ID   TPIC_SPIOL              Reviewed;         322 AA.
AC   P48496;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 102.
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=TPIP1;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Amaranthaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Monnopa; TISSUE=Leaf, and Seedling;
RX   PubMed=7858230; DOI=10.1007/bf00019506;
RA   Henze K., Schnarrenberger C., Kellermann J., Martin W.;
RT   "Chloroplast and cytosolic triosephosphate isomerases from spinach:
RT   purification, microsequencing and cDNA cloning of the chloroplast enzyme.";
RL   Plant Mol. Biol. 26:1961-1973(1994).
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.
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; L36387; AAA66289.1; -; mRNA.
DR   PIR; S52032; S52032.
DR   AlphaFoldDB; P48496; -.
DR   SMR; P48496; -.
DR   OrthoDB; 6715177at2759; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000813463; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:TreeGrafter.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd00311; TIM; 1.
DR   FunFam; 3.20.20.70:FF:000025; Triosephosphate isomerase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR00419; tim; 1.
DR   PANTHER; PTHR21139; TRIOSEPHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR21139:SF2; TRIOSEPHOSPHATE ISOMERASE; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   1: Evidence at protein level;
KW   Calvin cycle; Chloroplast; Direct protein sequencing; Isomerase; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..67
FT                   /note="Chloroplast"
FT   CHAIN           68..322
FT                   /note="Triosephosphate isomerase, chloroplastic"
FT                   /id="PRO_0000035652"
FT   ACT_SITE        162
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        232
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   322 AA;  34409 MW;  CB47803C402DDDDE CRC64;
     MAVVSTSLAS QITNPNSAVS TQFSGLRRSF LKLENSVSTQ SSFFQNVDSH LRLSSSSRRC
     PRGVVAMAGS GKFFVGGNWK CNGTKESITK LVSDLNSATL EADVDVVVAP PFVYIDQVKS
     SLTGRVEISA QNCWIGKGGA FTGEISVEQL KDLGCQWVIL GHSERRHVIG EQNEFIGKKA
     AYALNQGVGV IACIGELLEE REAGKTFDVC YQQLKAFADA LPSWDNVVVA YEPVWAIGTG
     KVASPDQAQE VHVAVRDWLK KNVSEEVASK TRIIYGGSVN GGNCAELAKQ EDIDGFLVGG
     ASLKGPEFAT IVNSVTAKKV AA
//