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 24-JAN-2024, entry version 76. DE RecName: Full=Thymidine kinase; DE EC=2.7.1.21; GN Name=OPG101; Synonyms=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. {ECO:0000250|UniProtKB:O57203}. 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:0000250|UniProtKB:O57203}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=25 uM for 2'deoxythymidine {ECO:0000269|PubMed:17335913}; CC -!- SUBUNIT: Homotetramer. Two molecules of substrate bind to each enzyme CC tetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 3.30.60.20; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001267; Thymidine_kinase. DR InterPro; IPR020633; Thymidine_kinase_CS. DR PANTHER; PTHR11441; THYMIDINE KINASE; 1. DR PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1. DR Pfam; PF00265; TK; 1. DR PIRSF; PIRSF035805; TK_cell; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1. PE 1: Evidence at protein level; KW ATP-binding; Disulfide bond; DNA synthesis; Kinase; Metal-binding; KW Nucleotide-binding; 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:0000250|UniProtKB:O57203" FT BINDING 11..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O57203" FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O57203" FT BINDING 138 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:O57203" FT BINDING 141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:O57203" FT BINDING 157..161 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O57203" FT BINDING 170 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:O57203" FT BINDING 173 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:O57203" FT DISULFID 170 FT /note="Interchain (with C-173)" FT /evidence="ECO:0000250|UniProtKB:O57203" FT DISULFID 173 FT /note="Interchain (with C-170)" FT /evidence="ECO:0000250|UniProtKB:O57203" 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 //