work has been retracted (PubMed:16498716). {ECO:0000269|PubMed:11535583, ECO:0000305|PubMed:16498716}. retracted-reference Q15743 GPR68 Homo sapiens (Human) 9606 G protein-coupled receptor 68 (G protein-coupled receptor 12A) (GPR12A) (Ovarian cancer G protein-coupled receptor 1) (OGR-1) Was originally thought to be a receptor for sphingosylphosphorylcholine (SPC) (PubMed:10806476). However, this work has been retracted (PubMed:16508674). {ECO:0000305|PubMed:10806476, ECO:0000305|PubMed:16508674}. retracted-reference P62993 GRB2 Homo sapiens (Human) 9606 Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2) Was shown to interact with ZDHHC19, leading to recruitment of STAT3. However, this study was later retracted. {ECO:0000305|PubMed:31462771, ECO:0000305|PubMed:32555452}. retracted-reference P84243 H3-3A; H3-3B Homo sapiens (Human) 9606 Histone H3.3 The original paper reporting lysine deamination at Lys-5 by LOXL2 has been retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148). However, this modification was confirmed in a subsequent publication (PubMed:27735137). {ECO:0000269|PubMed:27735137, ECO:0000305|PubMed:22483618, ECO:0000305|PubMed:27392148}. retracted-reference Q71DI3 H3C15; H3C14; H3C13 Homo sapiens (Human) 9606 Histone H3.2 (H3-clustered histone 13) (H3-clustered histone 14) (H3-clustered histone 15) (Histone H3/m) (Histone H3/o) The original paper reporting lysine deamination at Lys-5 by LOXL2 has been retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148). However, this modification was confirmed in a subsequent publication (PubMed:27735137). {ECO:0000269|PubMed:27735137, ECO:0000305|PubMed:22483618, ECO:0000305|PubMed:27392148}. retracted-reference P68431 H3C1; H3C2; H3C3; H3C4; H3C6; H3C7; H3C8; H3C10; H3C11; H3C12 Homo sapiens (Human) 9606 Histone H3.1 (Histone H3/a) (Histone H3/b) (Histone H3/c) (Histone H3/d) (Histone H3/f) (Histone H3/h) (Histone H3/i) (Histone H3/j) (Histone H3/k) (Histone H3/l) The original paper reporting lysine deamination at Lys-5 by LOXL2 has been retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148). However, this modification was confirmed in a subsequent publication (PubMed:27735137). {ECO:0000269|PubMed:27735137, ECO:0000305|PubMed:22483618, ECO:0000305|PubMed:27392148}. retracted-reference P51610 HCFC1 Homo sapiens (Human) 9606 Host cell factor 1 (HCF) (HCF-1) (C1 factor) (CFF) (VCAF) (VP16 accessory protein) [Cleaved into: HCF N-terminal chain 1; HCF N-terminal chain 2; HCF N-terminal chain 3; HCF N-terminal chain 4; HCF N-terminal chain 5; HCF N-terminal chain 6; HCF C-terminal chain 1; HCF C-terminal chain 2; HCF C-terminal chain 3; HCF C-terminal chain 4; HCF C-terminal chain 5; HCF C-terminal chain 6] Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203}. retracted-reference P61978 HNRNPK Homo sapiens (Human) 9606 Heterogeneous nuclear ribonucleoprotein K (hnRNP K) (Transformation up-regulated nuclear protein) (TUNP) Was originally reported to be induced by DNA damage; the protein is also reported to interact with MDM2 and p53/TP53. However, the corresponding article has been retracted. {ECO:0000305|PubMed:16360036, ECO:0000305|PubMed:39389056}. retracted-reference O60341 KDM1A Homo sapiens (Human) 9606 Lysine-specific histone demethylase 1A (EC 1.14.11.-) (EC 1.14.11.65) (EC 1.14.99.66) (BRAF35-HDAC complex protein BHC110) (Flavin-containing amine oxidase domain-containing protein 2) ([histone H3]-dimethyl-L-lysine(4) FAD-dependent demethylase 1A) Was previously reported to interact with ASXL1. However, this publication has been retracted. {ECO:0000305|PubMed:19880879, ECO:0000305|PubMed:25750265}.; retracted-reference Q8IZD2 KMT2E Homo sapiens (Human) 9606 Histone reader KMT2E (Inactive histone-lysine N-methyltransferase 2E) (Inactive lysine N-methyltransferase 2E) (Myeloid/lymphoid or mixed-lineage leukemia protein 5) Isoform 3 was originally thought to display histone methyltransferase activity only following O-glycosylation at Thr-440 (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203). Does not exhibit histone methyltransferase towards histone H3 in vitro (PubMed:19264965, PubMed:27812132). The isolated catalytic SET domain lacks binding activity towards cofactor S-adenosyl-L-methionine; instead of the highly conserved XGXG, Y and NH motifs, KMT2E displays NKKI (Asn-339-Ile-342), F (Phe-381) and RR (Arg-408-Arg-409) motifs (PubMed:27812132). Also lacks binding activity towards histone H3 due to a poor conservation of the key residues involved in the binding and the presence of large loop which prevents the docking of the H3 'Lys-4' side chain (PubMed:27812132). {ECO:0000269|PubMed:19264965, ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203, ECO:0000269|PubMed:27812132}. retracted-reference O95970 LGI1 Homo sapiens (Human) 9606 Leucine-rich glioma-inactivated protein 1 (Epitempin-1) Was originally reported to be down-regulated in neuroblastoma cells and may play a role in the control of neuroblastoma cell survival. However, the corresponding article has been retracted. {ECO:0000305|PubMed:16518856, ECO:0000305|PubMed:39221895}. retracted-reference Q96S06 LMF1 Homo sapiens (Human) 9606 Lipase maturation factor 1 (Transmembrane protein 112) Additional evidence for its localization to the endoplasmic reticulum membrane was found. However this paper was retracted due to manipulation of data. {ECO:0000305|PubMed:19783858, ECO:0000305|PubMed:31399538}. retracted-reference Q9Y4K0 LOXL2 Homo sapiens (Human) 9606 Lysyl oxidase homolog 2 (EC 1.4.3.13) (Lysyl oxidase-like protein 2) (Lysyl oxidase-related protein 2) (Lysyl oxidase-related protein WS9-14) The original paper reporting the role of LOXL2 in deamination of trimethylated 'Lys-4' of histone H3 was retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148). However, this role was confirmed in a subsequent publication (PubMed:27735137). {ECO:0000269|PubMed:27735137, ECO:0000305|PubMed:22483618, ECO:0000305|PubMed:27392148}. retracted-reference P41279 MAP3K8 Homo sapiens (Human) 9606 Mitogen-activated protein kinase kinase kinase 8 (EC 2.7.11.25) (Cancer Osaka thyroid oncogene) (Proto-oncogene c-Cot) (Serine/threonine-protein kinase cot) (Tumor progression locus 2) (TPL-2) A paper describing a role for this protein in IRAK1-independent activation of the MAPK/ERK pathway in response to IL1 has been retracted, because some of the experimental data could not be reproduced. {ECO:0000305|PubMed:19754427, ECO:0000305|PubMed:24325551}. retracted-reference Q9UIS9 MBD1 Homo sapiens (Human) 9606 Methyl-CpG-binding domain protein 1 (CXXC-type zinc finger protein 3) (Methyl-CpG-binding protein MBD1) (Protein containing methyl-CpG-binding domain 1) Was reported to recruit SETDB1 during DNA replication, to form a S phase-specific complex that would facilitate methylation of H3 'Lys-9' during replication-coupled chromatin assembly and vould be at least composed of the CAF-1 subunit CHAF1A, MBD1 and SETDB1 (PubMed:15327775). The interaction with SETDB1 was also reported to be inhibited by sumoylation at Lys-499 and Lys-538 (PubMed:17066076). However, these papers have been retracted because some data, results and conclusions are not reliable (PubMed:30849389, PubMed:31612521). {ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:17066076, ECO:0000269|PubMed:30849389, ECO:0000269|PubMed:31612521}. retracted-reference Q8N6R0 METTL13 Homo sapiens (Human) 9606 eEF1A lysine and N-terminal methyltransferase (eEF1A-KNMT) (Methyltransferase-like protein 13) [Includes: eEF1A lysine methyltransferase (EC 2.1.1.-); eEF1A N-terminal methyltransferase (EC 2.1.1.