G3P_ATLHE
ID G3P_ATLHE Reviewed; 294 AA.
AC P24750;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Atlantibacter hermannii (Escherichia hermannii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Atlantibacter.
OX NCBI_TaxID=565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33650 / DSM 4560 / CCUG 15714 / JCM 1473 / NBRC 105704 / NCTC
RC 12129 / CDC 980-72, and ATCC 33652 / CDC 1479-80;
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; M63361; AAA23851.1; -; Genomic_DNA.
DR EMBL; M63362; AAA23854.1; -; Genomic_DNA.
DR PIR; I41222; I41222.
DR AlphaFoldDB; P24750; -.
DR SMR; P24750; -.
DR PRIDE; P24750; -.
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_0000145658"
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; 31394 MW; FA87ABC98E7F5FFD CRC64;
IVFRAAQTRS DIEIVAINDL LDAEYMAYML KYDSTHGRFD GTVEVKDGHL VVNGKKIRVT
AEKDPANLKW NEVGVDVVAE ATGIFLTDET ARKHITAGAK KVVLTGPSKD DTPMFVKGAN
FDKYNGQDIV SNASCTTNCL APLAKVINDN FGIIEGLMTT VHATTATQKT VDGPSHKDWR
GGRGAAQNII PSSTGAAKAV GKVLPELNGK LTGMAFRVPT PNVSVVDLTV RLEKAASYED
IKKAIKAAAE GEMKGVLGYT EDDVVSTDFN GEVCTSVFDA KAGIALNDNF VKLV
