ID   G3P1_BACCE              Reviewed;         334 AA.
AC   Q4MQ58; P83078;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE            Short=GAPDH 1;
DE            EC=1.2.1.12;
GN   Name=gap1; ORFNames=BCE_G9241_5218;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G9241;
RX   PubMed=15155910; DOI=10.1073/pnas.0402414101;
RA   Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D.,
RA   Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W.,
RA   Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z.,
RA   Rilstone J., Peterson S.N., Weyant R.S., Galloway D.R., Read T.D.,
RA   Popovic T., Fraser C.M.;
RT   "Identification of anthrax toxin genes in a Bacillus cereus associated
RT   with an illness resembling inhalation anthrax.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21, AND INDUCTION.
RC   STRAIN=NCIMB 11796 / DSM 626;
RX   PubMed=11851817; DOI=10.1046/j.1365-2672.2001.01478.x;
RA   Browne N., Dowds B.C.A.;
RT   "Heat and salt stress in the food pathogen Bacillus cereus.";
RL   J. Appl. Microbiol. 91:1085-1094(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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Repressed by salt stress.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; AAEK01000016; EAL14305.1; -; Genomic_DNA.
DR   SMR; Q4MQ58; 3-334.
DR   BRENDA; 1.2.1.12; 604.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    334       Glyceraldehyde-3-phosphate dehydrogenase
FT                                1.
FT                                /FTId=PRO_0000271247.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      150    152       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    151    151       Nucleophile (By similarity).
FT   BINDING      33     33       NAD (By similarity).
FT   BINDING      77     77       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     119    119       NAD (By similarity).
FT   BINDING     181    181       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     196    196       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     232    232       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     314    314       NAD (By similarity).
FT   SITE        178    178       Activates thiol group during catalysis
FT                                (By similarity).
FT   CONFLICT     13     13       G -> R (in Ref. 2; AA sequence).
SQ   SEQUENCE   334 AA;  35826 MW;  D5E1F3F4C45BF23B CRC64;
     MTKIGINGFG RIGRNVFRAA LNNSEVEVVA INDLTDAKTL AHLLKYDTVH GTLNAEVSAN
     ENSIVVNGKE IKVIAERDPA QLPWSDYGVE VVVESTGRFT KKSDAEKHLG GSVKKVIISA
     PASDEDITVV MGVNHEQYDA ANHNVVSNAS CTTNCLAPFA KVLNEKFGVK RGMMTTIHSY
     TNDQQILDLP HKDLRRARAA AENMIPTSTG AAKAVALVLP ELKGKLNGGA VRVPTANVSL
     VDLVVELDKE VTVEEVNAAF KAAAEGELKG ILGYSEEPLV SIDYNGCTAS STIDALSTMV
     MEGNMVKVLS WYDNETGYSN RVVDLAAYMT SKGL
//