ID   G3P2_STAES              Reviewed;         341 AA.
AC   Q8CNY0;
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 2;
DE            Short=GAPDH 2;
DE            EC=1.2.1.12;
GN   Name=gapA2; Synonyms=gapB; OrderedLocusNames=SE_1361;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE015929; AAO04960.1; -; Genomic_DNA.
DR   RefSeq; NP_764916.1; -.
DR   HSSP; P00362; 1GD1.
DR   GeneID; 1056375; -.
DR   GenomeReviews; AE015929_GR; SE_1361.
DR   KEGG; sep:SE1361; -.
DR   HOGENOM; Q8CNY0; -.
DR   OMA; Q8CNY0; TNPHSAI.
DR   BioCyc; SEPI176280:SE_1361-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    341       Glyceraldehyde-3-phosphate dehydrogenase
FT                                2.
FT                                /FTId=PRO_0000145697.
FT   NP_BIND      12     13       NAD (By similarity).
FT   REGION      152    154       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      211    212       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    153    153       Nucleophile (By similarity).
FT   BINDING      78     78       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     183    183       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     313    313       NAD (By similarity).
FT   SITE        180    180       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   341 AA;  37092 MW;  1A63E6D561C77592 CRC64;
     MATNIAINGM GRIGRMVLRI ALNNKNLNVK AINASYPPET IAHLLNYDTT HGVYDKKVEP
     IESGIKVNGH EIKLLSDRNP ENLPWNEMDI DVVIEATGKF NHGDKAVAHI NAGAKKVLLT
     GPSKGGDVQM IVKGVNDNQL DIDTYDIFSN ASCTTNCIGP VAKVLNDKFG IINGLMTTVH
     AITNDQKNID NPHKDLRRAR SCNESIIPTS TGAAKALKEV LPEVEGKLHG MALRVPTKNV
     SLVDLVVDLE QNVTVTQVND AFKNADLSGV LDVEEAPLVS VDFNTNPHSA IIDSQSTMVM
     GQNKVKVIAW YDNEWGYSNR VVEVAVKIGQ LIDDKAMVKA I
//