TPIS_LEIME
ID TPIS_LEIME Reviewed; 251 AA.
AC P48499;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
OS Leishmania mexicana.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5665;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8125090; DOI=10.1111/j.1432-1033.1994.tb18629.x;
RA Kohl L., Callens M., Wierenga R.K., Opperdoes F.R., Michels P.A.M.;
RT "Triose-phosphate isomerase of Leishmania mexicana mexicana. Cloning and
RT characterization of the gene, overexpression in Escherichia coli and
RT analysis of the protein.";
RL Eur. J. Biochem. 220:331-338(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
RX PubMed=10235625; DOI=10.1093/protein/12.3.243;
RA Williams J.C., Zeelen J.P., Neubauer G., Vriend G., Backmann J.,
RA Michels P.A.M., Lambeir A.-M., Wierenga R.K.;
RT "Structural and mutagenesis studies of leishmania triosephosphate
RT isomerase: a point mutation can convert a mesophilic enzyme into a
RT superstable enzyme without losing catalytic power.";
RL Protein Eng. 12:243-250(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RX PubMed=11589711; DOI=10.1046/j.0014-2956.2001.02452.x;
RA Kursula I., Partanen S., Lambeir A.-M., Antonov D.M., Augustyns K.,
RA Wierenga R.K.;
RT "Structural determinants for ligand binding and catalysis of
RT triosephosphate isomerase.";
RL Eur. J. Biochem. 268:5189-5196(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (0.83 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RX PubMed=12522213; DOI=10.1074/jbc.m211389200;
RA Kursula I., Wierenga R.K.;
RT "Crystal structure of triosephosphate isomerase complexed with 2-
RT phosphoglycolate at 0.83-A resolution.";
RL J. Biol. Chem. 278:9544-9551(2003).
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. {ECO:0000269|PubMed:11589711,
CC ECO:0000269|PubMed:12522213}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Glycosome.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X74797; CAA52804.1; -; Genomic_DNA.
DR PIR; S42356; S42356.
DR PDB; 1AMK; X-ray; 1.83 A; A=1-251.
DR PDB; 1IF2; X-ray; 2.00 A; A=1-251.
DR PDB; 1N55; X-ray; 0.83 A; A=1-251.
DR PDB; 1QDS; X-ray; 2.00 A; A=1-251.
DR PDB; 2VXN; X-ray; 0.82 A; A=1-251.
DR PDB; 2Y61; X-ray; 0.99 A; A=1-251.
DR PDB; 2Y62; X-ray; 1.08 A; A=1-251.
DR PDB; 2Y63; X-ray; 1.97 A; A=1-251.
DR PDB; 7ABX; X-ray; 1.20 A; A=1-251.
DR PDB; 7AZ3; Other; 1.15 A; A=1-251.
DR PDB; 7AZ4; Other; 1.15 A; A=1-251.
DR PDB; 7AZ9; Other; 1.10 A; A=1-251.
DR PDB; 7AZA; Other; 1.10 A; A=1-251.
DR PDBsum; 1AMK; -.
DR PDBsum; 1IF2; -.
DR PDBsum; 1N55; -.
DR PDBsum; 1QDS; -.
DR PDBsum; 2VXN; -.
DR PDBsum; 2Y61; -.
DR PDBsum; 2Y62; -.
DR PDBsum; 2Y63; -.
DR PDBsum; 7ABX; -.
DR PDBsum; 7AZ3; -.
DR PDBsum; 7AZ4; -.
DR PDBsum; 7AZ9; -.
DR PDBsum; 7AZA; -.
DR AlphaFoldDB; P48499; -.
DR SMR; P48499; -.
DR VEuPathDB; TriTrypDB:LmxM.24.0850; -.
DR BRENDA; 5.3.1.1; 2951.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P48499; -.
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; Cytoplasm; Gluconeogenesis; Glycolysis; Glycosome; Isomerase;
KW Peroxisome.
FT CHAIN 1..251
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090137"
FT ACT_SITE 96
FT /note="Electrophile"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT BINDING 12
FT /ligand="substrate"
FT BINDING 14
FT /ligand="substrate"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:2VXN"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:2VXN"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2VXN"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:2VXN"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:2VXN"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:2VXN"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2VXN"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 181..198
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:2VXN"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:2VXN"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:2VXN"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:2VXN"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:2VXN"
SQ SEQUENCE 251 AA; 27178 MW; 987DFEED46F1E3EE CRC64;
MSAKPQPIAA ANWKCNGTTA SIEKLVQVFN EHTISHDVQC VVAPTFVHIP LVQAKLRNPK
YVISAENAIA KSGAFTGEVS MPILKDIGVH WVILGHSERR TYYGETDEIV AQKVSEACKQ
GFMVIACIGE TLQQREANQT AKVVLSQTSA IAAKLTKDAW NQVVLAYEPV WAIGTGKVAT
PEQAQEVHLL LRKWVSENIG TDVAAKLRIL YGGSVNAANA ATLYAKPDIN GFLVGGASLK
PEFRDIIDAT R
