ID   TPIS_LACSA              Reviewed;         195 AA.
AC   P48493;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Triosephosphate isomerase, cytosolic;
DE            Short=TIM;
DE            Short=Triose-phosphate isomerase;
DE            EC=5.3.1.1;
DE   Flags: Fragment;
OS   Lactuca sativa (Garden lettuce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Lactucinae; Lactuca.
OX   NCBI_TaxID=4236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=1356093; DOI=10.1139/g92-094;
RA   Paran I., Kesseli R.V., Westphal L., Michelmore R.W.;
RT   "Recent amplification of triose phosphate isomerase related sequences in
RT   lettuce.";
RL   Genome 35:627-635(1992).
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:0000255|PROSITE-ProRule:PRU10127};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-
CC       ProRule:PRU10127}.
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:0000255|PROSITE-ProRule:PRU10127}.
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; S46215; AAB23371.1; -; mRNA.
DR   EMBL; S46210; AAB23372.1; -; Genomic_DNA.
DR   EMBL; S46213; AAB23372.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; P48493; -.
DR   SMR; P48493; -.
DR   PRIDE; P48493; -.
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   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035990; TIM_sf.
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..195
FT                   /note="Triosephosphate isomerase, cytosolic"
FT                   /id="PRO_0000090148"
FT   ACT_SITE        37
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   ACT_SITE        107
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   NON_TER         1
SQ   SEQUENCE   195 AA;  20540 MW;  40F1F9C408F97600 CRC64;
     IQVAAQNCWV KKGGAFTGEV SAEMLANLGV PWVILGHSER RALLNETNEF VGDKVAYALS
     QGLKVIACVG ETLEQREAGT TMEVVAAQTK AIADKISSWD NVVLAYEPVW AIGTGKVASP
     AQAQEVHAGL RKWFCDNVSA EVSASTRIIY GGSVSGSNCK ELGGQTDVDG FLVGGASLKP
     EFIDIIKAAE VKKSA