KITH_VACCW
ID KITH_VACCW Reviewed; 177 AA.
AC P68563; P03297; Q76ZT2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Thymidine kinase;
DE EC=2.7.1.21;
GN Name=TK; OrderedLocusNames=VACWR094; ORFNames=J2R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2987815; DOI=10.1093/nar/13.3.985;
RA Plucienniczak A., Schroeder E., Zettlmeissl G., Streeck R.E.;
RT "Nucleotide sequence of a cluster of early and late genes in a conserved
RT segment of the vaccinia virus genome.";
RL Nucleic Acids Res. 13:985-998(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6842679; DOI=10.1128/jvi.46.2.530-537.1983;
RA Weir J.P., Moss B.;
RT "Nucleotide sequence of the vaccinia virus thymidine kinase gene and the
RT nature of spontaneous frameshift mutations.";
RL J. Virol. 46:530-537(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6304709; DOI=10.1073/pnas.80.11.3411;
RA Hruby D.E., Maki R.A., Miller D.B., Ball L.A.;
RT "Fine structure analysis and nucleotide sequence of the vaccinia virus
RT thymidine kinase gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3411-3415(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17335913; DOI=10.1016/j.jviromet.2007.01.017;
RA Smith R.F., Freyer M.W., Lewis E.A.;
RT "Biophysical characterization of vaccinia virus thymidine kinase substrate
RT utilization.";
RL J. Virol. Methods 142:151-158(2007).
CC -!- FUNCTION: Phosphorylates thymidine and thymidine analogs, such as
CC azidothymidine (AZT). Part of the salvage pathway for pyrimidine
CC deoxyribonucleotide synthesis (By similarity). {ECO:0000250}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for 2'deoxythymidine {ECO:0000269|PubMed:17335913};
CC -!- SUBUNIT: Homotetramer (By similarity). Two molecules of substrate bind
CC to each enzyme tetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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DR EMBL; X01978; CAA26016.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89373.1; -; Genomic_DNA.
DR PIR; A00609; KIVZ.
DR RefSeq; YP_232976.1; NC_006998.1.
DR SMR; P68563; -.
DR MINT; P68563; -.
DR ChEMBL; CHEMBL1075034; -.
DR DNASU; 3707550; -.
DR GeneID; 3707550; -.
DR KEGG; vg:3707550; -.
DR SABIO-RK; P68563; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 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; DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..177
FT /note="Thymidine kinase"
FT /id="PRO_0000174940"
FT ACT_SITE 83
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 157..161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 177 AA; 20100 MW; 57E3595EBE6F3C54 CRC64;
MNGGHIQLII GPMFSGKSTE LIRRVRRYQI AQYKCVTIKY SNDNRYGTGL WTHDKNNFEA
LEATKLCDVL ESITDFSVIG IDEGQFFPDI VEFCERMANE GKIVIVAALD GTFQRKPFNN
ILNLIPLSEM VVKLTAVCMK CFKEASFSKR LGEETEIEII GGNDMYQSVC RKCYIDS