ID   TPIS_BACCE              Reviewed;         251 AA.
AC   Q4MQ55; P83069; Q8RQH4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=tpiA; Synonyms=tim; ORFNames=BCE_G9241_5215;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141.
RC   STRAIN=Tim-r01;
RA   Nishizawa M., Itoi Y., Ito S., Inoue M.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 1-15, 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 = glycerone
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- INDUCTION: By salt stress and heat shock.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
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DR   EMBL; AAEK01000016; EAL14302.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AB083542; BAB88970.1; -; Genomic_DNA.
DR   SMR; Q4MQ55; 2-249.
DR   BRENDA; 5.3.1.1; 604.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:HAMAP.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   HAMAP; MF_00147; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000652; Triosephosphate_isomerase.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR21139; Triophos_ismrse; 1.
DR   Pfam; PF00121; TIM; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW   Isomerase; Pentose shunt; Phosphoprotein; Stress response.
FT   CHAIN         1    251       Triosephosphate isomerase.
FT                                /FTId=PRO_0000271233.
FT   ACT_SITE     95     95       Electrophile (By similarity).
FT   ACT_SITE    167    167       Proton acceptor (By similarity).
FT   BINDING       9      9       Substrate (By similarity).
FT   BINDING      11     11       Substrate (By similarity).
FT   MOD_RES     213    213       Phosphoserine (By similarity).
SQ   SEQUENCE   251 AA;  26468 MW;  65066B1BDE8FA601 CRC64;
     MRKPIIAGNW KMNKTLSEAV SFVEEVKGQI PAASAVDAVV CSPALFLERL VAATEGTDLQ
     VGAQNMHFEK NGAFTGEISP VALSDLKVGY VVLGHSERRE MFAETDESVN KKTIAAFEHG
     LTPIVCCGET LEERESGKTF DLVAGQVTKA LAGLTEEQVK ATVIAYEPIW AIGTGKSSSS
     ADANEVCAHI RKVVAEAVSP EAAEAVRIQY GGSVKPENIK EYMAQSDIDG ALVGGASLEP
     ASFLGLLGAV K
//