ID   G3P2_STAAM              Reviewed;         341 AA.
AC   P64180; Q99TH5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-NOV-2008, entry version 28.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2;
DE            Short=GAPDH 2;
DE            EC=1.2.1.12;
GN   Name=gapA2; Synonyms=gapB; OrderedLocusNames=SAV1687;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB57849.1; -; Genomic_DNA.
DR   RefSeq; NP_372211.1; -.
DR   HSSP; P00362; 1GD1.
DR   World-2DPAGE; 0002:P64180; -.
DR   GeneID; 1121662; -.
DR   GenomeReviews; BA000017_GR; SAV1687.
DR   KEGG; sav:SAV1687; -.
DR   HOGENOM; P64180; -.
DR   BioCyc; SAUR158878:SAV1687-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro.
DR   GO; GO:0051287; F:NAD 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_DHase.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DHase_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   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN         1    341       Glyceraldehyde-3-phosphate dehydrogenase
FT                                2.
FT                                /FTId=PRO_0000145692.
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;  36979 MW;  0757DE38BC89F14C CRC64;
     MSTNIAINGM GRIGRMVLRI ALQNKNLNVV AINASYPPET IAHLINYDTT HGKYNLKVEP
     IENGLQVGDH KIKLVADRNP ENLPWKELDI DIAIDATGKF NHGDKAIAHI KAGAKKVLLT
     GPSKGGHVQM VVKGVNDNQL DIEAFDIFSN ASCTTNCIGP VAKVLNNQFG IVNGLMTTVH
     AITNDQKNID NPHKDLRRAR SCNESIIPTS TGAAKALKEV LPELEGKLHG MALRVPTKNV
     SLVDLVVDLE KEVTAEEVNQ AFENAGLEGI IEVEHQPLVS VDFNTNPNSA IIDAKSTMVM
     SGNKVKVIAW YDNEWGYSNR VVDVAEQIGA LLTSKETVSA S
//