TPIS_PLAF7
ID TPIS_PLAF7 Reviewed; 248 AA.
AC Q7KQM0; A0A144A4G4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Triosephosphate isomerase {ECO:0000250|UniProtKB:Q07412};
DE Short=PfTIM {ECO:0000250|UniProtKB:Q07412};
DE EC=5.3.1.1 {ECO:0000250|UniProtKB:Q07412};
DE AltName: Full=Triose-phosphate isomerase;
GN Name=TPI {ECO:0000250|UniProtKB:Q07412}; ORFNames=PF14_0378, PF3D7_1439900;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
CC -!- FUNCTION: Catalyzes the interconversion of glyceraldehyde 3-phosphate
CC and dihydroxyacetone phosphate in the glycolytic and gluconeogenic
CC pathways. {ECO:0000250|UniProtKB:Q07412}.
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:0000250|UniProtKB:Q07412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18586;
CC Evidence={ECO:0000250|UniProtKB:Q07412};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000250|UniProtKB:Q07412}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1.
CC {ECO:0000250|UniProtKB:Q07412}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q07412}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; LN999946; CZU00095.1; -; Genomic_DNA.
DR RefSeq; XP_001348552.1; XM_001348516.2.
DR AlphaFoldDB; Q7KQM0; -.
DR SMR; Q7KQM0; -.
DR STRING; 5833.PF14_0378; -.
DR SwissPalm; Q7KQM0; -.
DR PRIDE; Q7KQM0; -.
DR EnsemblProtists; CZU00095; CZU00095; PF3D7_1439900.
DR GeneID; 811960; -.
DR KEGG; pfa:PF3D7_1439900; -.
DR VEuPathDB; PlasmoDB:PF3D7_1439900; -.
DR HOGENOM; CLU_024251_2_3_1; -.
DR InParanoid; Q7KQM0; -.
DR OMA; QEVCGAI; -.
DR PhylomeDB; Q7KQM0; -.
DR Reactome; R-PFA-70171; Glycolysis.
DR Reactome; R-PFA-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001450; Chromosome 14.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:GeneDB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISS:GeneDB.
DR GO; GO:0006094; P:gluconeogenesis; ISS:GeneDB.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; ISS:GeneDB.
DR GO; GO:0006098; P:pentose-phosphate shunt; ISS:GeneDB.
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 Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..248
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000233387"
FT ACT_SITE 95
FT /note="Electrophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT BINDING 10
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q07412"
FT BINDING 12
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q07412"
FT BINDING 171
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q07412"
FT BINDING 230
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q07412"
FT BINDING 232..233
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q07412"
SQ SEQUENCE 248 AA; 27935 MW; EFC8A4373EA9BED1 CRC64;
MARKYFVAAN WKCNGTLESI KSLTNSFNNL DFDPSKLDVV VFPVSVHYDH TRKLLQSKFS
TGIQNVSKFG NGSYTGEVSA EIAKDLNIEY VIIGHFERRK YFHETDEDVR EKLQASLKNN
LKAVVCFGES LEQREQNKTI EVITKQVKAF VDLIDNFDNV ILAYEPLWAI GTGKTATPEQ
AQLVHKEIRK IVKDTCGEKQ ANQIRILYGG SVNTENCSSL IQQEDIDGFL VGNASLKESF
VDIIKSAM
