# Snapshot of the UniProtKB records used by the alternative_records block of # GPD-ai-review.yaml. Retrieved from the UniProt REST API; not generated by the # uniprot-orphan-analysis exporter. accession: A0A2U9RB90 retrieved_at: '2026-10-28T00:33:57+00:00' source_url: https://rest.uniprot.org/uniprotkb/A0A2U9RB90.txt current_record_status: Current UniProtKB/TrEMBL entry proteome_search: description: >- UniProtKB REST search for every EC 1.1.1.8 entry of Pichia kudriavzevii (NCBITaxon:4909), returning exactly two records. source_url: 'https://rest.uniprot.org/uniprotkb/search?query=organism_id:4909+AND+ec:1.1.1.8&fields=accession,id,protein_name,gene_names,xref_proteomes,length&format=tsv' retrieved_at: '2026-10-28T00:33:57+00:00' result_text: | Entry Entry Name Protein names Gene Names Proteomes Length A0A2U9RB90 A0A2U9RB90_PICKU Glycerol-3-phosphate dehydrogenase [NAD(+)] (EC 1.1.1.8) C5L36_0E02100 UP000249293: Chromosome 5 415 A8W1U0 A8W1U0_PICKU Glycerol-3-phosphate dehydrogenase [NAD(+)] (EC 1.1.1.8) GPD 388 unisave_records: - entry_version: 26 sequence_version: 1 record_text: | ID A0A2U9RB90_PICKU Unreviewed; 415 AA. AC A0A2U9RB90; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 28-JAN-2026, entry version 26. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=C5L36_0E02100 {ECO:0000313|EMBL:AWU78148.1}; OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes; OC Pichiales; Pichiaceae; Pichia. OX NCBI_TaxID=4909 {ECO:0000313|EMBL:AWU78148.1, ECO:0000313|Proteomes:UP000249293}; RN [1] {ECO:0000313|EMBL:AWU78148.1, ECO:0000313|Proteomes:UP000249293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS573 {ECO:0000313|EMBL:AWU78148.1, RC ECO:0000313|Proteomes:UP000249293}; RA Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A., RA Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.; RT "Population genomics shows no distinction between pathogenic Candida krusei RT and environmental Pichia kudriavzevii: One species, four names."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=sn-glycerol 3-phosphate + NAD(+) = dihydroxyacetone phosphate CC + NADH + H(+); Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, CC ChEBI:CHEBI:57945; EC=1.1.1.8; CC Evidence={ECO:0000256|ARBA:ARBA00048683, CC ECO:0000256|RuleBase:RU361243}; CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009, CC ECO:0000256|RuleBase:RU000437}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP028777; AWU78148.1; -; Genomic_DNA. DR RefSeq; XP_029323624.1; XM_029467764.1. DR AlphaFoldDB; A0A2U9RB90; -. DR STRING; 4909.A0A2U9RB90; -. DR GeneID; 40386007; -. DR KEGG; pkz:C5L36_0E02100; -. DR VEuPathDB; FungiDB:C5L36_0E02100; -. DR OrthoDB; 10263760at2759; -. DR Proteomes; UP000249293; Chromosome 5. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0141152; F:glycerol-3-phosphate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:UniProtKB-UniRule. DR FunFam; 1.10.1040.10:FF:000004; Glycerol-3-phosphate dehydrogenase [NAD(+)]; 1. DR FunFam; 3.40.50.720:FF:000294; Glycerol-3-phosphate dehydrogenase [NAD(+)]; 1. DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR006168; G3P_DH_NAD-dep. DR InterPro; IPR006109; G3P_DH_NAD-dep_C. DR InterPro; IPR017751; G3P_DH_NAD-dep_euk. DR InterPro; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR03376; glycerol3P_DH; 1. DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11728:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 1. DR Pfam; PF07479; NAD_Gly3P_dh_C; 1. DR Pfam; PF01210; NAD_Gly3P_dh_N; 1. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000114-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000437}; KW Reference proteome {ECO:0000313|Proteomes:UP000249293}. FT DOMAIN 63..228 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 261..406 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 272 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 68..73 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 156 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 179 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 212 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 337..338 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 337 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 366 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 415 AA; 45822 MW; CEE80564DA1066F7 CRC64; MFLISKSLHF TRSFSNTIKT LNRSNIKMVS PAERLSTIAS TIKPNRKDST SLQPEDYPEH PFKVTVVGSG NWGCTIAKVI AENTVERPRQ FQRDVNMWVY EELIEGEKLT EIINTKHENV KYLPGIKLPV NVVAVPDIVE ACAGSDLIVF NIPHQFLPRI LSQLKGKVNP KARAISCLKG LDVNPNGCKL LSTVITEELG IYCGALSGAN LAPEVAQCKW SETTVAYTIP DDFRGKGKDI DHQILKSLFH RPYFHVRVIS DVAGISIAGA LKNVVAMAAG FVEGLGWGDN AKAAVMRIGL VETIQFAKTF FDGCHAATFT HESAGVADLI TTCAGGRNVR VGRYMAQHSV SATEAEEKLL NGQSCQGIHT TREVYEFLSN MGRTDEFPLF TTTYRIIYEN FPIEKLPECL EPVED //