ID G3P_PSEVU Reviewed; 294 AA. AC P24751; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 18-JUN-2025, entry version 116. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P0A9B2}; DE Short=GAPDH {ECO:0000250|UniProtKB:P0A9B2}; DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P0A9B2}; DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P0A9B2}; DE Flags: Fragment; GN Name=gap; OS Pseudescherichia vulneris (Escherichia vulneris). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Pseudescherichia. OX NCBI_TaxID=566; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29943 / CDC 2898-73; RX PubMed=1955870; DOI=10.1099/00221287-137-8-1911; RA Lawrence J.G., Ochman H., Hartl D.L.; RT "Molecular and evolutionary relationships among enteric bacteria."; RL J. Gen. Microbiol. 137:1911-1921(1991). CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3- CC phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor CC NAD. The first reaction step involves the formation of a hemiacetal CC intermediate between G3P and a cysteine residue, and this hemiacetal CC intermediate is then oxidized to a thioester, with concomitant CC reduction of NAD to NADH. The reduced NADH is then exchanged with the CC second NAD, and the thioester is attacked by a nucleophilic inorganic CC phosphate to produce BPG. {ECO:0000250|UniProtKB:P0A9B2}. 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=1.2.1.12; CC Evidence={ECO:0000250|UniProtKB:P0A9B2}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A9B2}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000305}. 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; M63363; AAA23850.1; -; Genomic_DNA. DR PIR; I41221; I41221. DR AlphaFoldDB; P24751; -. DR SMR; P24751; -. DR UniPathway; UPA00109; UER00184. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS: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; IEA:InterPro. 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:000001; 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; NF011954; PRK15425.1; 1. DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 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 3: Inferred from homology; KW Acetylation; Cytoplasm; Glycolysis; NAD; Nucleotide-binding; KW Oxidoreductase. FT CHAIN <1..>294 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_0000145659" FT ACT_SITE 135 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 19 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 63 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 105 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 134..136 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 165 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 194..195 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 217 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT SITE 162 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT MOD_RES 177 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT MOD_RES 234 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT NON_TER 1 FT NON_TER 294 SQ SEQUENCE 294 AA; 31365 MW; 270A233457394730 CRC64; IVFRAAQKRS DIEIVAINDL LDAEYMAYML KYDSTHGRFD GTVEVKDGHL VVNGKKIRVT AERDPANLKW DEVGVDVVAE ATGIFLTDET ARKHITAGAK KVVLTGPSKD NTPMFVRGAN FDTYAGQDIV SNASCTTNCL APLAKVINDN FGIVEGLMTT VHATTATQKT VDGPSHKDWR GGRGAAQNII PSSTGAAKAV GKVLPELNGK LTGMAFRVPT PNVSVVDLTV RLEKAASYEE IKKAIKAASE GAMKGVLGYT EDDVVSTDFN GEVCTSVFDA KAGIALNDNF VKLV //