KITHA_ARATH
ID KITHA_ARATH Reviewed; 238 AA.
AC Q9S750; Q8LDP6;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Thymidine kinase a {ECO:0000303|PubMed:22897443};
DE Short=AtTK1a {ECO:0000303|PubMed:22897443};
DE EC=2.7.1.21 {ECO:0000269|PubMed:22897443, ECO:0000269|PubMed:23351158};
GN Name=TK1A {ECO:0000303|PubMed:22897443};
GN OrderedLocusNames=At3g07800 {ECO:0000312|Araport:AT3G07800};
GN ORFNames=F17A17.14 {ECO:0000312|EMBL:AAF21190.1},
GN MLP3.25 {ECO:0000312|EMBL:AAF13097.1};
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 FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=22897443; DOI=10.1111/j.1742-4658.2012.08747.x;
RA Clausen A.R., Girandon L., Ali A., Knecht W., Rozpedowska E.,
RA Sandrini M.P., Andreasson E., Munch-Petersen B., Piskur J.;
RT "Two thymidine kinases and one multisubstrate deoxyribonucleoside kinase
RT salvage DNA precursors in Arabidopsis thaliana.";
RL FEBS J. 279:3889-3897(2012).
RN [6]
RP SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=23351158; DOI=10.1111/febs.12154;
RA Mutahir Z., Clausen A.R., Andersson K.-M., Wisen S.M., Munch-Petersen B.,
RA Piskur J.;
RT "Thymidine kinase 1 regulatory fine-tuning through tetramer formation.";
RL FEBS J. 280:1531-1541(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION BY GENOTOXINS.
RC STRAIN=cv. Columbia;
RX PubMed=25537647; DOI=10.1007/s11103-014-0277-7;
RA Pedroza-Garcia J.A., Najera-Martinez M., de la Paz Sanchez M.,
RA Plasencia J.;
RT "Arabidopsis thaliana thymidine kinase 1a is ubiquitously expressed during
RT development and contributes to confer tolerance to genotoxic stress.";
RL Plant Mol. Biol. 87:303-315(2015).
CC -!- FUNCTION: Part of the salvage pathway for purine and pyrimidine
CC deoxyribonucleotide synthesis. Phosphorylates preferentially purines
CC over pyrimidines (PubMed:22897443). Mediates tolerance to genotoxins,
CC such as ultraviolet-C (UV-C) irradiation, MMC, a DNA crosslinker, and
CC ZEO, a DNA intercalator, that induce double-strand breaks and thus
CC contributes to several DNA repair pathways by providing deoxythymidine
CC triphosphate that serve as precursors for DNA repair and to balance
CC deoxyribonucleotides pools (PubMed:25537647).
CC {ECO:0000269|PubMed:22897443, ECO:0000269|PubMed:25537647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC Evidence={ECO:0000269|PubMed:22897443, ECO:0000269|PubMed:23351158};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for deoxyuridine {ECO:0000269|PubMed:22897443};
CC KM=0.48 uM for deoxythymidine {ECO:0000269|PubMed:22897443};
CC KM=2.7 uM for AZT {ECO:0000269|PubMed:22897443};
CC KM=0.6 uM for thymidine (in the absence of ATP)
CC {ECO:0000269|PubMed:23351158};
CC KM=0.7 uM for thymidine (in the presence of ATP)
CC {ECO:0000269|PubMed:23351158};
CC Vmax=0.5 umol/min/mg enzyme with thymidine as substrate (in the
CC absence of ATP) {ECO:0000269|PubMed:23351158};
CC Vmax=1 umol/min/mg enzyme with thymidine as substrate (in the
CC presence of ATP) {ECO:0000269|PubMed:23351158};
CC Note=kcat is 1.5 sec(-1) with deoxyuridine (dU) as substrate. kcat is
CC 0.48 sec(-1) with deoxythymidine (dT) as substrate. kcat is 0.13
CC sec(-1) with 3'-azido-3'-deoxythymidine (AZT) as substrate.
CC {ECO:0000269|PubMed:22897443};
CC -!- PATHWAY: Purine metabolism. {ECO:0000269|PubMed:22897443}.
CC -!- PATHWAY: Pyrimidine metabolism. {ECO:0000269|PubMed:22897443,
CC ECO:0000269|PubMed:23351158}.
