TKTC2_ARATH
ID TKTC2_ARATH Reviewed; 741 AA.
AC F4IW47; O22143; Q93ZH6;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Transketolase-2, chloroplastic;
DE Short=TK;
DE EC=2.2.1.1;
DE Flags: Precursor;
GN Name=TKL-2; OrderedLocusNames=At2g45290; ORFNames=F4L23.20;
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=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 [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] OF 54-741.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-66, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ARG-65, 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 thylakoid membrane. Plastid,
CC chloroplast stroma {ECO:0000269|PubMed:18431481}.
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=AAB82634.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL09768.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC002387; AAB82634.2; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC10535.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62077.1; -; Genomic_DNA.
DR EMBL; AY057528; AAL09768.1; ALT_INIT; mRNA.
DR PIR; G84888; G84888.
DR RefSeq; NP_001324258.1; NM_001337121.1.
DR RefSeq; NP_566041.2; NM_130092.3.
DR AlphaFoldDB; F4IW47; -.
DR SMR; F4IW47; -.
DR BioGRID; 4473; 7.
DR STRING; 3702.AT2G45290.1; -.
DR iPTMnet; F4IW47; -.
DR PaxDb; F4IW47; -.
DR PRIDE; F4IW47; -.
DR ProteomicsDB; 232457; -.
DR EnsemblPlants; AT2G45290.1; AT2G45290.1; AT2G45290.
DR EnsemblPlants; AT2G45290.2; AT2G45290.2; AT2G45290.
DR GeneID; 819137; -.
DR Gramene; AT2G45290.1; AT2G45290.1; AT2G45290.
DR Gramene; AT2G45290.2; AT2G45290.2; AT2G45290.
DR KEGG; ath:AT2G45290; -.
DR Araport; AT2G45290; -.
DR TAIR; locus:2050837; AT2G45290.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_0_0_1; -.
DR InParanoid; F4IW47; -.
DR OMA; EYRWTSG; -.
DR OrthoDB; 354970at2759; -.
DR BioCyc; ARA:AT2G45290-MON; -.
DR UniPathway; UPA00116; -.
DR PRO; PR:F4IW47; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IW47; baseline and differential.
DR Genevisible; F4IW47; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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: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; Calcium; Chloroplast; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Plastid; Reference proteome; Thiamine pyrophosphate;
KW Thylakoid; Transferase; Transit peptide.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 66..741
FT /note="Transketolase-2, chloroplastic"
FT /id="PRO_0000421818"
FT REGION 171..190
FT /note="Disordered"
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 66
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8RWV0"
SQ SEQUENCE 741 AA; 79922 MW; C712DFDE2C7D63C6 CRC64;
MASTSSLALS QALLTRAISH NGSENCVSIP AFSALKSTSP RTSGTISSRR RNASTISHSL
RPLVRAAAVE AIVTSSDSSL VDKSVNTIRF LAIDAVEKAK SGHPGLPMGC APMSHILYDE
VMKYNPKNPY WFNRDRFVLS AGHGCMLQYA LLHLAGYDSV REEDLKSFRQ WGSKTPGHPE
NFETPGVEAT TGPLGQGIAN AVGLALAEKH LAARFNKPDN EIVDHYTYSI LGDGCQMEGI
SNEVCSLAGH WGLGKLIAFY DDNHISIDGD TDIAFTESVD KRFEALGWHV IWVKNGNNGY
DEIRAAIREA KAVTDKPTLI KVTTTIGYGS PNKANSYSVH GAALGEKEVE ATRNNLGWPY
EPFHVPEDVK SHWSRHTPEG AALEADWNAK FAAYEKKYPE EAAELKSIIS GELPVGWEKA
LPTYTPDSPG DATRNLSQQC LNALAKAVPG FLGGSADLAS SNMTMLKAFG NFQKATPEER
NLRFGVREHG MGAICNGIAL HSPGFIPYCA TFFVFTDYMR AAMRISALSE AGVIYVMTHD
SIGLGEDGPT HQPIEHLSSF RAMPNIMMFR PADGNETAGA YKIAVTKRKT PSVLALSRQK
LPQLPGTSIE SVEKGGYTIS DNSTGNKPDV ILIGTGSELE IAAQAAEKLR EQGKSVRVVS
FVCWELFDEQ SDAYKESVLP SDVSARVSIE AGSTFGWGKI VGGKGKSIGI DTFGASAPAG
KLYKEFGITI EAMVEAAKSL I
