ID   TPIS_ARATH              Reviewed;         254 AA.
AC   P48491; Q9M2T5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   04-NOV-2026, entry version 176.
DE   RecName: Full=Triosephosphate isomerase, cytosolic;
DE            Short=TIM;
DE            Short=Triose-phosphate isomerase;
DE            EC=5.3.1.1;
GN   Name=CTIMC; OrderedLocusNames=At3g55440; ORFNames=T22E16.100;
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.
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RA   Shih M.-C.;
RT   "Structure and regulation of nuclear genes encoding chloroplast and
RT   cytosolic triosephosphate isomerase in Arabidopsis thaliana.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=12953116; DOI=10.1105/tpc.012500;
RA   Giege P., Heazlewood J.L., Roessner-Tunali U., Millar A.H., Fernie A.R.,
RA   Leaver C.J., Sweetlove L.J.;
RT   "Enzymes of glycolysis are functionally associated with the mitochondrion
RT   in Arabidopsis cells.";
RL   Plant Cell 15:2140-2151(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131 AND SER-139, AND
RP   IDENTIFICATION BY 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; 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}. Mitochondrion
CC       {ECO:0000269|PubMed:12953116}.
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; U02949; AAA03449.1; -; mRNA.
DR   EMBL; AL132975; CAB75902.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79384.1; -; Genomic_DNA.
DR   EMBL; OZ408685; CAO7044544.1; -; Genomic_DNA.
DR   EMBL; AF375426; AAK53010.1; -; mRNA.
DR   EMBL; AY074822; AAL69518.1; -; mRNA.
DR   PIR; T47683; T47683.
DR   PIR; T50646; T50646.
DR   PDB; 4OBT; X-ray; 1.60 A; A/B=1-254.
DR   PDB; 6NXQ; X-ray; 1.96 A; A=1-254.
DR   PDB; 6NXR; X-ray; 1.30 A; A=1-254.
DR   PDB; 6NXS; X-ray; 1.52 A; A/B=1-254.
DR   PDB; 6NXW; X-ray; 1.95 A; A/B/C/D=1-254.
DR   PDB; 6NXX; X-ray; 1.64 A; A/B=1-254.
DR   PDB; 6NXY; X-ray; 1.05 A; A=1-254.
DR   SMR; P48491; -.
DR   BioGRID; 10026; 37.
DR   IntAct; P48491; 31.
DR   STRING; 3702.P48491; -.
DR   iPTMnet; P48491; -.
DR   MetOSite; P48491; -.
DR   PaxDb; 3702-P48491; -.
DR   ProteomicsDB; 234445; -.
DR   KEGG; ath:AT3G55440; -.
DR   Araport; AT3G55440; -.
DR   TAIR; AT3G55440; TPI.
DR   eggNOG; KOG1643; Eukaryota.
DR   HOGENOM; CLU_024251_2_0_1; -.
DR   InParanoid; P48491; -.
DR   OMA; ADNVRDW; -.
DR   OrthoDB; 6715177at2759; -.
DR   PhylomeDB; P48491; -.
DR   BioCyc; ARA:AT3G55440-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G55440-MONOMER; -.
DR   BRENDA; 5.3.1.1; 399.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   EvolutionaryTrace; P48491; -.
DR   PRO; PR:P48491; -.
DR   ExpressionAtlas; P48491; baseline and differential.
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   PANTHER; PTHR21139; TRIOSEPHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR21139:SF34; TRIOSEPHOSPHATE ISOMERASE, CYTOSOLIC; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1.
DR   NCBIfam; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; ISM:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:TAIR.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IDA:TAIR.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR   Proteomes; UP000006548; Chromosome 3.
DR   Proteomes; UP001984100; Chromosome 3.
DR   AlphaFoldDB; P48491; -.
DR   CD-CODE; 4299E36E; Nucleolus.
DR   FunCoup; P48491; 2616.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW   Mitochondrion; Phosphoprotein; Reference proteome.
FT   CHAIN           1..254
FT                   /note="Triosephosphate isomerase, cytosolic"
FT                   /id="PRO_0000090144"
FT   ACT_SITE        96
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         131
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22092075"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22092075"
FT   CONFLICT        251
FT                   /note="K -> N (in Ref. 1; AAA03449)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           17..29
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           49..55
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   STRAND          60..65
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:6NXX"
FT   HELIX           81..86
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   STRAND          91..95
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           97..101
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           107..119
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   STRAND          123..128
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           132..136
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           140..152
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:6NXW"
FT   STRAND          161..165
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           168..170
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   STRAND          171..174
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           179..196
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           199..204
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   TURN            215..217
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           218..222
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   STRAND          229..232
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           234..237
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           240..246
FT                   /evidence="ECO:0007829|PDB:6NXY"
FT   HELIX           247..250
FT                   /evidence="ECO:0007829|PDB:4OBT"
SQ   SEQUENCE   254 AA;  27169 MW;  428023AFEB3269B4 CRC64;
     MARKFFVGGN WKCNGTAEEV KKIVNTLNEA QVPSQDVVEV VVSPPYVFLP LVKSTLRSDF
     FVAAQNCWVK KGGAFTGEVS AEMLVNLDIP WVILGHSERR AILNESSEFV GDKVAYALAQ
     GLKVIACVGE TLEEREAGST MDVVAAQTKA IADRVTNWSN VVIAYEPVWA IGTGKVASPA
     QAQEVHDELR KWLAKNVSAD VAATTRIIYG GSVNGGNCKE LGGQADVDGF LVGGASLKPE
     FIDIIKAAEV KKSA
//