TPIS_CLOTE
ID TPIS_CLOTE Reviewed; 255 AA.
AC Q898R2;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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}; OrderedLocusNames=CTC_00380;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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 -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00147}.
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DR EMBL; AE015927; AAO35017.1; -; Genomic_DNA.
DR AlphaFoldDB; Q898R2; -.
DR SMR; Q898R2; -.
DR STRING; 212717.CTC_00380; -.
DR EnsemblBacteria; AAO35017; AAO35017; CTC_00380.
DR KEGG; ctc:CTC_00380; -.
DR HOGENOM; CLU_024251_2_3_9; -.
DR OMA; QEVCGAI; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001412; Chromosome.
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 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..255
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090212"
FT ACT_SITE 100
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 15..17
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 239..240
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
SQ SEQUENCE 255 AA; 28288 MW; 68A42903A7EEBC40 CRC64;
MKGVYGLRKA IIAGNWKMHN TIDESVKLVE ELIPKVKEAE CEVVVCPPFI CLPKIREITE
GTNIKVGAQN MYFEEKGAFT GEVSPLMLEK LNIDYVIIGH SERRQYFKET DQTVNKKLKA
AFEHNLIPIL CVGETLDEKE NGVTEEVVSK QVKLGLFELK EEQVEKLVIA YEPIWAIGTG
KTATSEEANE VIALIRSTVK SLYGDKVAES LRIQYGGSVK PSTIKEQMSM SDIDGALVGG
ASLKANDFSA IVNYK
