KITHB_ARATH
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 03-AUG-2022, entry version 72.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT 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 reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
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 [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., Munch-Petersen B.,
RA Piskur J.;
RT "Thymidine kinase 1 regulatory fine-tuning through tetramer formation.";
RL FEBS J. 280:1531-1541(2013).
CC -!- FUNCTION: Part of the salvage pathway for purine and pyrimidine
CC deoxyribonucleotide synthesis. Phosphorylates preferentially purines
CC over pyrimidines. {ECO:0000269|PubMed:22897443}.
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=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. kcat
CC is 0.02 sec(-1) with deoxythymidine (dT) as substrate. kcat is 0.009
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: Dimer. {ECO:0000269|PubMed:23351158}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04183}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09824.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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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 AlphaFoldDB; F4KBF5; -.
DR SMR; F4KBF5; -.
DR MINT; F4KBF5; -.
DR STRING; 3702.AT5G23070.1; -.
DR PaxDb; F4KBF5; -.
DR PRIDE; F4KBF5; -.
DR ProteomicsDB; 247212; -.
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 HOGENOM; CLU_064400_1_1_1; -.
DR InParanoid; F4KBF5; -.
DR OMA; ATHSKMT; -.
DR OrthoDB; 1413914at2759; -.
DR BioCyc; MetaCyc:AT5G23070-MON; -.
DR BRENDA; 2.7.1.21; 399.
DR PRO; PR:F4KBF5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KBF5; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0090351; P:seedling development; IMP:TAIR.
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 synthesis; Kinase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..282
FT /note="Thymidine kinase b"
FT /id="PRO_0000435652"
FT REGION 45..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 84..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 116..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04183"
FT BINDING 162..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04183"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 238..242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04183"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O57203"
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