CC -!- SUBUNIT: Monomer and dimer. Dimerization is stimulated by ATP.
CC {ECO:0000269|PubMed:23351158}.
CC -!- INTERACTION:
CC Q9S750; Q9S750: TK1A; NbExp=2; IntAct=EBI-4455798, EBI-4455798;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04183}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:25537647}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed at the early stages of
CC germination upon testa rupture and throughout seedling development.
CC Accumulates in the cotyledons and foliar primordia. In seedlings,
CC highly present in almost every organ except the root meristem and
CC secondary root primordia. In young leaves, detected in the trichomes.
CC In mature leaves, present in the vasculature as well as in the pedicel
CC and base. In flowers organs, mostly expressed in stigma, petals,
CC anthers and pollen. In developing siliques, restricted to pedicels and
CC septum. {ECO:0000269|PubMed:25537647}.
CC -!- INDUCTION: Induced by genotoxins such as ultraviolet-C radiation (UV-
CC C), and ZEO and MMC treatments. {ECO:0000269|PubMed:25537647}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. The double mutant tk1a tk1b
CC is seedling lethal. {ECO:0000269|PubMed:22897443}.
CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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DR EMBL; AC009176; AAF13097.1; -; Genomic_DNA.
DR EMBL; AC013483; AAF21190.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74605.1; -; Genomic_DNA.
DR EMBL; AF370344; AAK44159.1; -; mRNA.
DR EMBL; AY142670; AAN13208.1; -; mRNA.
DR EMBL; AY085873; AAM63086.1; -; mRNA.
DR RefSeq; NP_187437.1; NM_111659.4.
DR AlphaFoldDB; Q9S750; -.
DR SMR; Q9S750; -.
DR IntAct; Q9S750; 1.
DR MINT; Q9S750; -.
DR STRING; 3702.AT3G07800.1; -.
DR PaxDb; Q9S750; -.
DR PRIDE; Q9S750; -.
DR ProteomicsDB; 230183; -.
DR EnsemblPlants; AT3G07800.1; AT3G07800.1; AT3G07800.
DR GeneID; 819971; -.
DR Gramene; AT3G07800.1; AT3G07800.1; AT3G07800.
DR KEGG; ath:AT3G07800; -.
DR Araport; AT3G07800; -.
DR TAIR; locus:2077382; AT3G07800.
DR eggNOG; KOG3125; Eukaryota.
DR HOGENOM; CLU_064400_1_1_1; -.
DR InParanoid; Q9S750; -.
DR OMA; KARAETC; -.
DR OrthoDB; 1413914at2759; -.
DR PhylomeDB; Q9S750; -.
DR BioCyc; ARA:AT3G07800-MON; -.
DR BioCyc; MetaCyc:AT3G07800-MON; -.
DR BRENDA; 2.7.1.21; 399.
DR PRO; PR:Q9S750; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S750; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004797; F:thymidine kinase activity; IDA:UniProtKB.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010225; P:response to UV-C; IMP:UniProtKB.
DR GO; GO:0046104; P:thymidine metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR InterPro; IPR020633; Thymidine_kinase_CS.
DR PANTHER; PTHR11441; PTHR11441; 1.
DR Pfam; PF00265; TK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA synthesis; Kinase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..238
FT /note="Thymidine kinase a"
FT /id="PRO_0000435651"
FT ACT_SITE 116
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 70..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04183"
FT BINDING 115..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04183"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 191..195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04183"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT CONFLICT 15
FT /note="S -> N (in Ref. 4; AAM63086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 26079 MW; D27E84291427A62C CRC64;
MATLKASFLI KTLDSDVTGD FLSDLERRGS GAVHVIMGPM FSGKSTSLLR RIKSEISDGR
SVAMLKSSKD TRYAKDSVVT HDGIGFPCWA LPDLMSFPEK FGLDAYNKLD VIGIDEAQFF
GDLYEFCCKV ADDDGKIVIV AGLDGDYLRR SFGAVLDIIP IADSVTKLTA RCEVCGHKAF
FTLRKNCDTR TELIGGADVY MPVCRKHYIT NHIVIKASKK VLEDSDKARA ESCVAATI
