TPIS_TRYCR
ID TPIS_TRYCR Reviewed; 251 AA.
AC P52270;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Triosephosphate isomerase, glycosomal;
DE Short=TIM;
DE Short=Triose-phosphate isomerase;
DE EC=5.3.1.1;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ninoa;
RX PubMed=9108237; DOI=10.1111/j.1432-1033.1997.00700.x;
RA Ostoa-Saloma P., Garza-Ramos G., Ramirez J., Becker I., Berzunza M.,
RA Landa A., Gomez-Puyou A., Tuena de Gomez-Puyou M., Perez-Montfort R.;
RT "Cloning, expression, purification and characterization of triosephosphate
RT isomerase from Trypanosoma cruzi.";
RL Eur. J. Biochem. 244:700-705(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), AND HOMODIMERIZATION.
RC STRAIN=Ninoa;
RX PubMed=9761683; DOI=10.1006/jmbi.1998.2094;
RA Maldonado E., Soriano-Garcia M., Moreno A., Cabrera N., Garza-Ramos G.,
RA Tuena de Gomez-Puyou M., Gomez-Puyou A., Perez-Montfort R.;
RT "Differences in the intersubunit contacts in triosephosphate isomerase from
RT two closely related pathogenic trypanosomes.";
RL J. Mol. Biol. 283:193-203(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND HOMODIMERIZATION.
RC STRAIN=Ninoa;
RX PubMed=10468562; DOI=10.1073/pnas.96.18.10062;
RA Gao X.-G., Maldonado E., Perez-Montfort R., Garza-Ramos G.,
RA Tuena de Gomez-Puyou M., Gomez-Puyou A., Rodriguez-Romero A.;
RT "Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in
RT hexane.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10062-10067(1999).
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;
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Glycosome.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; U53867; AAB58349.1; -; Genomic_DNA.
DR PDB; 1CI1; X-ray; 2.00 A; A/B=1-251.
DR PDB; 1SUX; X-ray; 2.00 A; A/B=1-251.
DR PDB; 1TCD; X-ray; 1.83 A; A/B=3-251.
DR PDB; 2OMA; X-ray; 2.15 A; A/B=2-251.
DR PDB; 2V5B; X-ray; 2.00 A; A=1-251.
DR PDB; 3Q37; X-ray; 1.65 A; A/B/C/D=37-92, A/B/C/D=121-251.
DR PDB; 4HHP; X-ray; 1.50 A; A/B=1-251.
DR PDBsum; 1CI1; -.
DR PDBsum; 1SUX; -.
DR PDBsum; 1TCD; -.
DR PDBsum; 2OMA; -.
DR PDBsum; 2V5B; -.
DR PDBsum; 3Q37; -.
DR PDBsum; 4HHP; -.
DR AlphaFoldDB; P52270; -.
DR SMR; P52270; -.
DR BindingDB; P52270; -.
DR ChEMBL; CHEMBL5834; -.
DR DrugBank; DB03132; 3-(2-Benzothiazolylthio)-1-Propanesulfonic Acid.
DR VEuPathDB; TriTrypDB:BCY84_02271; -.
DR VEuPathDB; TriTrypDB:C3747_69g188; -.
DR VEuPathDB; TriTrypDB:C4B63_28g114; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0009200; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM12473; -.
DR VEuPathDB; TriTrypDB:TcCLB.508647.200; -.
DR VEuPathDB; TriTrypDB:TCDM_00802; -.
DR VEuPathDB; TriTrypDB:TcG_00710; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_001494; -.
DR VEuPathDB; TriTrypDB:TcYC6_0081760; -.
DR BRENDA; 5.3.1.1; 6524.
DR SABIO-RK; P52270; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P52270; -.
DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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 3D-structure; Gluconeogenesis; Glycolysis; Glycosome; Isomerase;
KW Peroxisome.
FT CHAIN 1..251
FT /note="Triosephosphate isomerase, glycosomal"
FT /id="PRO_0000090143"
FT ACT_SITE 96
FT /note="Electrophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:4HHP"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:4HHP"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:4HHP"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:4HHP"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:4HHP"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:4HHP"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:4HHP"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 181..199
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:4HHP"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:4HHP"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:4HHP"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:4HHP"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:4HHP"
SQ SEQUENCE 251 AA; 27329 MW; 03010B66586C186D CRC64;
MASKPQPIAA ANWKCNGSES LLVPLIETLN AATFDHDVQC VVAPTFLHIP MTKARLTNPK
FQIAAQNAIT RSGAFTGEVS LQILKDYGIS WVVLGHSERR LYYGETNEIV AEKVAQACAA
GFHVIVCVGE TNEEREAGRT AAVVLTQLAA VAQKLSKEAW SRVVIAYEPV WAIGTGKVAT
PQQAQEVHEL LRRWVRSKLG TDIAAQLRIL YGGSVTAKNA RTLYQMRDIN GFLVGGASLK
PEFVEIIEAT K
