GenomeNet

Database: UniProt/SWISS-PROT
Entry: KITHA_ARATH
LinkDB: KITHA_ARATH
Original site: 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   25-APR-2018, entry version 131.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RP   BIOPHYSICOCHEMICAL 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
RT   kinase 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.,
RA   Munch-Petersen B., Piskur J.;
RT   "Thymidine kinase 1 regulatory fine-tuning through tetramer
RT   formation.";
RL   FEBS J. 280:1531-1541(2013).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, 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
RT   during development and contributes to confer tolerance to genotoxic
RT   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
CC       purines over pyrimidines (PubMed:22897443). Mediates tolerance to
CC       genotoxins, such as ultraviolet-C (UV-C) irradiation, MMC, a DNA
CC       crosslinker, and ZEO, a DNA intercalator, that induce double-
CC       strand breaks and thus contributes to several DNA repair pathways
CC       by providing deoxythymidine triphosphate that serve as precursors
CC       for DNA repair and to balance deoxyribonucleotides pools
CC       (PubMed:25537647). {ECO:0000269|PubMed:22897443,
CC       ECO:0000269|PubMed:25537647}.
CC   -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC       phosphate. {ECO:0000269|PubMed:22897443,
CC       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.
CC         kcat is 0.48 sec(-1) with deoxythymidine (dT) as substrate. kcat
CC         is 0.13 sec(-1) with 3'-azido-3'-deoxythymidine (AZT) as
CC         substrate. {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       Self; 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
CC       development. Accumulates in the cotyledons and foliar primordia.
CC       In seedlings, highly present in almost every organ except the root
CC       meristem and secondary root primordia. In young leaves, detected
CC       in the trichomes. In mature leaves, present in the vasculature as
CC       well as in the pedicel and base. In flowers organs, mostly
CC       expressed in stigma, petals, anthers and pollen. In developing
CC       siliques, restricted to pedicels and septum.
CC       {ECO:0000269|PubMed:25537647}.
CC   -!- INDUCTION: Induced by genotoxins such as ultraviolet-C radiation
CC       (UV-C), and ZEO and MMC treatments. {ECO:0000269|PubMed:25537647}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. The double mutant tk1a
CC       tk1b is seedling lethal. {ECO:0000269|PubMed:22897443}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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   UniGene; At.18348; -.
DR   ProteinModelPortal; Q9S750; -.
DR   SMR; Q9S750; -.
DR   IntAct; Q9S750; 1.
DR   MINT; Q9S750; -.
DR   STRING; 3702.AT3G07800.1; -.
DR   PaxDb; Q9S750; -.
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   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; CKAADDD; -.
DR   OrthoDB; EOG09360L6B; -.
DR   PhylomeDB; Q9S750; -.
DR   BioCyc; ARA:AT3G07800-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G07800-MONOMER; -.
DR   BRENDA; 2.7.1.21; 399.
DR   Reactome; R-ATH-73614; Pyrimidine salvage.
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:0010225; P:response to UV-C; IMP:UniProtKB.
DR   GO; GO:0046104; P:thymidine metabolic process; IBA:GO_Central.
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   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA repair;
KW   DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN         1    238       Thymidine kinase a.
FT                                /FTId=PRO_0000435651.
FT   NP_BIND      38     45       ATP. {ECO:0000250|UniProtKB:O57203}.
FT   NP_BIND      70     72       ATP. {ECO:0000250|UniProtKB:P04183}.
FT   NP_BIND     115    118       ATP. {ECO:0000250|UniProtKB:P04183}.
FT   REGION      191    195       Substrate binding.
FT                                {ECO:0000250|UniProtKB:O57203}.
FT   ACT_SITE    116    116       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:O57203}.
FT   METAL       172    172       Zinc. {ECO:0000250|UniProtKB:O57203}.
FT   METAL       175    175       Zinc. {ECO:0000250|UniProtKB:O57203}.
FT   METAL       204    204       Zinc. {ECO:0000250|UniProtKB:O57203}.
FT   BINDING     147    147       Substrate.
FT                                {ECO:0000250|UniProtKB:O57203}.
FT   BINDING     200    200       Substrate.
FT                                {ECO:0000250|UniProtKB:P04183}.
FT   CONFLICT     15     15       S -> N (in Ref. 4; AAM63086).
FT                                {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
//
DBGET integrated database retrieval system