TPIS_ARATH
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 03-AUG-2022, entry version 158.
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 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 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 [6]
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; AF375426; AAK53010.1; -; mRNA.
DR EMBL; AY074822; AAL69518.1; -; mRNA.
DR PIR; T47683; T47683.
DR PIR; T50646; T50646.
DR RefSeq; NP_191104.1; NM_115402.4.
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 PDBsum; 4OBT; -.
DR PDBsum; 6NXQ; -.
DR PDBsum; 6NXR; -.
DR PDBsum; 6NXS; -.
DR PDBsum; 6NXW; -.
DR PDBsum; 6NXX; -.
DR PDBsum; 6NXY; -.
DR AlphaFoldDB; P48491; -.
DR SMR; P48491; -.
DR BioGRID; 10026; 37.
DR IntAct; P48491; 26.
DR STRING; 3702.AT3G55440.1; -.
DR iPTMnet; P48491; -.
DR MetOSite; P48491; -.
DR SWISS-2DPAGE; P48491; -.
DR World-2DPAGE; 0003:P48491; -.
DR PaxDb; P48491; -.
DR PRIDE; P48491; -.
DR ProteomicsDB; 234445; -.
DR EnsemblPlants; AT3G55440.1; AT3G55440.1; AT3G55440.
DR GeneID; 824710; -.
DR Gramene; AT3G55440.1; AT3G55440.1; AT3G55440.
DR KEGG; ath:AT3G55440; -.
DR Araport; AT3G55440; -.
DR TAIR; locus:2099906; AT3G55440.
DR eggNOG; KOG1643; Eukaryota.
DR HOGENOM; CLU_024251_2_0_1; -.
DR InParanoid; P48491; -.
DR OMA; EWAEEEW; -.
DR OrthoDB; 1272577at2759; -.
DR PhylomeDB; P48491; -.
DR BioCyc; ARA:AT3G55440-MON; -.
DR BioCyc; MetaCyc:AT3G55440-MON; -.
DR BRENDA; 5.3.1.1; 399.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR PRO; PR:P48491; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P48491; baseline and differential.
DR Genevisible; P48491; AT.
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: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:0044262; P:cellular 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:0019563; P:glycerol catabolic 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 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; 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..120
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 TURN 168..172
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
