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 01-MAY-2013, entry version 65.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE Short=GAPDH 1;
DE EC=1.2.1.12;
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 -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC dehydrogenase family.
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DR EMBL; BA000033; BAB94599.1; -; Genomic_DNA.
DR RefSeq; NP_645551.1; NC_003923.1.
DR ProteinModelPortal; P0A037; -.
DR SMR; P0A037; 1-336.
DR STRING; 196620.MW0734; -.
DR PRIDE; P0A037; -.
DR EnsemblBacteria; BAB94599; BAB94599; BAB94599.
DR GeneID; 1002845; -.
DR KEGG; sam:MW0734; -.
DR PATRIC; 19568022; VBIStaAur44266_0772.
DR eggNOG; COG0057; -.
DR HOGENOM; HOG000071678; -.
DR KO; K00134; -.
DR OMA; IVYNTNH; -.
DR ProtClustDB; CLSK884889; -.
DR BioCyc; SAUR196620:GJ9Z-755-MONOMER; -.
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; IEA:EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolysis; 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 TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT CHAIN 1 336 Glyceraldehyde-3-phosphate dehydrogenase
FT 1.
FT /FTId=PRO_0000145687.
FT NP_BIND 12 13 NAD (By similarity).
FT REGION 150 152 Glyceraldehyde 3-phosphate binding (By
FT similarity).
FT REGION 211 212 Glyceraldehyde 3-phosphate binding (By
FT similarity).
FT ACT_SITE 151 151 Nucleophile (By similarity).
FT BINDING 34 34 NAD (By similarity).
FT BINDING 181 181 Glyceraldehyde 3-phosphate (By
FT similarity).
FT BINDING 198 198 Glyceraldehyde 3-phosphate (By
FT similarity).
FT BINDING 234 234 Glyceraldehyde 3-phosphate (By
FT similarity).
FT BINDING 316 316 NAD (By similarity).
FT SITE 178 178 Activates thiol group during catalysis
FT (By similarity).
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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