ID KITH_MONPZ Reviewed; 177 AA. AC P04363; Q8V4Z6; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2002, sequence version 2. DT 08-NOV-2023, entry version 93. DE RecName: Full=Thymidine kinase; DE EC=2.7.1.21; GN Name=OPG101; Synonyms=TK; ORFNames=L2R; OS Monkeypox virus (strain Zaire-96-I-16) (MPX). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Monkeypox virus. OX NCBI_TaxID=619591; OH NCBI_TaxID=45479; Cynomys gunnisoni (Gunnison's prairie dog) (Spermophilus gunnisoni). OH NCBI_TaxID=99825; Cynomys leucurus (White-tailed prairie dog). OH NCBI_TaxID=45480; Cynomys ludovicianus (Black-tailed prairie dog). OH NCBI_TaxID=99826; Cynomys mexicanus (Mexican prairie dog). OH NCBI_TaxID=99827; Cynomys parvidens (Utah prairie dog). OH NCBI_TaxID=30650; Gliridae (dormice). OH NCBI_TaxID=226685; Heliosciurus ruwenzorii (Ruwenzori sun squirrel). OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=10090; Mus musculus (Mouse). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6330986; DOI=10.1016/0042-6822(84)90212-5; RA Esposito J.J., Knight J.C.; RT "Nucleotide sequence of the thymidine kinase gene region of monkeypox and RT variola viruses."; RL Virology 135:561-567(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Isolate Zaire-96-I-16; RX PubMed=11734207; DOI=10.1016/s0014-5793(01)03144-1; RA Shchelkunov S.N., Totmenin A.V., Babkin I.V., Safronov P.F., RA Ryazankina O.I., Petrov N.A., Gutorov V.V., Uvarova E.A., Mikheev M.V., RA Sisler J.R., Esposito J.J., Jahrling P.B., Moss B., Sandakhchiev L.S.; RT "Human monkeypox and smallpox viruses: genomic comparison."; RL FEBS Lett. 509:66-70(2001). 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 -!- 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; K02025; AAA80529.1; -; Genomic_DNA. DR EMBL; AF380138; AAL40544.1; -; Genomic_DNA. DR PIR; A00610; KIVZMV. DR RefSeq; NP_536513.1; NC_003310.1. DR SMR; P04363; -. DR GeneID; 928935; -. DR KEGG; vg:928935; -. DR Proteomes; UP000101269; 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 3: Inferred from homology; KW ATP-binding; Disulfide bond; DNA synthesis; Kinase; Metal-binding; KW Nucleotide-binding; Transferase; Zinc. FT CHAIN 1..177 FT /note="Thymidine kinase" FT /id="PRO_0000174931" 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" FT CONFLICT 14 FT /note="L -> F (in Ref. 1; AAA80529)" FT /evidence="ECO:0000305" FT CONFLICT 90 FT /note="I -> V (in Ref. 1; AAA80529)" FT /evidence="ECO:0000305" FT CONFLICT 153 FT /note="A -> T (in Ref. 1; AAA80529)" FT /evidence="ECO:0000305" SQ SEQUENCE 177 AA; 19990 MW; 8A7BAAB3238C91D2 CRC64; MNGGHIQLII GPMLSGKSTE LIRRVRRYQI AQYKCVTIKY SNDNRYGTGL WTHDKNNFAA LEVTKLCDVL EAITDFSVIG IDEGQFFPDI VEFCERMANE GKIVIVAALD GTFQRRPFNN ILNLIPLSEM VVKLTAVCMK CFKEASFSKR LGAETEIEII GGNDMYQSVC RKCYIDS //