ID   TPIS_TAESO              Reviewed;         250 AA.
AC   Q9GTX8;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
OS   Taenia solium (Pork tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=6204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10980291; DOI=10.1016/s0020-7519(00)00089-8;
RA   Jimenez L., Vibanco-Perez N., Navarro L., Landa A.;
RT   "Cloning, expression and characterisation of a recombinant triosephosphate
RT   isomerase from Taenia solium.";
RL   Int. J. Parasitol. 30:1007-1012(2000).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; AF244894; AAG21132.1; -; mRNA.
DR   PDB; 6OOG; X-ray; 2.02 A; A=1-250.
DR   PDBsum; 6OOG; -.
DR   AlphaFoldDB; Q9GTX8; -.
DR   SMR; Q9GTX8; -.
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-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; Isomerase.
FT   CHAIN           1..250
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000090141"
FT   ACT_SITE        94
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           17..29
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   STRAND          37..42
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           47..53
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   STRAND          58..63
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           79..84
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           95..99
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           105..117
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   STRAND          121..126
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           130..134
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           138..150
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           157..161
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   TURN            172..174
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           180..197
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           200..205
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   STRAND          208..213
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   TURN            216..218
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           219..223
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           235..238
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   HELIX           241..246
FT                   /evidence="ECO:0007829|PDB:6OOG"
FT   TURN            247..249
FT                   /evidence="ECO:0007829|PDB:6OOG"
SQ   SEQUENCE   250 AA;  27167 MW;  34FBA51A9853EDFD CRC64;
     MTRKLFVGGN WKMNGSYSHI NTFFDTLQKA DTDPNADIVI GVPACYLKYA QDKAPKGIKI
     AAENCYKVGS GAFTGEISTE MIKDCGCEWV ILGHSERRHI FGESNELIGE KVKHALDSGL
     NVIPCIGELL SEREAGKTND VCFAQMDAIA KNVPSKEAWD KVVIAYEPVW AIGTGKTATP
     AQAQEVHKVV RDWIRKHVDA GIADKVRILY GGSVTASNAK DLGTQPDVDG FLVGGASLKP
     DFITIINARR