GenomeNet

Database: UniProt
Entry: P0A037
LinkDB: P0A037
Original site: P0A037 
ID   G3P1_STAAW              Reviewed;         336 AA.
AC   P0A037; Q9Z5C5;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   09-DEC-2015, entry version 80.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1 {ECO:0000250|UniProtKB:Q6GIL8};
DE            Short=GAPDH 1 {ECO:0000250|UniProtKB:Q6GIL8};
DE            EC=1.2.1.12 {ECO:0000250|UniProtKB:Q6GIL8};
DE   AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:Q6GIL8};
GN   Name=gapA1; Synonyms=gap, gapA; OrderedLocusNames=MW0734;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Catalyzes the oxidative phosphorylation of
CC       glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG)
CC       using the cofactor NAD. The first reaction step involves the
CC       formation of a hemiacetal intermediate between G3P and a cysteine
CC       residue, and this hemiacetal intermediate is then oxidized to a
CC       thioester, with concomitant reduction of NAD to NADH. The reduced
CC       NADH is then exchanged with the second NAD, and the thioester is
CC       attacked by a nucleophilic inorganic phosphate to produce BPG.
CC       {ECO:0000250|UniProtKB:Q6GIL8}.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC       {ECO:0000250|UniProtKB:Q6GIL8}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q6GIL8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; BA000033; BAB94599.1; -; Genomic_DNA.
DR   RefSeq; WP_000279414.1; NC_003923.1.
DR   ProteinModelPortal; P0A037; -.
DR   SMR; P0A037; 1-336.
DR   PRIDE; P0A037; -.
DR   EnsemblBacteria; BAB94599; BAB94599; BAB94599.
DR   GeneID; 23196651; -.
DR   PATRIC; 19568022; VBIStaAur44266_0772.
DR   HOGENOM; HOG000071678; -.
DR   OMA; FVRVLSW; -.
DR   OrthoDB; EOG66TG3S; -.
DR   BioCyc; SAUR196620:GJ9Z-755-MONOMER; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000000418; 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   Gene3D; 3.40.50.720; -; 1.
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; IPR016040; NAD(P)-bd_dom.
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   Complete proteome; Cytoplasm; Glycolysis; NAD; Nucleotide-binding;
KW   Oxidoreductase.
FT   CHAIN         1    336       Glyceraldehyde-3-phosphate dehydrogenase
FT                                1.
FT                                /FTId=PRO_0000145687.
FT   NP_BIND      12     13       NAD. {ECO:0000250|UniProtKB:Q6GIL8}.
FT   REGION      150    152       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000250|UniProtKB:Q6GIL8}.
FT   REGION      211    212       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000250|UniProtKB:Q6GIL8}.
FT   ACT_SITE    151    151       Nucleophile.
FT                                {ECO:0000250|UniProtKB:Q6GIL8}.
FT   BINDING      34     34       NAD. {ECO:0000250|UniProtKB:Q6GIL8}.
FT   BINDING     120    120       NAD. {ECO:0000250|UniProtKB:Q6GIL8}.
FT   BINDING     181    181       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000250|UniProtKB:Q6GIL8}.
FT   BINDING     198    198       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000250|UniProtKB:P00362}.
FT   BINDING     234    234       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000250|UniProtKB:Q6GIL8}.
FT   BINDING     316    316       NAD. {ECO:0000250|UniProtKB:Q6GIL8}.
FT   SITE        178    178       Activates thiol group during catalysis.
FT                                {ECO:0000250|UniProtKB:Q6GIL8}.
SQ   SEQUENCE   336 AA;  36281 MW;  37A6CEA9376779E5 CRC64;
     MAVKVAINGF GRIGRLAFRR IQEVEGLEVV AVNDLTDDDM LAHLLKYDTM QGRFTGEVEV
     VDGGFRVNGK EVKSFSEPDA SKLPWKDLNI DVVLECTGFY TDKDKAQAHI EAGAKKVLIS
     APATGDLKTI VFNTNHQELD GSETVVSGAS CTTNSLAPVA KVLNDDFGLV EGLMTTIHAY
     TGDQNTQDAP HRKGDKRRAR AAAENIIPNS TGAAKAIGKV IPEIDGKLDG GAQRVPVATG
     SLTELTVVLE KQDVTVEQVN EAMKNASNES FGYTEDEIVS SDVVGMTYGS LFDATQTRVM
     SVGDRQLVKV AAWYDNEMSY TAQLVRTLAY LAELSK
//
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