TPIC_ARATH
ID TPIC_ARATH Reviewed; 315 AA.
AC Q9SKP6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
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=TIM; OrderedLocusNames=At2g21170; ORFNames=F26H11.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Shih M.-C.;
RT "Structure and regulation of nuclear genes encoding chloroplast and
RT cytosolic triosephosphate isomerase in Arabidopsis thaliana.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SKP6-1; Sequence=Displayed;
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; AC006264; AAD29799.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07131.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61768.1; -; Genomic_DNA.
DR EMBL; AF247559; AAF70259.1; -; mRNA.
DR EMBL; AF378898; AAK55701.1; -; mRNA.
DR EMBL; AY052748; AAK96462.1; -; mRNA.
DR EMBL; AY087893; AAM65444.1; -; mRNA.
DR PIR; A84598; A84598.
DR RefSeq; NP_001323967.1; NM_001335732.1. [Q9SKP6-1]
DR RefSeq; NP_179713.1; NM_127687.4. [Q9SKP6-1]
DR PDB; 4OHQ; X-ray; 2.15 A; A/B=60-315.
DR PDBsum; 4OHQ; -.
DR AlphaFoldDB; Q9SKP6; -.
DR SMR; Q9SKP6; -.
DR BioGRID; 2005; 20.
DR IntAct; Q9SKP6; 1.
DR STRING; 3702.AT2G21170.1; -.
DR iPTMnet; Q9SKP6; -.
DR World-2DPAGE; 0003:Q9SKP6; -.
DR PaxDb; Q9SKP6; -.
DR PRIDE; Q9SKP6; -.
DR ProteomicsDB; 232434; -. [Q9SKP6-1]
DR EnsemblPlants; AT2G21170.1; AT2G21170.1; AT2G21170. [Q9SKP6-1]
DR EnsemblPlants; AT2G21170.3; AT2G21170.3; AT2G21170. [Q9SKP6-1]
DR GeneID; 816652; -.
DR Gramene; AT2G21170.1; AT2G21170.1; AT2G21170. [Q9SKP6-1]
DR Gramene; AT2G21170.3; AT2G21170.3; AT2G21170. [Q9SKP6-1]
DR KEGG; ath:AT2G21170; -.
DR Araport; AT2G21170; -.
DR TAIR; locus:2047072; AT2G21170.
DR eggNOG; KOG1643; Eukaryota.
DR HOGENOM; CLU_024251_2_0_1; -.
DR InParanoid; Q9SKP6; -.
DR OMA; QVIACIG; -.
DR PhylomeDB; Q9SKP6; -.
DR BioCyc; ARA:AT2G21170-MON; -.
DR UniPathway; UPA00116; -.
DR PRO; PR:Q9SKP6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKP6; baseline and differential.
DR Genevisible; Q9SKP6; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IDA:TAIR.
DR GO; GO:0019563; P:glycerol catabolic process; IMP:TAIR.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0032504; P:multicellular organism reproduction; IMP:TAIR.
DR GO; GO:0080022; P:primary root development; IMP:TAIR.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0006642; P:triglyceride mobilization; IMP:TAIR.
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 3D-structure; Alternative splicing; Calvin cycle; Chloroplast; Isomerase;
KW Phosphoprotein; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 61..315
FT /note="Triosephosphate isomerase, chloroplastic"
FT /id="PRO_0000035649"
FT ACT_SITE 155
FT /note="Electrophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 225
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:4OHQ"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:4OHQ"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:4OHQ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:4OHQ"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:4OHQ"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:4OHQ"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:4OHQ"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:4OHQ"
FT TURN 227..232
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 238..255
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:4OHQ"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:4OHQ"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:4OHQ"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:4OHQ"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:4OHQ"
SQ SEQUENCE 315 AA; 33346 MW; BD580F9B37FA0269 CRC64;
MAATSLTAPP SFSGLRRISP KLDAAAVSSH QSFFHRVNSS TRLVSSSSSS HRSPRGVVAM
AGSGKFFVGG NWKCNGTKDS IAKLISDLNS ATLEADVDVV VSPPFVYIDQ VKSSLTDRID
ISGQNSWVGK GGAFTGEISV EQLKDLGCKW VILGHSERRH VIGEKDEFIG KKAAYALSEG
LGVIACIGEK LEEREAGKTF DVCFAQLKAF ADAVPSWDNI VVAYEPVWAI GTGKVASPQQ
AQEVHVAVRG WLKKNVSEEV ASKTRIIYGG SVNGGNSAEL AKEEDIDGFL VGGASLKGPE
FATIVNSVTS KKVAA
