ID   TPIC_FRAAN              Reviewed;         314 AA.
AC   Q9M4S8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Triosephosphate isomerase, chloroplastic;
DE            Short=TIM;
DE            Short=Triose-phosphate isomerase;
DE            EC=5.3.1.1;
DE   Flags: Precursor;
GN   Name=TPI;
OS   Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC   Fragaria.
OX   NCBI_TaxID=3747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Duch.;
RA   Kim I.-J., Chung W.-I.;
RT   "Cloning of a strawberry gene encoding a chloroplast triosephosphate
RT   isomerase.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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; Calvin cycle.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
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; AF257322; AAF66071.1; -; mRNA.
DR   AlphaFoldDB; Q9M4S8; -.
DR   SMR; Q9M4S8; -.
DR   PRIDE; Q9M4S8; -.
DR   UniPathway; UPA00116; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; 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   Calvin cycle; Chloroplast; Isomerase; Plastid; Transit peptide.
FT   TRANSIT         1..59
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           60..314
FT                   /note="Triosephosphate isomerase, chloroplastic"
FT                   /id="PRO_0000035650"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        224
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  33526 MW;  A7D8BBD98CE55853 CRC64;
     MAVASTSLAS QLSGPKSLSQ PYSGLRRSCP KLDQSHSSLF QHLSLSSSSR KASRAVVAMA
     GTGKFFVGGN WKCNGTKDLI SKLVSDLNSA KLEPDVDVVV APPFLYLDQV KSSLTDRIEI
     SGQNSWVAKG GAFTGEISVE QLKDIGRKWV ILGHSERRHV IGEDDQFIGK KAAYALNEGL
     GVIACIGEKL EEREAGKTFD VCYEQLKAFA DAVPSWENIV VAYEPVWAIG TGKVASPQQA
     QEVHVAVREW LKKNVSAEVA SKTRIIYGGS VNGGNSAELA KEEDIDGFLV GGASLKGPEF
     ATIVNAVTSK KVAA