-)] Was thought to negatively regulate cell proliferation at G1/S transition via transcriptional suppression of cell cycle regulatory genes. However this publication has been retracted due to unexplained image anomalies. {ECO:0000305|PubMed:37488192}. retracted-reference Q9H8L6 MMRN2 Homo sapiens (Human) 9606 Multimerin-2 (EMILIN-3) (Elastin microfibril interface located protein 3) (Elastin microfibril interfacer 3) (EndoGlyx-1 p125/p140 subunit) Was originally thought to play significant roles in the vascular system and to be required for the maintenance and stability of blood vessels; also thought to be processed by matrix metalloproteinases (MMPs) including MMP9 and, to a lesser degree, by MMP2 upon angiogenic stimulation (PubMed:28435016). However, the corresponding article has been retracted (PubMed:41107108). {ECO:0000269|PubMed:28435016, ECO:0000269|PubMed:41107108}. retracted-reference Q00013 MPP1 Homo sapiens (Human) 9606 55 kDa erythrocyte membrane protein (p55) (Membrane protein, palmitoylated 1) Thought to be palmitoylated by ZDHHC17 (PubMed:22496366). This work was later retracted due to image manipulation (PubMed:29475958). {ECO:0000269|PubMed:22496366, ECO:0000269|PubMed:29475958}. retracted-reference Q969H8 MYDGF Homo sapiens (Human) 9606 Myeloid-derived growth factor (MYDGF) Was originally thought to signal lymphoid cells to proliferate via thymic shared antigen 1 (PubMed:11714798). This work was later retracted (PubMed:12538725). {ECO:0000305|PubMed:11714798, ECO:0000305|PubMed:12538725}.; retracted-reference Q15788 NCOA1 Homo sapiens (Human) 9606 Nuclear receptor coactivator 1 (NCoA-1) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 74) (bHLHe74) (Protein Hin-2) (RIP160) (Renal carcinoma antigen NY-REN-52) (Steroid receptor coactivator 1) (SRC-1) Was previously reported to interact with DDX1. However the paper was retracted because certain images were duplicated, leading to concerns regarding the findings of the manuscript. {ECO:0000305|PubMed:11250900, ECO:0000305|PubMed:25452582}. retracted-reference Q15596 NCOA2 Homo sapiens (Human) 9606 Nuclear receptor coactivator 2 (NCoA-2) (Class E basic helix-loop-helix protein 75) (bHLHe75) (Transcriptional intermediary factor 2) (hTIF2) Was previously reported to interact with DDX1. However the paper was retracted because certain images were duplicated, leading to concerns regarding the findings of the manuscript. {ECO:0000305|PubMed:11250900, ECO:0000305|PubMed:25452582}. retracted-reference Q9Y6Q9 NCOA3 Homo sapiens (Human) 9606 Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (ACTR) (Amplified in breast cancer 1 protein) (AIB-1) (CBP-interacting protein) (pCIP) (Class E basic helix-loop-helix protein 42) (bHLHe42) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (TRAM-1) Was previously reported to interact with DDX1. However the paper was retracted because certain images were duplicated, leading to concerns regarding the findings of the manuscript. {ECO:0000305|PubMed:11250900, ECO:0000305|PubMed:25452582}.; retracted-reference Q9HC98 NEK6 Homo sapiens (Human) 9606 Serine/threonine-protein kinase Nek6 (EC 2.7.11.34) (Never in mitosis A-related kinase 6) (NimA-related protein kinase 6) (Protein kinase SID6-1512) A paper showing a role in tumorigenesis has been retracted due to panel duplication in several figures. {ECO:0000269|PubMed:20407017, ECO:0000305|PubMed:28250205}. retracted-reference Q9UBE8 NLK Homo sapiens (Human) 9606 Serine/threonine-protein kinase NLK (EC 2.7.11.24) (Nemo-like kinase) (Protein LAK1) Was reported to form a transcriptional repressor complex with CHD7 and SETDB1 involved in PPARG repression (PubMed:17952062). However, this work was later retracted (PubMed:25358353). {ECO:0000269|PubMed:17952062, ECO:0000269|PubMed:25358353}. retracted-reference P04150 NR3C1 Homo sapiens (Human) 9606 Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1) Had previously been shown to interact with PELP1. However this paper was retracted as cell-based data was viewed as unreliable. {ECO:0000305|PubMed:12415108, ECO:0000305|PubMed:19666546}. retracted-reference O15294 OGT Homo sapiens (Human) 9606 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC 2.4.1.255) (O-GlcNAc transferase subunit p110) (O-linked N-acetylglucosamine transferase 110 kDa subunit) (OGT) Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203}. retracted-reference Q9UJX0 OSGIN1 Homo sapiens (Human) 9606 Oxidative stress-induced growth inhibitor 1 (EC 1.14.13.-) (Bone marrow stromal cell-derived growth inhibitor) (BMSC-derived growth inhibitor) (Ovary, kidney and liver protein 38) (huOKL38) (Pregnancy-induced growth inhibitor OKL38) The article reporting the nucleotide sequence with PMID:15569677 was retracted due to suspected data duplication; the nucleotide sequence of the protein remains unchanged. {ECO:0000305|PubMed:15569677, ECO:0000305|PubMed:34237895}. retracted-reference Q96S96 PEBP4 Homo sapiens (Human) 9606 Phosphatidylethanolamine-binding protein 4 (PEBP-4) (hPEBP4) (Protein cousin-of-RKIP 1) It was previously reported that PEBP4 is a lysosomal protein which is highly expressed in tumor cells, and may promote cellular resistance to TNF-induced apoptosis. However the paper has since been retracted by the journal due to concerns of image manipulation. {ECO:0000305|PubMed:15302887, ECO:0000305|PubMed:32978330}. retracted-reference Q86TG7 PEG10 Homo sapiens (Human) 9606 Retrotransposon-derived protein PEG10 (Embryonal carcinoma differentiation-regulated protein) (Mammalian retrotransposon-derived protein 2) (Myelin expression factor 3-like protein 1) (MEF3-like protein 1) (Paternally expressed gene 10 protein) (Retrotransposon gag domain-containing protein 3) (Retrotransposon-derived gag-like polyprotein) (Ty3/Gypsy-like protein) Was reported to be activated by androgen receptor agonist dihydrotestosterone (DHT) in hepatic cancer cells (HCC), resulting in HCC growth and apoptotic resistance. However, this study was later retracted. {ECO:0000305|PubMed:17369855, ECO:0000305|PubMed:21677654}. retracted-reference Q8IZL8 PELP1 Homo sapiens (Human) 9606 Proline-, glutamic acid- and leucine-rich protein 1 (Modulator of non-genomic activity of estrogen receptor) (Transcription factor HMX3) There was previous evidence for interactions with AR, NR3C1 and ESR2. However this paper was retracted as cell-based data was viewed as unreliable. {ECO:0000305|PubMed:12415108, ECO:0000305|PubMed:19666546}. retracted-reference O75925 PIAS1 Homo sapiens (Human) 9606 E3 SUMO-protein ligase PIAS1 (EC 2.3.2.-) (DEAD/H box-binding protein 1) (E3 SUMO-protein transferase PIAS1) (Gu-binding protein) (GBP) (Protein inhibitor of activated STAT protein 1) (RNA helicase II-binding protein) A paper showing that PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling has been retracted, because some of the data was found to be deliberately falsified. {ECO:0000305|PubMed:19136629, ECO:0000305|PubMed:21724836}. retracted-reference Q9UL19 PLAAT4 Homo sapiens (Human) 9606 Phospholipase A and acyltransferase 4 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (HRAS-like suppressor 4) (HRSL4) (RAR-responsive protein TIG3) (Retinoic acid receptor responder protein 3) (Retinoid-inducible gene 1 protein) (Tazarotene-induced gene 3 protein) Was originally reported to promote keratinocyte differentiation via activation of TGM1. However, the corresponding article has been retracted. {ECO:0000305|PubMed:17762858, ECO:0000305|PubMed:40409913}. retracted-reference Q96S99 PLEKHF1 Homo sapiens (Human) 9606 Pleckstrin homology domain-containing family F member 1 (PH domain-containing family F member 1) (Lysosome-associated apoptosis-inducing protein containing PH and FYVE domains) (Apoptosis-inducing protein) (PH and FYVE domain-containing protein 1) (Phafin-1) (Zinc finger FYVE domain-containing protein 15) Was originally reported to induce apoptosis through the lysosomal-mitochondrial pathway; was also reported to be widely expressed in the nucleus, perinuclear region and lysosome. However, the corresponding article has been retracted. This article also provides the mRNA sequencing data and that information appears to be still valid. {ECO:0000305, ECO:0000305|PubMed:16188880, ECO:0000305|PubMed:34237888}. retracted-reference O75417 POLQ Homo sapiens (Human) 9606 DNA polymerase theta (DNA polymerase eta) [Includes: Helicase POLQ (EC 5.6.2.4); DNA polymerase POLQ (EC 2.7.7.7) (RNA-directed DNA polymerase POLQ) (EC 2.7.7.49)] A publication reported some endonuclease activity required to trim the 3' ends before synthesis can occur. However, subsequent research from the same group showed that DNA synthesis products generated by POLQ that migrate more quickly on denaturing polyacrylamide gels arise by production of stable stem-loop structures rather than from nuclease activity (PubMed:38640889). The original publication was therefore retracted. {ECO:0000269|PubMed:38640889, ECO:0000305|PubMed:33577776, ECO:0000305|PubMed:38640897}.; retracted-reference P24928 POLR2A Homo sapiens (Human) 9606 DNA-directed RNA polymerase II subunit RPB1 (RNA polymerase II subunit B1) (EC 2.7.7.6) (3'-5' exoribonuclease) (EC 3.1.13.