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Database: UniProt
Entry: F4KBF5
LinkDB: F4KBF5
Original site: F4KBF5 
ID   KITHB_ARATH             Reviewed;         282 AA.
AC   F4KBF5; Q9FN47;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   16-JAN-2019, entry version 55.
DE   RecName: Full=Thymidine kinase b {ECO:0000303|PubMed:22897443};
DE            Short=AtTK1b {ECO:0000305};
DE            EC=2.7.1.21 {ECO:0000269|PubMed:22897443, ECO:0000269|PubMed:23351158};
GN   Name=TK1B {ECO:0000303|PubMed:22897443};
GN   OrderedLocusNames=At5g23070 {ECO:0000312|Araport:AT5G23070};
GN   ORFNames=MYJ24.6 {ECO:0000312|EMBL:BAB09824.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II.
RT   Sequence features of the regions of 1,044,062 bp covered by thirteen
RT   physically assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
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   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   [4]
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).
CC   -!- FUNCTION: Part of the salvage pathway for purine and pyrimidine
CC       deoxyribonucleotide synthesis. Phosphorylates preferentially
CC       purines over pyrimidines. {ECO:0000269|PubMed:22897443}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         EC=2.7.1.21; Evidence={ECO:0000269|PubMed:22897443,
CC         ECO:0000269|PubMed:23351158};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.6 uM for deoxyuridine {ECO:0000269|PubMed:22897443};
CC         KM=1.4 uM for deoxythymidine {ECO:0000269|PubMed:22897443};
CC         KM=0.38 uM for AZT {ECO:0000269|PubMed:22897443};
CC         KM=0.9 uM for thymidine (in the absence of ATP)
CC         {ECO:0000269|PubMed:23351158};
CC         KM=0.9 uM for thymidine (in the presence of ATP)
CC         {ECO:0000269|PubMed:23351158};
CC         Vmax=0.7 umol/min/mg enzyme with thymidine as substrate (in the
CC         absence of ATP) {ECO:0000269|PubMed:23351158};
CC         Vmax=0.8 umol/min/mg enzyme with thymidine as substrate (in the
CC         presence of ATP) {ECO:0000269|PubMed:23351158};
CC         Note=kcat is 0.045 sec(-1) with deoxyuridine (dU) as substrate.
CC         kcat is 0.02 sec(-1) with deoxythymidine (dT) as substrate. kcat
CC         is 0.009 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: Dimer. {ECO:0000269|PubMed:23351158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04183}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09824.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AB006708; BAB09824.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002688; AED93115.1; -; Genomic_DNA.
DR   RefSeq; NP_568426.1; NM_122213.4.
DR   UniGene; At.49050; -.
DR   UniGene; At.71128; -.
DR   ProteinModelPortal; F4KBF5; -.
DR   SMR; F4KBF5; -.
DR   MINT; F4KBF5; -.
DR   STRING; 3702.AT5G23070.1; -.
DR   PaxDb; F4KBF5; -.
DR   EnsemblPlants; AT5G23070.1; AT5G23070.1; AT5G23070.
DR   GeneID; 832371; -.
DR   Gramene; AT5G23070.1; AT5G23070.1; AT5G23070.
DR   KEGG; ath:AT5G23070; -.
DR   Araport; AT5G23070; -.
DR   TAIR; locus:2178297; AT5G23070.
DR   eggNOG; KOG3125; Eukaryota.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   InParanoid; F4KBF5; -.
DR   KO; K00857; -.
DR   OMA; FTMRKTE; -.
DR   OrthoDB; 1413914at2759; -.
DR   BioCyc; MetaCyc:AT5G23070-MONOMER; -.
DR   BRENDA; 2.7.1.21; 399.
DR   Reactome; R-ATH-73614; Pyrimidine salvage.
DR   PRO; PR:F4KBF5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4KBF5; 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:UniProtKB.
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:0006259; P:DNA metabolic process; IBA:GO_Central.
DR   GO; GO:0009409; P:response to cold; IMP:TAIR.
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   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; Kinase;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    282       Thymidine kinase b.
FT                                /FTId=PRO_0000435652.
FT   NP_BIND      84     91       ATP. {ECO:0000250|UniProtKB:O57203}.
FT   NP_BIND     116    118       ATP. {ECO:0000250|UniProtKB:P04183}.
FT   NP_BIND     162    165       ATP. {ECO:0000250|UniProtKB:P04183}.
FT   REGION      238    242       Substrate binding.
FT                                {ECO:0000250|UniProtKB:O57203}.
FT   ACT_SITE    163    163       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:O57203}.
FT   METAL       219    219       Zinc. {ECO:0000250|UniProtKB:O57203}.
FT   METAL       222    222       Zinc. {ECO:0000250|UniProtKB:O57203}.
FT   METAL       251    251       Zinc. {ECO:0000250|UniProtKB:O57203}.
FT   BINDING     194    194       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:O57203}.
FT   BINDING     247    247       Substrate.
FT                                {ECO:0000250|UniProtKB:P04183}.
SQ   SEQUENCE   282 AA;  31226 MW;  FCEB4FC1AF5FC695 CRC64;
     MFGVSMRTLI SPSLAPFSLH LHKPSLFSTA LRFSFSINNI TPTNSPPSTI STRKLQTKAT
     RVTSSSSSQP LSSSSPGEIH VVVGPMFSGK TTTLLRRILA ERETGKRIAI IKSNKDTRYC
     TESIVTHDGE KYPCWSLPDL SSFKERFGFD DYENRLDVIG IDEAQFFGDL YEFCREAADK
     EGKTVIVAGL DGDFMRRRFG SVLDLIPIAD TVTKLTSRCE VCGKRALFTM RKTEEKETEL
     IGGAEVYMPV CRSHYVCGQN VLETARAVLD SSNNHSVVAS SL
//
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