ID   G3P2_SYNY3              Reviewed;         337 AA.
AC   P80505;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 164.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2 {ECO:0000303|PubMed:9226260};
DE            EC=1.2.1.59 {ECO:0000269|PubMed:9226260};
DE   AltName: Full=GAPDH 2 {ECO:0000303|PubMed:9226260};
DE   AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:9226260};
DE   AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:9226260};
GN   Name=gap2; OrderedLocusNames=sll1342;
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP   AND SUBSTRATE SPECIFICITY.
RC   STRAIN=strain PCC 6803 / Kazusa;
RX   PubMed=9226260; DOI=10.1128/jb.179.14.4513-4522.1997;
RA   Valverde F., Losada M., Serrano A.;
RT   "Functional complementation of an Escherichia coli gap mutant supports an
RT   amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate
RT   dehydrogenase of Synechocystis sp. strain PCC 6803.";
RL   J. Bacteriol. 179:4513-4522(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Schubert M., Brinkmann H., Cerff R.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-11.
RA   Valverde F., Serrano A.;
RL   Submitted (NOV-1995) to UniProtKB.
CC   -!- FUNCTION: Involved in photosynthetic carbon assimilation. Catalyzes the
CC       NAD(P)-dependent oxidative phosphorylation of glyceraldehyde 3-
CC       phosphate (G3P) to 1,3-bisphosphoglycerate (BPG). The first reaction
CC       step involves the formation of a hemiacetal intermediate between G3P
CC       and a cysteine residue, and this hemiacetal intermediate is then
CC       oxidized to a thioester, with concomitant reduction of NAD to NADH. The
CC       reduced NADH is then exchanged with the second NAD, and the thioester
CC       is attacked by a nucleophilic inorganic phosphate to produce BPG. It
CC       can use both NADP and NAD. {ECO:0000269|PubMed:9226260}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + phosphate + NADP(+) = (2R)-3-
CC         phospho-glyceroyl phosphate + NADPH + H(+); Xref=Rhea:RHEA:10296,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC         Evidence={ECO:0000269|PubMed:9226260};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = (2R)-3-
CC         phospho-glyceroyl phosphate + NADH + H(+); Xref=Rhea:RHEA:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC         Evidence={ECO:0000269|PubMed:9226260};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9226260}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; X83564; CAA58550.1; -; Genomic_DNA.
DR   EMBL; X86376; CAA60135.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18633.1; -; Genomic_DNA.
DR   PIR; S54141; S54141.
DR   AlphaFoldDB; P80505; -.
DR   SMR; P80505; -.
DR   FunCoup; P80505; 449.
DR   IntAct; P80505; 3.
DR   STRING; 1148.gene:10500398; -.
DR   PaxDb; 1148-gene:10500398; -.
DR   EnsemblBacteria; BAA18633; BAA18633; BAA18633.
DR   KEGG; syn:sll1342; -.
DR   eggNOG; COG0057; Bacteria.
DR   InParanoid; P80505; -.
DR   PhylomeDB; P80505; -.
DR   SABIO-RK; P80505; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; EXP:UniProtKB.
DR   GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; EXP:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd18126; GAPDH_I_C; 1.
DR   CDD; cd05214; GAPDH_I_N; 1.
DR   FunFam; 3.30.360.10:FF:000002; Glyceraldehyde-3-phosphate dehydrogenase; 1.
DR   FunFam; 3.40.50.720:FF:000001; Glyceraldehyde-3-phosphate dehydrogenase; 1.
DR   Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01534; GAPDH-I; 1.
DR   NCBIfam; NF005641; PRK07403.1; 1.
DR   PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glycolysis; NAD; NADP;
KW   Nucleotide-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CHAIN           2..337
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT                   /id="PRO_0000145709"
FT   ACT_SITE        154
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         11..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         79
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         153..155
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         184
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         199
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         212..213
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         235
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         317
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   SITE            181
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GIL8"
FT   CONFLICT        57
FT                   /note="A -> G (in Ref. 1; CAA58550)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162..163
FT                   /note="FG -> IA (in Ref. 2; CAA60135/BAA18633)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   337 AA;  36512 MW;  FC8FF0E7FEAC1585 CRC64;
     MTRVAINGFG RIGRNFLRCW LGRTDSQLEV VGINDTSDPR TNAHLLRYDS MLGKLDADIS
     ADENSITVNG KTIKCVSDRN PLNLPWAEWN VDLVIEATGV FVTHEGATKH VQAGAKKVLI
     TAPGKGPNIG TYVVGVNAHE YKHEEYEVIS NASCTTNCLA PFGKVINDNF GIIKGTMTTT
     HSYTGDQRIL DASHRDLRRA RAAAVNIVPT STGAAKAVAL VIPELQGKLN GIALRVPTPN
     VSVVDLVVQV EKNTIAEQVN GVLKEAANTS LKGVLEYTDL ELVSSDFRGT DCSSTVDGSL
     TMVMGGDMVK VIAWYDNEWG YSQRVVDLAE IVAKNWK
//