-) (DNA-directed RNA polymerase II subunit A) (DNA-directed RNA polymerase III largest subunit) (RNA-directed RNA polymerase II subunit RPB1) (EC 2.7.7.48) The paper showing an interaction with CCNL2 was retracted due to suspected data duplication that affected the interaction data. {ECO:0000305|PubMed:14684736, ECO:0000305|PubMed:34237909}. retracted-reference P62136 PPP1CA Homo sapiens (Human) 9606 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16) Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203}. retracted-reference P62140 PPP1CB Homo sapiens (Human) 9606 Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (PPP1CD) (EC 3.1.3.16) (EC 3.1.3.53) Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203}. retracted-reference P36873 PPP1CC Homo sapiens (Human) 9606 Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit) Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203}. retracted-reference Q99873 PRMT1 Homo sapiens (Human) 9606 Protein arginine N-methyltransferase 1 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT1) (Interferon receptor 1-bound protein 4) A paper showing that PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling has been retracted, because some of the data was found to be deliberately falsified. {ECO:0000305|PubMed:19136629, ECO:0000305|PubMed:21724836}. retracted-reference P43119 PTGIR Homo sapiens (Human) 9606 Prostacyclin receptor (Prostaglandin I2 receptor) (PGI receptor) (PGI2 receptor) (Prostanoid IP receptor) Palmitoylation of either Cys-308 or Cys-311 was reported to be sufficient to maintain functional coupling to G(s) proteins and signaling (PubMed:12488443). However, this publication was retracted due to figure duplication. {ECO:0000269|PubMed:12488443, ECO:0000305|PubMed:27613955}. retracted-reference Q03431 PTH1R Homo sapiens (Human) 9606 Parathyroid hormone/parathyroid hormone-related peptide receptor (PTH/PTHrP type I receptor) (PTH/PTHr receptor) (Parathyroid hormone 1 receptor) (PTH1 receptor) Was shown to interact with G protein subunit GNB1 and GNG2, the interaction was reduced by mutation of Trp-474 and Trp-477. However this paper was retracted due to a lack of clear and continous electron density in the complex structure. {ECO:0000305|PubMed:18611381, ECO:0000305|PubMed:21827955}.; retracted-reference Q12913 PTPRJ Homo sapiens (Human) 9606 Receptor-type tyrosine-protein phosphatase eta (Protein-tyrosine phosphatase eta) (R-PTP-eta) (EC 3.1.3.48) (Density-enhanced phosphatase 1) (DEP-1) (HPTP eta) (Protein-tyrosine phosphatase receptor type J) (R-PTP-J) (CD antigen CD148) Originally thought to dephosphorylate RET. However this paper was retracted due to manipulation of immunoblot data. {ECO:0000305|PubMed:16778204, ECO:0000305|PubMed:30552125}. retracted-reference Q99708 RBBP8 Homo sapiens (Human) 9606 DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2) Upon DNA damage, was shown to interact with SIRT6 resulting in its deacetylation. However, this study was later retracted. {ECO:0000305|PubMed:20829486, ECO:0000305|PubMed:30975768}. retracted-reference P07949 RET Homo sapiens (Human) 9606 Proto-oncogene tyrosine-protein kinase receptor Ret (EC 2.7.10.1) (Cadherin family member 12) (Proto-oncogene c-Ret) [Cleaved into: Soluble RET kinase fragment; Extracellular cell-membrane anchored RET cadherin 120 kDa fragment] Original thought to be dephosphorylated by PTPRJ on Tyr-905, Tyr-1015 and Tyr-1062. However this paper was retracted due to manipulation of immunoblot data. {ECO:0000305|PubMed:16778204, ECO:0000305|PubMed:30552125}. retracted-reference Q15047 SETDB1 Homo sapiens (Human) 9606 Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.366) (ERG-associated protein with SET domain) (ESET) (Histone H3-K9 methyltransferase 4) (H3-K9-HMTase 4) (Lysine N-methyltransferase 1E) (SET domain bifurcated 1) Was reported to be recruited by MBD1, during DNA replication, to form a S phase-specific complex that would facilitate methylation of H3 'Lys-9' during replication-coupled chromatin assembly and would be at least composed of the CAF-1 subunit CHAF1A, MBD1 and SETDB1 (PubMed:15327775, PubMed:17066076). However, these papers have been retracted because some data, results and conclusions are not reliable (PubMed:30849389, PubMed:31612521). {ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:17066076, ECO:0000269|PubMed:30849389, ECO:0000269|PubMed:31612521}.; retracted-reference Q8N6T7 SIRT6 Homo sapiens (Human) 9606 NAD-dependent protein deacylase sirtuin-6 (EC 2.3.1.-) (NAD-dependent protein deacetylase sirtuin-6) (EC 2.3.1.286) (Protein mono-ADP-ribosyltransferase sirtuin-6) (EC 2.4.2.-) (Regulatory protein SIR2 homolog 6) (hSIRT6) (SIR2-like protein 6) Upon DNA damage, was reported to promote DNA end resection via deacetylation of RBBP8. However, this study was later retracted. {ECO:0000305|PubMed:20829486, ECO:0000305|PubMed:30975768}.; retracted-reference Q9NRC8 SIRT7 Homo sapiens (Human) 9606 NAD-dependent protein deacetylase sirtuin-7 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-7) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 7) (SIR2-like protein 7) Was originally termed SIR-T8/SIRT8 (PubMed:11953824). This was later retracted (PubMed:12454780, PubMed:12454781). {ECO:0000303|PubMed:11953824, ECO:0000303|PubMed:12454780, ECO:0000303|PubMed:12454781}. retracted-reference P31645 SLC6A4 Homo sapiens (Human) 9606 Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4) Was reported to interact with VIM, however the paper was retracted as some results and conclusions are not reliable. {ECO:0000269|PubMed:19270731, ECO:0000305|PubMed:30707744}.; retracted-reference O94813 SLIT2 Homo sapiens (Human) 9606 Slit homolog 2 protein (Slit-2) [Cleaved into: Slit homolog 2 protein N-product; Slit homolog 2 protein C-product] Was previously reported to silence the attractive effect of NTN1. However, the article has been retracted because certain micrograph and Western blot images were duplicated, leading to concerns about the findings in the manuscript. {ECO:0000305|PubMed:11239147, ECO:0000305|PubMed:36520150}. retracted-reference O94875 SORBS2 Homo sapiens (Human) 9606 Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin) Was shown to interact with AKT1 and PAK1 (PubMed:15784622). This work has later been retracted due to concerns of image manipulation. {ECO:0000269|PubMed:15784622, ECO:0000305|PubMed:27825083}. retracted-reference Q01130 SRSF2 Homo sapiens (Human) 9606 Serine/arginine-rich splicing factor 2 (Protein PR264) (Splicing component, 35 kDa) (Splicing factor SC35) (SC-35) (Splicing factor, arginine/serine-rich 2) The paper showing an interaction with CCNL2 was retracted due to suspected data duplication that affected the interaction data. {ECO:0000305|PubMed:14684736, ECO:0000305|PubMed:34237909}. retracted-reference Q16629 SRSF7 Homo sapiens (Human) 9606 Serine/arginine-rich splicing factor 7 (Splicing factor 9G8) (Splicing factor, arginine/serine-rich 7) The paper showing an interaction with CCNL2 was retracted due to suspected data duplication that affected the interaction data. {ECO:0000305|PubMed:14684736, ECO:0000305|PubMed:34237909}. retracted-reference Q8N3U4 STAG2 Homo sapiens (Human) 9606 Cohesin subunit SA-2 (SCC3 homolog 2) (Stromal antigen 2) Variants MKMS 743-Trp--Phe-1231 DEL and HPE13 1033-Arg--Phe-1231 DEL were previously described; however, the corresponding paper has been retracted as Case 1's sex was incorrectly reported invalidating the conclusions. {ECO:0000269|PubMed:30765867, ECO:0000305|PubMed:32536687}. retracted-reference P42229 STAT5A Homo sapiens (Human) 9606 Signal transducer and activator of transcription 5A It was reported that dephosphorylation on tyrosine residues by PTPN2 would negatively regulate prolactin signaling pathway (PubMed:11773439). However, the corresponding article has been retracted (PubMed:24319783). {ECO:0000269|PubMed:11773439, ECO:0000303|PubMed:24319783}. retracted-reference P51692 STAT5B Homo sapiens (Human) 9606 Signal transducer and activator of transcription 5B It was reported that dephosphorylation on tyrosine residues by PTPN2 would negatively regulate prolactin signaling pathway (PubMed:11773439). However, the corresponding article has been retracted (PubMed:24319783). {ECO:0000269|PubMed:11773439, ECO:0000303|PubMed:24319783}. retracted-reference Q13188 STK3 Homo sapiens (Human) 9606 Serine/threonine-protein