TKTC1_ARATH
ID TKTC1_ARATH Reviewed; 741 AA.
AC Q8RWV0; B9DGH8; Q84WI5; Q8LE99; Q944P9; Q9LZY8;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Transketolase-1, chloroplastic;
DE Short=TK;
DE EC=2.2.1.1;
DE Flags: Precursor;
GN Name=TKL-1; OrderedLocusNames=At3g60750; ORFNames=T4C21_160;
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 172-741.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP INDUCTION, AND FUNCTION.
RX PubMed=22214485; DOI=10.1186/1471-2229-12-2;
RA Rapala-Kozik M., Wolak N., Kujda M., Banas A.K.;
RT "The upregulation of thiamine (vitamin B1) biosynthesis in Arabidopsis
RT thaliana seedlings under salt and osmotic stress conditions is mediated by
RT abscisic acid at the early stages of this stress response.";
RL BMC Plant Biol. 12:2-2(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-67, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-66, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the reversible transfer of a two-carbon ketol group
CC from fructose-6-phosphate or sedoheptulose-7-phosphate to
CC glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-
CC 4-phosphate or ribose-5-phosphate, respectively (By similarity). Could
CC act as a stress sensor involved in adaptation process. {ECO:0000250,
CC ECO:0000269|PubMed:22214485}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481}.
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=Q8RWV0-1; Sequence=Displayed;
CC -!- INDUCTION: Up-regulated by salt, sorbitol, and abscisic acid (ABA).
CC {ECO:0000269|PubMed:22214485}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL11624.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAN18173.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB82679.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162295; CAB82679.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80103.1; -; Genomic_DNA.
DR EMBL; AF424631; AAL11624.1; ALT_FRAME; mRNA.
DR EMBL; AY091094; AAM14045.1; -; mRNA.
DR EMBL; AY133860; AAM91794.1; -; mRNA.
DR EMBL; BT000604; AAN18173.1; ALT_FRAME; mRNA.
DR EMBL; BT003331; AAO29950.1; -; mRNA.
DR EMBL; AY085542; AAM62766.1; -; mRNA.
DR EMBL; AK317159; BAH19845.1; -; mRNA.
DR PIR; T47886; T47886.
DR RefSeq; NP_567103.1; NM_115939.3. [Q8RWV0-1]
DR AlphaFoldDB; Q8RWV0; -.
DR SMR; Q8RWV0; -.
DR BioGRID; 10560; 8.
DR IntAct; Q8RWV0; 3.
DR MINT; Q8RWV0; -.
DR STRING; 3702.AT3G60750.1; -.
DR iPTMnet; Q8RWV0; -.
DR PaxDb; Q8RWV0; -.
DR PRIDE; Q8RWV0; -.
DR ProMEX; Q8RWV0; -.
DR ProteomicsDB; 234316; -. [Q8RWV0-1]
DR EnsemblPlants; AT3G60750.1; AT3G60750.1; AT3G60750. [Q8RWV0-1]
DR GeneID; 825246; -.
DR Gramene; AT3G60750.1; AT3G60750.1; AT3G60750. [Q8RWV0-1]
DR KEGG; ath:AT3G60750; -.
DR Araport; AT3G60750; -.
DR TAIR; locus:2101871; AT3G60750.
DR eggNOG; KOG0523; Eukaryota.
DR InParanoid; Q8RWV0; -.
DR PhylomeDB; Q8RWV0; -.
DR BioCyc; ARA:AT3G60750-MON; -.
DR UniPathway; UPA00116; -.
DR PRO; PR:Q8RWV0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RWV0; baseline and differential.
DR Genevisible; Q8RWV0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Chloroplast; Magnesium;
KW Metal-binding; Phosphoprotein; Plastid; Reference proteome;
KW Thiamine pyrophosphate; Transferase; Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 67..741
FT /note="Transketolase-1, chloroplastic"
FT /id="PRO_0000421817"
FT REGION 22..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 192..194
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 598
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 103
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 340
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 282
FT /note="R -> L (in Ref. 4; AAM62766)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="L -> V (in Ref. 3; AAO29950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 79968 MW; 5886543FBA70E79C CRC64;
MASTSSLALS QALLARAISH HGSDQRGSLP AFSGLKSTGS RASASSRRRI AQSMTKNRSL
RPLVRAAAVE TVEPTTDSSI VDKSVNSIRF LAIDAVEKAK SGHPGLPMGC APMAHILYDE
VMRYNPKNPY WFNRDRFVLS AGHGCMLLYA LLHLAGYDSV QEEDLKQFRQ WGSKTPGHPE
NFETPGIEVT TGPLGQGIAN AVGLALAEKH LAARFNKPDA EVVDHYTYAI LGDGCQMEGI
SNEACSLAGH WGLGKLIAFY DDNHISIDGD TEIAFTENVD QRFEALGWHV IWVKNGNTGY
DEIRAAIKEA KTVTDKPTLI KVTTTIGYGS PNKANSYSVH GAALGEKEVE ATRNNLGWPY
EPFQVPDDVK SHWSRHTPEG ATLESDWSAK FAAYEKKYPE EASELKSIIT GELPAGWEKA
LPTYTPESPG DATRNLSQQC LNALAKVVPG FLGGSADLAS SNMTLLKAFG DFQKATPEER
NLRFGVREHG MGAICNGIAL HSPGLIPYCA TFFVFTDYMR GAMRISALSE AGVIYVMTHD
SIGLGEDGPT HQPIEHIASF RAMPNTLMFR PADGNETAGA YKIAVTKRKT PSILALSRQK
LPHLPGTSIE GVEKGGYTIS DDSSGNKPDV ILIGTGSELE IAAQAAEVLR KDGKTVRVVS
FVCWELFDEQ SDEYKESVLP SDVSARVSIE AASTFGWGKI VGGKGKSIGI NSFGASAPAP
LLYKEFGITV EAVVDAAKSF F
