ID   G3P_SEROD               Reviewed;         294 AA.
AC   P24753;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 105.
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   Serratia odorifera.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=618;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 + NAD(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADH; 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}.
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DR   EMBL; M63374; AAA26555.1; -; Genomic_DNA.
DR   AlphaFoldDB; P24753; -.
DR   SMR; P24753; -.
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   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   PANTHER; PTHR10836; PTHR10836; 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; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; NAD; Nucleotide-binding; Oxidoreductase.
FT   CHAIN           <1..>294
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT                   /id="PRO_0000145681"
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   NON_TER         1
FT   NON_TER         294
SQ   SEQUENCE   294 AA;  31374 MW;  3F0F72CA5DC9C2AE CRC64;
     IVFRAAQERS DIEIVAINDL LDAEYMAYML KYDSTHGRFN GSVEVKDGHL VVNGQTIRVT
     AEKDPANLKW NEVGVDVVAE ATGIFLTDET ARKHIAAGAK KVVLTGPSKD DTPMFVMGVN
     LKSYAGQEIV SNASCTTNCL APLAKVINDK FGIVEALMTT VHATTATQKT VDGPFHKDWR
     GGRGASQNII PSSTGAAKAV GKVIPELNGK LTGMAFRVPT PNVSVVDLTA RLEKPASYKE
     VCAAIKEAAE GELKGVLGYT EDDVVSTDFN GEKLTSVFDA KAGIALNDNF VKLV