kinase 3 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 2) (MST-2) (STE20-like kinase MST2) (Serine/threonine-protein kinase Krs-1) [Cleaved into: Serine/threonine-protein kinase 3 36kDa subunit (MST2/N); Serine/threonine-protein kinase 3 20kDa subunit (MST2/C)] PUBMED:20231902 has been retracted because there was evidence of data fabrication and/or falsification in multiple figure panels. {ECO:0000305|PubMed:20231902, ECO:0000305|PubMed:37490513}. retracted-reference Q15208 STK38 Homo sapiens (Human) 9606 Serine/threonine-protein kinase 38 (EC 2.7.11.1) (NDR1 protein kinase) (Nuclear Dbf2-related kinase 1) Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203}. retracted-reference Q13043 STK4 Homo sapiens (Human) 9606 Serine/threonine-protein kinase 4 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 1) (MST-1) (STE20-like kinase MST1) (Serine/threonine-protein kinase Krs-2) [Cleaved into: Serine/threonine-protein kinase 4 37kDa subunit (MST1/N); Serine/threonine-protein kinase 4 18kDa subunit (MST1/C)] Was originally thought to be phosphorylated at Thr-120 (PubMed:19940129). However, this work has been retracted (PubMed:27825096). {ECO:0000269|PubMed:19940129, ECO:0000305|PubMed:27825096}. retracted-reference Q15633 TARBP2 Homo sapiens (Human) 9606 RISC-loading complex subunit TARBP2 (TAR RNA-binding protein 2) (Trans-activation-responsive RNA-binding protein) A paper describing truncating mutations of TARBP2 in tumor cells and resultant effects on DICER1 stability and miRNA processing has been retracted, due to concerns of image duplication in some of the figures. {ECO:0000305|PubMed:19219043, ECO:0000305|PubMed:26813765}. retracted-reference Q9Y6G1 TMEM14A Homo sapiens (Human) 9606 Transmembrane protein 14A Was originally thought to be expressed at significantly higher levels in ovarian cancer tissues than in normal tissues (at protein level) (PMID:26896463). However, the corresponding article has been retracted (PMID:37083009). {ECO:0000269|PubMed:26896463, ECO:0000269|PubMed:37083009}. retracted-reference Q8IU80 TMPRSS6 Homo sapiens (Human) 9606 Transmembrane protease serine 6 (EC 3.4.21.-) (Matriptase-2) A study described a function as serine protease towards extracellular matrix proteins in the liver; however, this article was later retracted. {ECO:0000269|PubMed:12149247, ECO:0000305|PubMed:30808001}. retracted-reference Q12933 TRAF2 Homo sapiens (Human) 9606 TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2) (Tumor necrosis factor type 2 receptor-associated protein 3) Was reported to interact with IL15RA (PubMed:10463949). However, this work was later retracted (PubMed:21357251). {ECO:0000305|PubMed:10463949, ECO:0000305|PubMed:21357251}. retracted-reference Q13107 USP4 Homo sapiens (Human) 9606 Ubiquitin carboxyl-terminal hydrolase 4 (EC 3.4.19.12) (Deubiquitinating enzyme 4) (Ubiquitin thioesterase 4) (Ubiquitin-specific-processing protease 4) (Ubiquitous nuclear protein homolog) The ubiquitin-like domain 2 was thought to interact with the catalytic domain competing with the ubiquitin substrate and thus partially inhibiting USP4 activity (PubMed:21415856). As the results could not be reproduced this work was later retracted (PubMed:24398133). The cristal structure in the paper was correct and was republished later (PubMed:25404403). {ECO:0000269|PubMed:21415856, ECO:0000269|PubMed:24398133, ECO:0000269|PubMed:25404403}. retracted-reference P63027 VAMP2 Homo sapiens (Human) 9606 Vesicle-associated membrane protein 2 (VAMP-2) (Synaptobrevin-2) A structure of a fragment of this protein in complex with the catalytic domain of C.botulinum neurotoxin type B (BoNT/B, botB) was reported; because of the lack of clear and continuous electron density for the VAMP2 peptide in the complex structure, the paper was retracted (PubMed:10932255, PubMed:19578378). However this protein is a substrate for BoNT/B (PubMed:22289120, PubMed:7803399). {ECO:0000269|PubMed:10932255, ECO:0000269|PubMed:19578378, ECO:0000269|PubMed:7803399, ECO:0000305|PubMed:22289120}. retracted-reference P08670 VIM Homo sapiens (Human) 9606 Vimentin Was reported to interact with SLC6A4, however the paper was retracted as some results and conclusions are not reliable. {ECO:0000269|PubMed:19270731, ECO:0000305|PubMed:30707744}. retracted-reference Q3ZAQ7 VMA21 Homo sapiens (Human) 9606 Vacuolar ATPase assembly integral membrane protein VMA21 (Myopathy with excessive autophagy protein) Protein characterization data are from PubMed:19379691. Due to a number of errors in the figure panels, the article has been retracted but the authors stand by the validity of the main results and conclusions (PubMed:20873370). {ECO:0000305|PubMed:19379691, ECO:0000305|PubMed:20873370}. retracted-reference Q14508 WFDC2 Homo sapiens (Human) 9606 WAP four-disulfide core domain protein 2 (Epididymal secretory protein E4) (Major epididymis-specific protein E4) (Putative protease inhibitor WAP5) Previously thought to be a broad range protease inhibitor that formed homotrimers. The publication was retracted due to image manipulation. {ECO:0000305|PubMed:23139753, ECO:0000305|PubMed:38861541}. retracted-reference P98170 XIAP Homo sapiens (Human) 9606 E3 ubiquitin-protein ligase XIAP (EC 2.3.2.27) (Baculoviral IAP repeat-containing protein 4) (IAP-like protein) (ILP) (hILP) (Inhibitor of apoptosis protein 3) (IAP-3) (hIAP-3) (hIAP3) (RING-type E3 ubiquitin transferase XIAP) (X-linked inhibitor of apoptosis protein) (X-linked IAP) Was originally shown to be phosphorylated at Ser-87 by PKB, protecting the protein from ubiquitination and proteasomal degradation (PubMed:14645242). However, this work was later retracted (PubMed:27825084). {ECO:0000305|PubMed:14645242, ECO:0000305|PubMed:27825084}. retracted-reference Q8IUH5 ZDHHC17 Homo sapiens (Human) 9606 Palmitoyltransferase ZDHHC17 (EC 2.3.1.225) (Acyltransferase ZDHHC17) (EC 2.3.1.-) (DHHC domain-containing cysteine-rich protein 17) (DHHC17) (Huntingtin yeast partner H) (Huntingtin-interacting protein 14) (HIP-14) (Huntingtin-interacting protein 3) (HIP-3) (Huntingtin-interacting protein H) (Putative MAPK-activating protein PM11) (Putative NF-kappa-B-activating protein 205) (Zinc finger DHHC domain-containing protein 17) Thought to palmitoylate MPP1 (PubMed:22496366). This work was later retracted due to image manipulation. {ECO:0000269|PubMed:22496366, ECO:0000305|PubMed:29475958}. retracted-reference Q8WVZ1 ZDHHC19 Homo sapiens (Human) 9606 Palmitoyltransferase ZDHHC19 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 19) (DHHC-19) Was shown to mediate palmitoylation of STAT3, leading to homodimerization and transcriptional activation of STAT3. However, this study was later retracted. {ECO:0000305|PubMed:31462771, ECO:0000305|PubMed:32555452}. retracted-reference P05777 M Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) 381518 Matrix protein 1 (M1) An article reported mutagenesis experiments; however, this paper was later retracted. {ECO:0000305|PubMed:17005709}. retracted-reference K9N4V0 ORF4a Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1) 1263720 Non-structural protein ORF4a (ORF4a) Previously shown to interact with host PRKRA and induce activation of RIGI and MDA5. The publication was retracted due to image manipulation concerns. {ECO:0000305|PubMed:24522921, ECO:0000305|PubMed:36314823}. retracted-reference E9Q394 Akap13 Mus musculus (Mouse) 10090 A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc) An article confirming some elements of the function, the interaction with PKA and PRKD1 was finally retracted. {ECO:0000269|PubMed:23658642, ECO:0000269|PubMed:38085732}. retracted-reference P07724 Alb Mus musculus (Mouse) 10090 Albumin Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference B8JKV0 Amn1 Mus musculus (Mouse) 10090 Protein AMN1 homolog Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q8R1L8 Angptl8 Mus musculus (Mouse) 10090 Angiopoietin-like protein 8 (Betatrophin) (Lipasin) (Refeeding-induced fat and liver protein) Initially reported to specifically promote pancreatic beta cell proliferation without insulin resistance and to promote beta cell mass expansion, thereby improving glucose tolerance (PubMed:23623304). However, this result could not be confirmed by further studies and the original paper was later retracted (PubMed:28038792). The lack of a role in beta cell proliferation was also confirmed in another study (PubMed:25417115). {ECO:0000269|PubMed:25417115, ECO:0000305|PubMed:23623304, ECO:0000305|PubMed:28038792}. retracted-reference Q8BXQ6 Aopep Mus musculus (Mouse) 10090 Aminopeptidase O (AP-O) (EC 3.4.11.