G3P_BACFR
ID G3P_BACFR Reviewed; 333 AA.
AC Q59199; Q64XQ9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
DE Short=GAPDH {ECO:0000250|UniProtKB:P00362};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P09124};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
GN Name=gap; OrderedLocusNames=BF0967;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-311.
RC STRAIN=IRL8;
RA Morin L., Muller M.;
RT "Glycolytic enzymes in Bacteroides fragilis.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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:P00362}.
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:P09124};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00362}.
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; AP006841; BAD47717.1; -; Genomic_DNA.
DR EMBL; U27541; AAA82598.1; -; Genomic_DNA.
DR RefSeq; WP_005785248.1; NZ_UYXF01000032.1.
DR RefSeq; YP_098251.1; NC_006347.1.
DR AlphaFoldDB; Q59199; -.
DR SMR; Q59199; -.
DR STRING; 295405.BF0967; -.
DR PRIDE; Q59199; -.
DR EnsemblBacteria; BAD47717; BAD47717; BF0967.
DR GeneID; 66330054; -.
DR KEGG; bfr:BF0967; -.
DR PATRIC; fig|295405.11.peg.967; -.
DR HOGENOM; CLU_030140_0_3_10; -.
DR OMA; NCVAPMA; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000002197; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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..333
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145631"
FT ACT_SITE 151
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 150..152
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 181
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 210..211
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 233
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 178
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:Q6GIL8"
FT CONFLICT 104
FT /note="D -> N (in Ref. 2; AAA82598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 35663 MW; 4565A140BFDCE266 CRC64;
MIKVGINGFG RIGRMVFRAA VKNFGNDIQI VGINDLLDAE YLAYMLKYDS VHGRFEGEVA
VEDGALIVNG NKIRLTAEMD PANLKWNEVD ADVVVESTGF FLTDETARKH IQAGAKKVIM
SAPSKDSTPM FVYGVNHTSY AGQDIISNAS CTTNCLAPIA KVLNDKFGIV KGLMTTVHAA
TATQKTVDGP SKKDWRGGRG ILENIIPSST GAAKAVGKVL PVLNGKLTGM AFRVPTSDVS
VVDLTVVLEK AATMAEINAA MKEASEGELK GILGYTEDAV VSTDFRGCAN TSIYDSKAGI
SLDSNFAKVV SWYDNEWGYS NKVCEMARVI AAK
