G3P_SALTY
ID G3P_SALTY Reviewed; 331 AA.
AC P0A1P0; P24165;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
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};
GN Name=gapA; Synonyms=gap; OrderedLocusNames=STM1290;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-309.
RC STRAIN=LT2;
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; AE006468; AAL20215.1; -; Genomic_DNA.
DR EMBL; M63369; AAA27114.1; -; Genomic_DNA.
DR RefSeq; NP_460256.1; NC_003197.2.
DR RefSeq; WP_000153505.1; NC_003197.2.
DR AlphaFoldDB; P0A1P0; -.
DR SMR; P0A1P0; -.
DR STRING; 99287.STM1290; -.
DR PaxDb; P0A1P0; -.
DR PRIDE; P0A1P0; -.
DR EnsemblBacteria; AAL20215; AAL20215; STM1290.
DR GeneID; 1252808; -.
DR KEGG; stm:STM1290; -.
DR PATRIC; fig|99287.12.peg.1371; -.
DR HOGENOM; CLU_030140_0_3_6; -.
DR OMA; NCVAPMA; -.
DR PhylomeDB; P0A1P0; -.
DR BioCyc; SENT99287:STM1290-MON; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..331
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145677"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT CONFLICT 95
FT /note="E -> D (in Ref. 2; AAA27114)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="G -> V (in Ref. 2; AAA27114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 35587 MW; 872BA8D616C807B0 CRC64;
MTIKVGINGF GRIGRIVFRA AQKRSDIEIV AINDLLDAEY MAYMLKYDST HGRFDGTVEV
KDGHLIVNGK KIRVTAERDP ANLKWDEVGV DVVAEATGIF LTDETARKHI TAGAKKVVLT
GPSKDNTPMF VKGANFDKYE GQDIVSNASC TTNCLAPLAK VINDNFGIIE GLMTTVHATT
ATQKTVDGPS HKDWRGGRGA SQNIIPSSTG AAKAVGKVLP ELNGKLTGMA FRVPTPNVSV
VDLTVRLEKA ATYEQIKAAV KAAAEGEMKG VLGYTEDDVV STDFNGEVCT SVFDAKAGIA
LNDNFVKLVS WYDNETGYSN KVLDLIAHIS K