-) A paper describing the expression patterns of this protein has been retracted due to concerns of image manipulation. {ECO:0000305|PubMed:15687497, ECO:0000305|PubMed:30808004}. retracted-reference P59598 Asxl1 Mus musculus (Mouse) 10090 Polycomb group protein ASXL1 (Additional sex combs-like protein 1) Was reported to act as a corepressor through recruitment of KDM1A and CBX; this publication has been retracted. {ECO:0000269|PubMed:19880879}. retracted-reference Q811C2 Atg4c Mus musculus (Mouse) 10090 Cysteine protease ATG4C (EC 3.4.22.-) (AUT-like 3 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 3) (Autophagin-3) (Autophagy-related protein 4 homolog C) Was reported that this protein is required for a proper autophagic response under stressful conditions such as prolonged starvation, based on experiments conducted on cells or mice claimed to have null alleles (PubMed:17442669). However, this paper has been retracted because of aberrations in the relevant figure (PubMed:30808006). Nevertheless, a separate experiment in the same paper suggests that the alleles are null and so the inferred function may be true. {ECO:0000269|PubMed:17442669, ECO:0000269|PubMed:30808006, ECO:0000305}. retracted-reference Q8VBU8 Banp Mus musculus (Mouse) 10090 Protein BANP (Btg3-associated nuclear protein) (Scaffold/matrix-associated region-1-binding protein) Interaction with TP35 was reported to promote TP53 'Ser-15' phosphorylation and nuclear accumulation causing cell cycle arrest and inhibition of tumor growth (PubMed:15701641). However, the publication has been retracted due to image duplication and manipulation. Interaction with TP35 has been confirmed by other studies (PubMed:12494467). The nuclear localization has been confirmed by other studies (PubMed:10940556, PubMed:12494467, PubMed:15371550, PubMed:16166625). {ECO:0000269|PubMed:10940556, ECO:0000269|PubMed:12494467, ECO:0000269|PubMed:15371550, ECO:0000269|PubMed:15701641, ECO:0000269|PubMed:16166625, ECO:0000305|PubMed:32144153}. retracted-reference Q9DCA7 Caly Mus musculus (Mouse) 10090 Neuron-specific vesicular protein calcyon The human ortholog was originally thought to interact with the D1 dopamine receptor (DRD1) and to play a role in potentiating calcium ion-dependent signaling but this work was later retracted. {ECO:0000305}. retracted-reference Q9JJA7 Ccnl2 Mus musculus (Mouse) 10090 Cyclin-L2 (Cyclin Ania-6b) (Paneth cell-enhanced expression protein) (PCEE) The article reporting the nucleotide sequence of isoform 1 with PMID:14684736 was retracted due to suspected data duplication; the nucleotide sequence of the protein remains unchanged. {ECO:0000305|PubMed:14684736, ECO:0000305|PubMed:34237909}. retracted-reference Q9Z0H4 Celf2 Mus musculus (Mouse) 10090 CUGBP Elav-like family member 2 (CELF-2) (Bruno-like protein 3) (CUG triplet repeat RNA-binding protein 2) (CUG-BP2) (CUG-BP- and ETR-3-like factor 2) (ELAV-type RNA-binding protein 3) (ETR-3) (mETR-3) (Neuroblastoma apoptosis-related RNA-binding protein) (mNapor) (RNA-binding protein BRUNOL-3) Was reported to modulate the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression, but the article was retracted due to suspected data duplication. {ECO:0000305|PubMed:15358864, ECO:0000305|PubMed:41223228}. retracted-reference A2AVQ5 Cimap2 Mus musculus (Mouse) 10090 Ciliary microtubule-associated protein 2 (Lymphocyte expansion molecule) Was reported to promote CD8+ T cell immunity through effects on mitochondrial respiration (PubMed:25883318). However, the corresponding article has been retracted (PubMed:27980177). retracted-reference P12960 Cntn1 Mus musculus (Mouse) 10090 Contactin-1 (Neural cell surface protein F3) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q99N11 Dusp22 Mus musculus (Mouse) 10090 Dual specificity protein phosphatase 22 (EC 3.1.3.16) (EC 3.1.3.48) (JNK pathway associated phosphatase) (JKAP) (Low molecular weight dual specificity phosphatase 2) (LMW-DSP2) The publication has been retracted as they duplicated images. {ECO:0000305|PubMed:11346645, ECO:0000305|PubMed:23997090}. retracted-reference Q5DW34 Ehmt1 Mus musculus (Mouse) 10090 Histone-lysine N-methyltransferase EHMT1 (EC 2.1.1.-) (EC 2.1.1.367) (Euchromatic histone-lysine N-methyltransferase 1) (Eu-HMTase1) (G9a-like protein 1) (GLP) (GLP1) (Lysine N-methyltransferase 1D) Thought to interact with MSX1. However the paper has been retracted over concerns of image tampering. {ECO:0000305|PubMed:37405986}. retracted-reference Q9Z148 Ehmt2 Mus musculus (Mouse) 10090 Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (EC 2.1.1.367) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Protein G9a) Thought to interact with MSX1. However the paper has been retracted over concerns of image tampering. {ECO:0000305|PubMed:37405986}.; retracted-reference Q9Z2R9 Eif2ak1 Mus musculus (Mouse) 10090 Eukaryotic translation initiation factor 2-alpha kinase 1 (EC 2.7.11.1) (Heme-controlled repressor) (HCR) (Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase) (Heme-regulated inhibitor) (Hemin-sensitive initiation factor 2-alpha kinase) Was reported, in hepatocytes, to be involved in heme-mediated translational control of CYP2B and CYP3A and possibly other hepatic P450 cytochromes. Was reported that it may also regulate endoplasmic reticulum (ER) stress during acute heme-deficient conditions. However, this paper has been retracted because of improper data manipulation, reuse, and analyses. {ECO:0000305|PubMed:20071449, ECO:0000305|PubMed:34404736}. retracted-reference Q05BC3 Eml1 Mus musculus (Mouse) 10090 Echinoderm microtubule-associated protein-like 1 (EMAP-1) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q99LC5 Etfa Mus musculus (Mouse) 10090 Electron transfer flavoprotein subunit alpha, mitochondrial (Alpha-ETF) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q9D968 Hcfc2 Mus musculus (Mouse) 10090 Host cell factor 2 (HCF-2) (C2 factor) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference P70288 Hdac2 Mus musculus (Mouse) 10090 Histone deacetylase 2 (HD2) (EC 3.5.1.98) (Protein deacylase HDAC2) (EC 3.5.1.-) (YY1 transcription factor-binding protein) Was originally thought to be S-nitrosylated and to interact with MTA1 (PubMed:20519513). However, this work was later retracted (PubMed:28314777). Nevertheless, other publications demonstrate that it is S-nitrosylated and there are several publications in the human ortholog demonstrating its interaction with MTA1 (PubMed:18754010, PubMed:20972425). {ECO:0000269|PubMed:18754010, ECO:0000269|PubMed:20519513, ECO:0000269|PubMed:20972425, ECO:0000305|PubMed:28314777}. retracted-reference P63158 Hmgb1 Mus musculus (Mouse) 10090 High mobility group protein B1 (High mobility group protein 1) (HMG-1) Was reported that reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities. Was reported to be secreted. However, this work was later retracted, although the roles of different redox forms in some functional activities is supported by similarity. {ECO:0000305|PubMed:22105604, ECO:0000305|PubMed:33380312}. retracted-reference P61979 Hnrnpk Mus musculus (Mouse) 10090 Heterogeneous nuclear ribonucleoprotein K (hnRNP K) Was originally reported to be induced by DNA damage. However, the corresponding article has been retracted. {ECO:0000305|PubMed:16360036, ECO:0000305|PubMed:39389056}. retracted-reference Q5ND04 Hsf5 Mus musculus (Mouse) 10090 Heat shock factor protein 5 (HSF 5) (Heat shock transcription factor 5) (HSTF 5) (Protein expressed in male leptotene and zygotene spermatocytes 220) (MLZ-220) Was previously reported to play a role in male germline meiotic sex chromosome remodeling and silencing through regulation of SMARCA4. However, this work was later retracted. {ECO:0000305|PubMed:37206036, ECO:0000305|PubMed:40535264}. retracted-reference Q60819 Il15ra Mus musculus (Mouse) 10090 Interleukin-15 receptor subunit alpha (IL-15 receptor subunit alpha) (IL-15R-alpha) (IL-15RA) (CD antigen CD215) [Cleaved into: Soluble interleukin-15 receptor subunit alpha (sIL-15 receptor subunit alpha) (sIL-15R-alpha) (sIL-15RA)] It was shown that proteolytic cleavage of Il15ra involves ADAM17/TACE; this