ID   TPIS_SECCE              Reviewed;         253 AA.
AC   P46226;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Triosephosphate isomerase, cytosolic;
DE            Short=TIM;
DE            Short=Triose-phosphate isomerase;
DE            EC=5.3.1.1;
OS   Secale cereale (Rye).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Secale.
OX   NCBI_TaxID=4550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Halo; TISSUE=Leaf;
RX   PubMed=7711069; DOI=10.1016/0167-4781(95)00015-9;
RA   Schmidt M., Svendsen I., Feierabend J.;
RT   "Analysis of the primary structure of the chloroplast isozyme of
RT   triosephosphate isomerase from rye leaves by protein and cDNA sequencing
RT   indicates a eukaryotic origin of its gene.";
RL   Biochim. Biophys. Acta 1261:257-264(1995).
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   -!- MISCELLANEOUS: In plants, there are two types of TPIS, cytosolic and
CC       plastid.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; Z26875; CAA81487.1; -; mRNA.
DR   PIR; S53760; S53760.
DR   AlphaFoldDB; P46226; -.
DR   SMR; P46226; -.
DR   PRIDE; P46226; -.
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   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..253
FT                   /note="Triosephosphate isomerase, cytosolic"
FT                   /id="PRO_0000090154"
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;  26927 MW;  FCFC24AEC06F6670 CRC64;
     MGRKFFVGGN WKCNGTVSQV ETIVNTLNAG QIASPDVVEV VVSPPYVFLP TVKDKLRPEI
     QVAAQNCWVK KGGAFTGEVS AEMLVNLGIP WVILGHSERR SLLAESSEFV GEKVAYALAQ
     GLKVIACVGE TLEQREAGST MEVVAEQTKA IADKIKDWTN VVVAYEPVWA IGTGKVASPA
     QAQEVHANLR DWLKTNVSPE VAESTRIIYG GSVTGASCKE LAAQPDVDGF LVGGASLKPE
     FIDIINAATV KSA