ID   TPIS_GRAGA              Reviewed;         250 AA.
AC   P48492;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Triosephosphate isomerase, cytosolic;
DE            Short=TIM;
DE            Short=Triose-phosphate isomerase;
DE            EC=5.3.1.1;
DE   Flags: Fragment;
GN   Name=TPI1;
OS   Gracilaria gracilis (Red alga).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Gracilaria.
OX   NCBI_TaxID=2777;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8590477; DOI=10.1007/bf00326429;
RA   Zhou Y.H., Ragan M.A.;
RT   "Cloning and characterization of the nuclear gene and cDNAs for
RT   triosephosphate isomerase of the marine red alga Gracilaria verrucosa.";
RL   Curr. Genet. 28:317-323(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; L38662; AAB01378.1; -; Genomic_DNA.
DR   PIR; S59523; S59523.
DR   AlphaFoldDB; P48492; -.
DR   SMR; P48492; -.
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   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           <1..250
FT                   /note="Triosephosphate isomerase, cytosolic"
FT                   /id="PRO_0000090146"
FT   ACT_SITE        87
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         1
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         3
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   250 AA;  26686 MW;  D800EFFF452D4D9D CRC64;
     NWKCNLSKAD IAELVSAFNA APPIDAAHVQ VVVAPPAVYL DSTRQALRAD FDTSAQNAWI
     SKGGAFTGEL DAAMVKDVGA EWVILGHSER RHIAQLKESD HTIAMKAAYA LQHASLGVIY
     CIGELLEERE SGQTIAVCER QLQALSDAIS DWSDVVIAYE PVWAIGTGKV ATPEQAEQVH
     EAVRAWLANN VSPQVAASTR ILYGGSVSPA NCESLAKQPN IDGFLVGGAS MKPTFLEIVD
     SYKATLAEAV