publication has later been retracted. {ECO:0000269|PubMed:15215246, ECO:0000305|PubMed:21516612}. retracted-reference Q7TNC9 Inpp5a Mus musculus (Mouse) 10090 Inositol polyphosphate-5-phosphatase A (EC 3.1.3.56) (Type I inositol 1,4,5-trisphosphate 5-phosphatase) (5PTase) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q9CQ82 Itgb3bp Mus musculus (Mouse) 10090 Centromere protein R (CENP-R) (Nuclear receptor-interacting factor 3) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q3U3R4 Lmf1 Mus musculus (Mouse) 10090 Lipase maturation factor 1 (Transmembrane protein 112) Additional evidence for its localization to the endoplasmic reticulum membrane was found. However this paper was retracted due to manipulation of data. {ECO:0000305|PubMed:19783858, ECO:0000305|PubMed:31399538}. retracted-reference P13297 Msx1 Mus musculus (Mouse) 10090 Homeobox protein MSX-1 (Homeobox protein Hox-7) (Hox-7.1) (Msh homeobox 1-like protein) Thought to negatively regulate transcription and thereby play a role in myoblast differentiation, also though to interact with EHMT1 and EHMT2. However the paper has been retracted over concerns of image tampering. {ECO:0000305|PubMed:37405986}.; retracted-reference Q8K4B0 Mta1 Mus musculus (Mouse) 10090 Metastasis-associated protein MTA1 Was originally thought to play a role in inflammatory responses both as a target and as a component of the NF-kappa-B signaling, to interact with the HDAC2, and be induced by lipopolysaccharide (LPS) (PubMed:20519513). However, this work was later retracted (PubMed:28314777). Nevertheless, the interaction with HDAC2 has been demonstrated by several publications in the human ortholog. {ECO:0000269|PubMed:20519513, ECO:0000305|PubMed:28314777}. retracted-reference Q9CPT4 Mydgf Mus musculus (Mouse) 10090 Myeloid-derived growth factor (MYDGF) Was originally thought to signal lymphoid cells to proliferate via thymic shared antigen 1 (PubMed:11714798). This work was later retracted (PubMed:12538725). {ECO:0000305|PubMed:11714798, ECO:0000305|PubMed:12538725}.; retracted-reference Q3UYV9 Ncbp1 Mus musculus (Mouse) 10090 Nuclear cap-binding protein subunit 1 (80 kDa nuclear cap-binding protein) (CBP80) (NCBP 80 kDa subunit) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q6IRT3 Parpbp Mus musculus (Mouse) 10090 PCNA-interacting partner (PARI) (PARP-1 binding protein) (PARP1-binding protein) (PARPBP) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q78Y63 Pdcl2 Mus musculus (Mouse) 10090 Phosducin-like protein 2 (MgcPhLP) (Phosducin-like protein similar 1) Reported to be expressed in male and female germ cells, to be up-regulated at the protein level as early as 3 hours after chorionic gonadotropin treatment in the ovary, and to interact with 14-3-3 proteins (PubMed:12424248). However, the publication has been retracted due to image duplication and manipulation. The nucleotide sequence has been confirmed by other studies (PubMed:11116088). {ECO:0000269|PubMed:11116088, ECO:0000269|PubMed:12424248, ECO:0000305|PubMed:31519761}. retracted-reference Q3TB82 Plekhf1 Mus musculus (Mouse) 10090 Pleckstrin homology domain-containing family F member 1 (PH domain-containing family F member 1) (Lysosome-associated apoptosis-inducing protein containing PH and FYVE domains) Was originally reported to be widely expressed in the nucleus, perinuclear region and lysosome. However, the corresponding article has been retracted. {ECO:0000305|PubMed:16188880, ECO:0000305|PubMed:34237888}. retracted-reference Q06180 Ptpn2 Mus musculus (Mouse) 10090 Tyrosine-protein phosphatase non-receptor type 2 (Protein-tyrosine phosphatase PTP-2) (EC 3.1.3.48) (MPTP) Was reported to dephosphorylate STAT5A and STAT5B in the nucleus to negatively regulate prolactin-mediated signaling pathway (PubMed:11773439). However, the corresponding article has been retracted (PubMed:24319783). {ECO:0000269|PubMed:11773439, ECO:0000303|PubMed:24319783}. retracted-reference Q9Z1S3 Rasgrp1 Mus musculus (Mouse) 10090 RAS guanyl-releasing protein 1 (Calcium and DAG-regulated guanine nucleotide exchange factor II) (CalDAG-GEFII) (Ras guanyl-releasing protein) Was reported that thymocytes isolated from a RasGRP1 mutant mouse strain show a defect in Ras activation following T-cell-receptor (TCR) engagement (PubMed:12932358). However, this paper has been retracted because the data in one figure was falsified by one of the authors (PubMed:22808526). The authors stand by the validity of the other figures, results and interpretation in this paper (PubMed:22808526). Furthermore, evidence supporting function is derived by similarity with the human ortholog, so may be true. {ECO:0000269|PubMed:12932358, ECO:0000269|PubMed:22808526, ECO:0000305}. retracted-reference Q80YR6 Rbbp8 Mus musculus (Mouse) 10090 DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2) Upon DNA damage, was shown to interact with SIRT6 resulting in its deacetylation. However, this study was later retracted. {ECO:0000305|PubMed:20829486, ECO:0000305|PubMed:30975768}. retracted-reference P08207 S100a10 Mus musculus (Mouse) 10090 Protein S100-A10 (Calpactin I light chain) (Calpactin-1 light chain) (Cellular ligand of annexin II) (S100 calcium-binding protein A10) (p10 protein) (p11) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference O88974 Setdb1 Mus musculus (Mouse) 10090 Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.366) (ERG-associated protein with SET domain) (ESET) (SET domain bifurcated 1) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q8K4L3 Svil Mus musculus (Mouse) 10090 Supervillin (Archvillin) (p205/p250) Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q69ZR9 Tasor Mus musculus (Mouse) 10090 Protein TASOR (Transgene activation suppressor protein) Was previously reported to coordinate an interaction network required for early embryonic development and cell division. However, the paper was later retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q9CQG9 Tmem100 Mus musculus (Mouse) 10090 Transmembrane protein 100 Was previously reported to interact with TASOR. However, the paper was subsequently retracted. {ECO:0000305|PubMed:31112734, ECO:0000305|PubMed:34272044}. retracted-reference Q9EPU5 Tnfrsf21 Mus musculus (Mouse) 10090 Tumor necrosis factor receptor superfamily member 21 (Death receptor 6) (CD antigen CD358) Was reported to play a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and to be required for both normal cell body death and axonal pruning. Was also reported to bind N-APP triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) (PubMed:19225519). This work was later retracted (PubMed:38110576). {ECO:0000305|PubMed:19225519, ECO:0000305|PubMed:38110576}.; retracted-reference O08747 Unc5c Mus musculus (Mouse) 10090 Netrin receptor UNC5C (Protein unc-5 homolog 3) (Protein unc-5 homolog C) (Rostral cerebellar malformation protein) The article has been retracted because some of the Western blot images in the article were erroneneous. {ECO:0000269|PubMed:10399920, ECO:0000269|PubMed:37669666}. retracted-reference Q8CF60 Znf263 Mus musculus (Mouse) 10090 Zinc finger protein 263 (Zinc finger protein FPM315) (Zinc finger protein with KRAB and SCAN domains 12) An isoform of Znf263 lacking residues 1-288 was described, however this paper was retracted due to concerns about the validity of figures published in the paper. {ECO:0000305|PubMed:12024037, ECO:0000305|PubMed:19474393}. retracted-reference P9WJB5 fhaB Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 FHA domain-containing protein FhaB (FtsZ-interacting protein A) The article by Sureka et al was retracted by the editors after publication. Concerns were raised regarding the results presented in multiple figure panels. The raw data or replacement panels that were available did not satisfactorily address all the issues, thus questioning the integrity of the data. {ECO:0000305|PubMed:35202441}. retracted-reference P9WNA1 ftsQ Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Cell division protein FtsQ The article by Sureka et al was retracted by the editors after publication. Concerns were raised regarding the results presented in multiple figure panels. The raw data or replacement panels that were available did not satisfactorily address all the issues, thus questioning the integrity of the data. {ECO:0000305|PubMed:35202441}. retracted-reference P9WN95 