ID   TPIS_COPJA              Reviewed;         253 AA.
AC   P21820;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Triosephosphate isomerase, cytosolic;
DE            Short=TIM;
DE            Short=Triose-phosphate isomerase;
DE            EC=5.3.1.1;
OS   Coptis japonica (Japanese goldthread).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Coptidoideae;
OC   Coptis.
OX   NCBI_TaxID=3442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2463630; DOI=10.1073/pnas.86.2.534;
RA   Okada N., Koizumi N., Tanaka T., Ohkubo H., Nakanishi S., Yamada Y.;
RT   "Isolation, sequence, and bacterial expression of a cDNA for (S)-
RT   tetrahydroberberine oxidase from cultured berberine-producing Coptis
RT   japonica cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:534-538(1989).
RN   [2]
RP   ERRATUM OF PUBMED:2463630.
RA   Okada N., Koizumi N., Tanaka T., Ohkubo H., Nakanishi S., Yamada Y.;
RL   Proc. Natl. Acad. Sci. U.S.A. 87:6928-6928(1990).
RN   [3]
RP   REVISION OF FUNCTION.
RX   PubMed=1368616; DOI=10.1271/bbb1961.54.2189;
RA   Sato F., Fitchen J.H., Takeshita N., Hashimoto T., Okada N., Yamada Y.;
RT   "Synthesis of plant triosephosphate isomerase in Escherichia coli.";
RL   Agric. Biol. Chem. 54:2189-2191(1990).
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: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: In plants, there are two types of TPIS, cytosolic and
CC       plastid.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be (S)-tetrahydro-berberine oxidase
CC       (EC 1.3.3.8). {ECO:0000305|PubMed:2463630}.
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DR   EMBL; J04121; AAB62730.1; -; mRNA.
DR   PIR; A32187; A32187.
DR   AlphaFoldDB; P21820; -.
DR   SMR; P21820; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..253
FT                   /note="Triosephosphate isomerase, cytosolic"
FT                   /id="PRO_0000090145"
FT   ACT_SITE        96
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        166
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"
SQ   SEQUENCE   253 AA;  27090 MW;  AF51C997D0A2E93A CRC64;
     MGRKFFVGGN WKCNGTSEEV KKIVTLLNEA EVPSEDVVEV VVSPPYVFLP FVKNLLRADF
     HVAAQNCWVK KGGAFTGEVS AEMLVNLGIP WVILGHSERR ALLNESNEFV GDKTAYALSQ
     GLKVIACVGE TLEQREAGST ISVVAAQTKA IAEKVSDWTN IVVAYEPVWA IGTGKVASPA
     QAQEVHFELR KWIKENVGAD VAGSVRIIYG GSVNGANSKE LAGQPDIDGF LVGGASLKPE
     FVDIIKSATV KSS