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G3P_BUCAP
ID   G3P_BUCAP               Reviewed;         332 AA.
AC   Q07234;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 145.
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; OrderedLocusNames=BUsg_287;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7765846; DOI=10.1007/bf00296197;
RA   Kolibachuk D., Baumann P.;
RT   "Buchnera aphidicola (aphid-endosymbiont) glyceraldehyde-3-phosphate
RT   dehydrogenase: molecular cloning and sequence analysis.";
RL   Curr. Microbiol. 30:133-136(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-170.
RX   PubMed=7763501; DOI=10.1007/bf01577382;
RA   Clark M.A., Baumann P.;
RT   "Aspects of energy-yielding metabolism in the aphid, Schizaphis graminum,
RT   and its endosymbiont: detection of gene fragments potentially coding for
RT   the ATP synthase beta-subunit and glyceraldehyde-3-phosphate
RT   dehydrogenase.";
RL   Curr. Microbiol. 26:233-237(1993).
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; U11045; AAC05798.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM67843.1; -; Genomic_DNA.
DR   EMBL; Z15146; CAA78852.1; -; Genomic_DNA.
DR   PIR; I40069; I40069.
DR   RefSeq; WP_011053810.1; NC_004061.1.
DR   AlphaFoldDB; Q07234; -.
DR   SMR; Q07234; -.
DR   STRING; 198804.BUsg_287; -.
DR   PRIDE; Q07234; -.
DR   EnsemblBacteria; AAM67843; AAM67843; BUsg_287.
DR   KEGG; bas:BUsg_287; -.
DR   eggNOG; COG0057; Bacteria.
DR   HOGENOM; CLU_030140_0_3_6; -.
DR   OMA; NCVAPMA; -.
DR   OrthoDB; 944149at2; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000000416; Chromosome.
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..332
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT                   /id="PRO_0000145639"
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"
SQ   SEQUENCE   332 AA;  36484 MW;  B72928326B2BB302 CRC64;
     MTIKIGINGF GRIGRVLFRL AQERENIEVV AINDLLDPKY IAYMLKYDST HGNFKKDIEV
     KNNNLIINGK KIRITSIKDP EKLMWDKLLI DVVIESTGLF LTKDTAYKHI LSGAKKVVIT
     GPSKDDIPMF VRGANFDKYK GEKIVSNASC TTNCLAPLSK VIDDHFGIIE GLMTTVHAST
     ATQKIVDSAS KKDWRGGRGA LQNIIPSSTG AAVAVGKVLP NLNGKLTGIA FRVPTANVSV
     VDLTVRYKKT ATYNEICEVV KNASEQKMKG ILGYTEDEVV STDFNGKELT SIFDAKAGLS
     LNKNFAKLIS WYDNETGYSS KVLDLVELVA LK
 
 
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