ftsZ Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Cell division protein FtsZ The article by Sureka et al was retracted by the editors after publication. Concerns were raised regarding the results presented in multiple figure panels. The raw data or replacement panels that were available did not satisfactorily address all the issues, thus questioning the integrity of the data. {ECO:0000305|PubMed:35202441}. retracted-reference P9WKD1 pbpA Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Peptidoglycan D,D-transpeptidase PbpA (EC 3.4.16.4) (Penicillin-binding protein A) (PBPA) An article reported the phosphorylation of PbpA by PknB, but this paper was later retracted as some figures were modified prior to publication. {ECO:0000305|PubMed:16436437, ECO:0000305|PubMed:26231854}. retracted-reference P9WI83 pknA Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Serine/threonine-protein kinase PknA (EC 2.7.11.1) The article by Sureka et al was retracted by the editors after publication. Concerns were raised regarding the results presented in multiple figure panels. The raw data or replacement panels that were available did not satisfactorily address all the issues, thus questioning the integrity of the data. {ECO:0000305|PubMed:35202441}. retracted-reference P9WI81 pknB Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 83332 Serine/threonine-protein kinase PknB (EC 2.7.11.1) An article reported the role of PknB in phosphorylation of PbpA, but this paper was later retracted as some figures were modified prior to publication. {ECO:0000305|PubMed:16436437, ECO:0000305|PubMed:26231854}. retracted-reference A0QNG6 fhaB Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) 246196 FHA domain-containing protein FhaB (FtsZ-interacting protein A) The article by Sureka et al was retracted by the editors after publication. Concerns were raised regarding the results presented in multiple figure panels. The raw data or replacement panels that were available did not satisfactorily address all the issues, thus questioning the integrity of the data. {ECO:0000305|PubMed:35202441}. retracted-reference Q6JE38 CITRX1 Nicotiana benthamiana 4100 Thioredoxin-like protein CITRX1, chloroplastic (EC 1.8.-.-) (Cf-9-interacting thioredoxin 1) (NbCiTrx1) The article has been retracted, because it has become clear that the thioredoxin that interacts in yeast 2-hybrid with the Cf-9 C-terminus is in fact localized in the chloroplast, rendering a role in Cf-9 signaling unlikely. All the authors agree that this paper should be withdrawn from the scientific literature. {ECO:0000305|PubMed:31310343}. retracted-reference Q6JE37 CITRX2 Nicotiana benthamiana 4100 Thioredoxin-like protein CITRX2, chloroplastic (EC 1.8.-.-) (Cf-9-interacting thioredoxin 2) (NbCiTrx2) The article has been retracted, because it has become clear that the thioredoxin that interacts in yeast 2-hybrid with the Cf-9 C-terminus is in fact localized in the chloroplast, rendering a role in Cf-9 signaling unlikely. All the authors agree that this paper should be withdrawn from the scientific literature. {ECO:0000305|PubMed:31310343}. retracted-reference P0C518 ATP9 Oryza sativa subsp. indica (Rice) 39946 ATP synthase subunit 9, mitochondrial (Lipid-binding protein) The species of origin is incorrect in one of the citations where it was originally thought to be rice (PubMed:2143016). However, the sequence from that paper was later shown to originate from Petunia and the paper was retracted (PubMed:2235528). {ECO:0000305|PubMed:2143016, ECO:0000305|PubMed:2235528}. retracted-reference Q84688 Peanut clump virus (isolate 87/TGTA2) (PCV) 652837 Suppressor of RNA silencing (15kD cysteine rich protein) (P15) The publication has been retracted because some figures presented signs of inappropriate manipulation. {ECO:0000305|PubMed:32202019}. retracted-reference Q9HWA4 pprB Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) 208964 Two-component response regulator PprB An article reported the role of PprB in modulation of the quorum-sensing signal production. However, this paper was later retracted as the authors' main conclusion on the regulatory role of PprB on AHL signal production in wild type P.aeruginosa is not correct. {ECO:0000305|PubMed:15882421, ECO:0000305|PubMed:18684246}. retracted-reference Q400C7 Amz2 Rattus norvegicus (Rat) 10116 Archaemetzincin-2 (EC 3.4.-.-) (Archeobacterial metalloproteinase-like protein 2) The protein has been described as presenting a second isoform with a missign Lys in position 309 (PubMed:15972818). However, the paper has been retracted. {ECO:0000269|PubMed:15972818, ECO:0000305|PubMed:30808005}. retracted-reference P58821 Caly Rattus norvegicus (Rat) 10116 Neuron-specific vesicular protein calcyon The human ortholog was originally thought to interact with the D1 dopamine receptor (DRD1) and to play a role in potentiating calcium ion-dependent signaling but this work was later retracted. {ECO:0000305}. retracted-reference B1H283 Cimap2 Rattus norvegicus (Rat) 10116 Ciliary microtubule-associated protein 2 (Lymphocyte expansion molecule) Was reported to promote CD8+ T cell immunity through effects on mitochondrial respiration. However, the corresponding article has been retracted. {ECO:0000250|UniProtKB:A2AVQ5}. retracted-reference Q63155 Dcc Rattus norvegicus (Rat) 10116 Netrin receptor DCC (Tumor suppressor protein DCC) The article has been retracted because some of the Western blot images in the article were erroneneous. {ECO:0000269|PubMed:10399920, ECO:0000269|PubMed:37669666}. retracted-reference Q63185 Eif2ak1 Rattus norvegicus (Rat) 10116 Eukaryotic translation initiation factor 2-alpha kinase 1 (EC 2.7.11.1) (Heme-controlled repressor) (HCR) (Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase) (Heme-regulated inhibitor) (Hemin-sensitive initiation factor 2-alpha kinase) Was reported to be induced by various cytochrome P450 inducers, including phenobarbital, dexamethasone, rifampicin and barbituric acid in its autophosphorylated state, and that carbamazepine has no effect. Was also reported to be expressed predominantly in erythroid cells, and at much lower levels, expressed in hepatocytes (at protein level). However, this paper has been retracted because of improper data manipulation, reuse, and analyses. {ECO:0000305|PubMed:20071449, ECO:0000305|PubMed:34404736}. retracted-reference Q4QQV3 Fam162a Rattus norvegicus (Rat) 10116 Protein FAM162A (E2-induced gene 5 protein homolog) A paper showing a role in apoptosis in neurons has been retracted due to panel duplication in several figures. {ECO:0000269|PubMed:19520982, ECO:0000305|PubMed:32272861}. retracted-reference P63159 Hmgb1 Rattus norvegicus (Rat) 10116 High mobility group protein B1 (Amphoterin) (Heparin-binding protein p30) (High mobility group protein 1) (HMG-1) Was reported that reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities. However, this work was later retracted, although the roles of different redox forms in some functional activities is supported by other papers. {ECO:0000305|PubMed:22105604, ECO:0000305|PubMed:33380312}. retracted-reference P21708 Mapk3 Rattus norvegicus (Rat) 10116 Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (MNK1) (Microtubule-associated protein 2 kinase) (p44-ERK1) The publication has been retracted as they falsified western blot data. {ECO:0000305|PubMed:10748187, ECO:0000305|PubMed:28550140}. retracted-reference Q62812 Myh9 Rattus norvegicus (Rat) 10116 Myosin-9 (Cellular myosin heavy chain, type A) (Myosin heavy chain 9) (Myosin heavy chain, non-muscle IIa) (Non-muscle myosin heavy chain A) (NMMHC-A) (Non-muscle myosin heavy chain IIa) (NMMHC II-a) (NMMHC-IIA) Reported to interact with SLC6A4 in its sialylated form. However, this publication was retracted due to image duplication in the figures. {ECO:0000305|PubMed:12944413, ECO:0000305|PubMed:31201245}. retracted-reference P31652 Slc6a4 Rattus norvegicus (Rat) 10116 Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4) Reported to be glycosylated with sialylated N-glycans and in its sialylated form to interact with MYH9 (PubMed:12944413). However, this publication was retracted due to image duplication in the figures. {ECO:0000269|PubMed:12944413, ECO:0000305|PubMed:31201245}. retracted-reference O08721 Unc5a Rattus norvegicus (Rat) 10116 Netrin receptor UNC5A (Protein unc-5 homolog 1) (Protein unc-5 homolog A) The article has been retracted because some of the Western blot images in the article were erroneneous. {ECO:0000269|PubMed:10399920, ECO:0000269|PubMed:37669666}. retracted-reference P38998 LYS1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Saccharopine dehydrogenase [NAD(+), L-lysine-forming] (SDH) (EC 1.5.1.7) (Lysine--2-oxoglutarate reductase) PubMed:10077615 shows data confirming the peroxisomal localization of the protein, however this study was later retracted as the images were additionally used in other articles for other proteins. {ECO:0000305|PubMed:15696628}. retracted-reference Q08601 MCA1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 559292 Metacaspase-1 (EC 3.4.22.