ID   TPIS_HORVU              Reviewed;         253 AA.
AC   P34937; P93189;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Triosephosphate isomerase, cytosolic;
DE            Short=TIM;
DE            Short=Triose-phosphate isomerase;
DE            EC=5.3.1.1;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Rasmussen S.K.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-10.
RC   STRAIN=cv. H354-295-2-5; TISSUE=Starchy endosperm;
RX   PubMed=8125056; DOI=10.1002/elps.11501401169;
RA   Flengsrud R.;
RT   "Separation of acidic barley endosperm proteins by two-dimensional
RT   electrophoresis.";
RL   Electrophoresis 14:1060-1066(1993).
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.
CC   -!- TISSUE SPECIFICITY: Starchy endosperm.
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   ---------------------------------------------------------------------------
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; U83414; AAB41052.1; -; mRNA.
DR   AlphaFoldDB; P34937; -.
DR   SMR; P34937; -.
DR   IntAct; P34937; 1.
DR   PRIDE; P34937; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   ExpressionAtlas; P34937; baseline and differential.
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   Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW   Isomerase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8125056"
FT   CHAIN           2..253
FT                   /note="Triosephosphate isomerase, cytosolic"
FT                   /id="PRO_0000090147"
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"
FT   CONFLICT        2
FT                   /note="G -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   253 AA;  26737 MW;  023B216A6577EA5F CRC64;
     MGRKFFVGGN WKCNGTVEQV EAIVQTLNAG QIVSPDVVEV VVSPPYVFLP IVKAKLRPEI
     QVAAQNCWVK KGGAFTGEVS AEMLANLGVP WVILGHSERR SLLGESSEFV GEKVAYALAQ
     GLKVIACVGE TLEQREAGST MEVVAEQTKA IAGKIKDWSN GVVAYEPVWA IGTGKVATPA
     QAQEVHANLR DWLKTNVSPE VAESTRIIYG GSVTGASCKE LAAQADVDGF LVGGASLKPE
     FIDIINAAAV KSA