TPIS_BACCE
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 03-AUG-2022, entry version 93.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147};
DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147};
DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; Synonyms=tim;
GN ORFNames=BCE_G9241_5215;
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; 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., Rilstone J.,
RA Peterson S.N., Weyant R.S., Galloway D.R., Read T.D., Popovic T.,
RA Fraser C.M.;
RT "Identification of anthrax toxin genes in a Bacillus cereus associated with
RT 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=DSM 626 / NCIMB 11796 / T;
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 -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate;
CC Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00147}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00147}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00147}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
CC -!- INDUCTION: By salt stress and heat shock.
CC {ECO:0000269|PubMed:11851817}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00147}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL14302.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AAEK01000016; EAL14302.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB083542; BAB88970.1; -; Genomic_DNA.
DR RefSeq; WP_001231038.1; NZ_WBPP01000004.1.
DR AlphaFoldDB; Q4MQ55; -.
DR SMR; Q4MQ55; -.
DR STRING; 1396.DJ87_4721; -.
DR GeneID; 58159340; -.
DR GeneID; 67509761; -.
DR eggNOG; COG0149; Bacteria.
DR OMA; QEVCGAI; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00147_B; TIM_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 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; Phosphoprotein; Stress response.
FT CHAIN 1..251
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000271233"
FT ACT_SITE 95
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 9..11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 234..235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
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