-) [Cleaved into: Large subunit p20; Small subunit p10] PubMed:19174511 reported that MCA1 may have a prion form, dubbed [MCA]. However, the same authors have later not been able to reproduce these results and retracted the paper. {ECO:0000305}. retracted-reference Q9UT23 fml1 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 284812 ATP-dependent DNA helicase fml1 (EC 5.6.2.4) (DNA 3'-5' helicase fml1) (FANCM-like protein 1) Several phenotypes were reported for a triple-alanine mutant. However this data was retracted as several constructs contained a C-terminal deletion instead of the reported triple-alanine mutation. Following strain regeneration, although many phenotypes were not reproducible, the central observations of the publication were confirmed. {ECO:0000305|PubMed:24026537, ECO:0000305|PubMed:29445032}. retracted-reference G4TS85 Serendipita indica (strain DSM 11827) (Root endophyte fungus) (Piriformospora indica) 1109443 Inorganic phosphate transporter PHO84 (PiPT) Reported to contribute to the symbiotic relationship between the fungus and host plant; expressed in external hyphae and functions as a high affinity phosphate transporter that supplies phosphate to the host roots (PubMed:20479005). However, the publication has been retracted due to image duplication (PubMed:20479005). The nucleotide sequence and function reported in the retracted paper have been confirmed by other studies (PubMed:21502815, PubMed:22022265, PubMed:34135124, PubMed:39089400). {ECO:0000269|PubMed:20479005, ECO:0000269|PubMed:21502815, ECO:0000269|PubMed:22022265, ECO:0000269|PubMed:34135124, ECO:0000269|PubMed:39089400, ECO:0000305|PubMed:34237905}. retracted-reference Q9LKW0 CITRX Solanum lycopersicum (Tomato) (Lycopersicon esculentum) 4081 Thioredoxin-like protein CITRX, chloroplastic (EC 1.8.-.-) (Cf-9-interacting thioredoxin) (LeCiTrx) The article has been retracted, because it has become clear that the thioredoxin that interacts in yeast 2-hybrid with the Cf-9 C-terminus is in fact localized in the chloroplast, rendering a role in Cf-9 signaling unlikely. All the authors agree that this paper should be withdrawn from the scientific literature. {ECO:0000305|PubMed:31310343}. retracted-reference Q40235 CF-9 Solanum pimpinellifolium (Currant tomato) (Lycopersicon pimpinellifolium) 4084 Receptor-like protein Cf-9 The article has been retracted, because it has become clear that the thioredoxin that interacts in yeast 2-hybrid with the Cf-9 C-terminus is in fact localized in the chloroplast, rendering a role in Cf-9 signaling unlikely. All the authors agree that this paper should be withdrawn from the scientific literature. {ECO:0000305|PubMed:31310343}. retracted-reference M1A3D5 CITRX Solanum tuberosum (Potato) 4113 Thioredoxin-like protein CITRX, chloroplastic (EC 1.8.-.-) (Cf-9-interacting thioredoxin) (StCiTrx) The article has been retracted, because it has become clear that the thioredoxin that interacts in yeast 2-hybrid with the Cf-9 C-terminus is in fact localized in the chloroplast, rendering a role in Cf-9 signaling unlikely. All the authors agree that this paper should be withdrawn from the scientific literature. {ECO:0000305|PubMed:31310343}. retracted-reference Q99R54 Staphylococcus aureus (strain Mu50 / ATCC 700699) 158878 Putative flavoprotein monooxygenase (EC 1.-.-.-) (Baeyer-Villiger flavin-containing monooxygenase) (BVFMO) (Baeyer-Villiger monooxygenase) (BVMO) (Flavin-containing monooxygenase) (FMO) (SAFMO) The crystal structure article has been retracted because submission was made without agreement from the last author. The protein was predicted in that paper to be a Baeyer-Villiger monooxygenase, but such activity was never experimentally shown. However, the protein binds to FAD in the crystal structure, and is probably an oxidoreductase. {ECO:0000305|PubMed:30338968}. retracted-reference Q5SLC9 pilB Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) 300852 Type IV pilus assembly ATPase PilB The article by Sukmana et al was retracted. Concerns were raised regarding the results presented in figure 7. An investigation revealed discrepancies in the underlying data, making the results in this figure irreproducible. {ECO:0000305|PubMed:40219993}. retracted-reference P09504 Turnip yellows virus (isolate FL-1) (TuYV) (BWYV-FL1) 12043 Suppressor of silencing P0 (29 kDa protein) (Protein ORF0) The publication has been retracted because some figures presented signs of inappropriate manipulation. {ECO:0000305|PubMed:29611664}. retracted-reference P0C0F7 rpfC Xanthomonas campestris pv. campestris (strain 8004) 314565 Sensory/regulatory protein RpfC (EC 2.7.13.3) The article describing the function has been retracted due to duplications and irregularities in some figures, but repeated experiments using the original strains support the findings. {ECO:0000305|PubMed:16611728, ECO:0000305|PubMed:28784774}. retracted-reference Q4UU85 rpfG Xanthomonas campestris pv. campestris (strain 8004) 314565 Cyclic di-GMP phosphodiesterase response regulator RpfG (EC 3.1.4.-) The article describing the function and the phosphodiesterase activity has been retracted due to duplications and irregularities in some figures, but repeated experiments using the original strains support the findings. {ECO:0000305|PubMed:16611728, ECO:0000305|PubMed:28784774}. retracted-reference P06677 Zea mays (Maize) 4577 Zein-alpha 19C2 (19 kDa alpha-zein 19C2) Was originally thought to interact with OP10 (via N-terminus) (PMID:27541862). However, the corresponding article has been retracted (PMID:36383521). {ECO:0000269|PubMed:27541862, ECO:0000269|PubMed:36383521}. retracted-reference P08031 Zea mays (Maize) 4577 16 kDa gamma-zein (16 kDa zein) (Zein Zc1) (Zein-2) (Zein-gamma) Was originally thought to interact with OP10 (via N-terminus) (PMID:27541862). However, the corresponding article has been retracted (PMID:36383521). {ECO:0000269|PubMed:27541862, ECO:0000269|PubMed:36383521}. retracted-reference C0P381 Zea mays (Maize) 4577 50 kDa gamma-zein Was originally thought to interact with OP10 (via N-terminus) (PMID:27541862). However, the corresponding article has been retracted (PMID:36383521). {ECO:0000269|PubMed:27541862, ECO:0000269|PubMed:36383521}. retracted-reference O48966 AZS22-4 Zea mays (Maize) 4577 22 kDa alpha-zein 4 (22 kDa alpha-zein PZ22.3) (22kD alpha-zein 3) (Zein-alpha PZ22.3) Was originally thought to interact with OP10 (via N-terminus) (PMID:27541862). However, the corresponding article has been retracted (PMID:36383521). {ECO:0000269|PubMed:27541862, ECO:0000269|PubMed:36383521}. retracted-reference A8DMN5 FL1 Zea mays (Maize) 4577 Protein FLOURY 1 Was originally thought to interact (via C-terminus) with OP10 (via N-terminus) (PMID:27541862). However, the corresponding article has been retracted (PMID:36383521). {ECO:0000269|PubMed:27541862, ECO:0000269|PubMed:36383521}. retracted-reference K7TQE3 HIP Zea mays (Maize) 4577 HSP-interacting protein Was originally thought to interact (via C-terminus) with OP10 (via N-terminus) (PMID:27541862). However, the corresponding article has been retracted (PMID:36383521). {ECO:0000269|PubMed:27541862, ECO:0000269|PubMed:36383521}. retracted-reference P0DKL2 O10 Zea mays (Maize) 4577 Protein OPAQUE10 Was originally thought to be required for distribution of gamma-zeins; to form homodimers; to interact with some zeins; to localize to the endoplasmic reticulum membrane; to be expressed in kernels continuously during kernel development and the seven repeat domain is thought to be responsible for dimerization (PMID:27541862). However, the corresponding article has been retracted (PMID:36383521). {ECO:0000269|PubMed:27541862, ECO:0000269|PubMed:36383521}.