ID   G3P1_STAES              Reviewed;         336 AA.
AC   Q8CPY5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 49.
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=SE_0557;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22832016; PubMed=12950922;
RX   DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04154.1; -; Genomic_DNA.
DR   RefSeq; NP_764112.1; -.
DR   HSSP; P17721; 1HDG.
DR   GeneID; 1055968; -.
DR   GenomeReviews; AE015929_GR; SE_0557.
DR   KEGG; sep:SE0557; -.
DR   HOGENOM; Q8CPY5; -.
DR   OMA; Q8CPY5; GKQLVKT.
DR   BioCyc; SEPI176280:SE_0557-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000173; GlycerAld_3-P_DH.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   PANTHER; PTHR10836; GAP_DH; 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   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_0000145689.
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;  36191 MW;  A962202D02AB5767 CRC64;
     MAIKVAINGF GRIGRLAFRR IQDVEGLEVV AVNDLTDDDM LAHLLKYDTM QGRFTGEVEV
     IEGGFRVNGK EIKSFDEPDA GKLPWGDLDI DVVLECTGFY TDKEKAQAHI DAGAKKVLIS
     APAKGDVKTI VFNTNHDTLD GSETVVSGAS CTTNSLAPVA KVLSDEFGLV EGFMTTIHAY
     TGDQNTQDAP HRKGDKRRAR AAAENIIPNS TGAAKAIGKV IPEIDGKLDG GAQRVPVATG
     SLTELTVVLD KQDVTVDQVN SAMKQASDES FGYTEDEIVS SDIVGMTYGS LFDATQTRVM
     TVGDRQLVKV AAWYDNEMSY TAQLVRTLAH LAELSK
//