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Database: UniProt
Entry: P68563
LinkDB: P68563
Original site: P68563 
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   16-JAN-2019, entry version 61.
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; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   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
RT   conserved segment of the vaccinia virus genome.";
RL   Nucleic Acids Res. 13:985-998(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6842679;
RA   Weir J.P., Moss B.;
RT   "Nucleotide sequence of the vaccinia virus thymidine kinase gene and
RT   the 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.,
RA   Osborne J., 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
RT   substrate 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(+);
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;
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
CC       bind to each enzyme tetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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   ProteinModelPortal; P68563; -.
DR   MINT; P68563; -.
DR   ChEMBL; CHEMBL1075034; -.
DR   GeneID; 3707550; -.
DR   KEGG; vg:3707550; -.
DR   KO; K00857; -.
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   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; DNA synthesis; Kinase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN         1    177       Thymidine kinase.
FT                                /FTId=PRO_0000174940.
FT   NP_BIND      11     18       ATP. {ECO:0000250}.
FT   REGION      157    161       Substrate binding. {ECO:0000250}.
FT   ACT_SITE     83     83       Proton acceptor. {ECO:0000255}.
FT   METAL       138    138       Zinc. {ECO:0000250}.
FT   METAL       141    141       Zinc. {ECO:0000250}.
FT   METAL       170    170       Zinc. {ECO:0000250}.
FT   METAL       173    173       Zinc. {ECO:0000250}.
FT   BINDING     113    113       Substrate; via amide nitrogen.
FT                                {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
//
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