TPIC_SPIOL
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 03-AUG-2022, entry version 91.
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; Chenopodiaceae; 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; 1272577at2759; -.
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 1: Evidence at protein level;
KW Calvin cycle; Chloroplast; Direct protein sequencing; Isomerase; Plastid;
KW 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
