ID KITH_VACCA Reviewed; 177 AA. AC O57203; Q6J3E4; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 13-SEP-2023, entry version 92. DE RecName: Full=Thymidine kinase; DE EC=2.7.1.21; GN Name=OPG101; Synonyms=TK; OrderedLocusNames=MVA086R, ACAM3000_MVA_086; GN ORFNames=J2R; OS Vaccinia virus (strain Ankara) (VACV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus. OX NCBI_TaxID=126794; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=9601507; DOI=10.1006/viro.1998.9123; RA Antoine G., Scheiflinger F., Dorner F., Falkner F.G.; RT "The complete genomic sequence of the modified vaccinia Ankara strain: RT comparison with other orthopoxviruses."; RL Virology 244:365-396(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate Acambis 3000; RA Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J., RA Khristova M., Wohlhueter R.M.; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND TTP, RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, AND DISULFIDE BONDS. RX PubMed=17062140; DOI=10.1186/1472-6807-6-22; RA El Omari K., Solaroli N., Karlsson A., Balzarini J., Stammers D.K.; RT "Structure of vaccinia virus thymidine kinase in complex with dTTP: RT insights for drug design."; RL BMC Struct. Biol. 6:22-22(2006). CC -!- FUNCTION: Phosphorylates thymidine and thymidine analogs, such as CC azidothymidine (AZT). Part of the salvage pathway for pyrimidine CC deoxyribonucleotide synthesis. {ECO:0000269|PubMed:17062140}. 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:17062140}; 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; U94848; AAB96503.1; -; Genomic_DNA. DR EMBL; AY603355; AAT10484.1; -; Genomic_DNA. DR PIR; T37362; T37362. DR PDB; 2J87; X-ray; 3.10 A; A/B/C/D=1-177. DR PDBsum; 2J87; -. DR SMR; O57203; -. DR BRENDA; 2.7.1.21; 6591. DR EvolutionaryTrace; O57203; -. DR Proteomes; UP000159908; Segment. DR Proteomes; UP000172909; Segment. 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 3D-structure; ATP-binding; Disulfide bond; DNA synthesis; Kinase; KW Metal-binding; Nucleotide-binding; Transferase; Zinc. FT CHAIN 1..177 FT /note="Thymidine kinase" FT /id="PRO_0000174937" FT ACT_SITE 83 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:17062140, FT ECO:0007744|PDB:2J87" FT BINDING 11..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:17062140, FT ECO:0007744|PDB:2J87" FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:17062140, FT ECO:0007744|PDB:2J87" FT BINDING 138 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:17062140, FT ECO:0007744|PDB:2J87" FT BINDING 141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:17062140, FT ECO:0007744|PDB:2J87" FT BINDING 157..161 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:17062140, FT ECO:0007744|PDB:2J87" FT BINDING 170 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:17062140, FT ECO:0007744|PDB:2J87" FT BINDING 173 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:17062140, FT ECO:0007744|PDB:2J87" FT DISULFID 170 FT /note="Interchain (with C-173)" FT /evidence="ECO:0000269|PubMed:17062140, FT ECO:0007744|PDB:2J87" FT DISULFID 173 FT /note="Interchain (with C-170)" FT /evidence="ECO:0000269|PubMed:17062140, FT ECO:0007744|PDB:2J87" FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:2J87" FT HELIX 17..29 FT /evidence="ECO:0007829|PDB:2J87" FT TURN 30..32 FT /evidence="ECO:0007829|PDB:2J87" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:2J87" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:2J87" FT HELIX 66..69 FT /evidence="ECO:0007829|PDB:2J87" FT TURN 70..72 FT /evidence="ECO:0007829|PDB:2J87" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:2J87" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:2J87" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:2J87" FT HELIX 90..99 FT /evidence="ECO:0007829|PDB:2J87" FT STRAND 103..107 FT /evidence="ECO:0007829|PDB:2J87" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:2J87" FT HELIX 122..126 FT /evidence="ECO:0007829|PDB:2J87" FT STRAND 129..133 FT /evidence="ECO:0007829|PDB:2J87" FT TURN 139..141 FT /evidence="ECO:0007829|PDB:2J87" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:2J87" FT STRAND 147..153 FT /evidence="ECO:0007829|PDB:2J87" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:2J87" FT STRAND 166..169 FT /evidence="ECO:0007829|PDB:2J87" FT HELIX 171..174 FT /evidence="ECO:0007829|PDB:2J87" SQ SEQUENCE 177 AA; 20028 MW; 57E19BCEBE6F3C54 CRC64; MNGGHIQLII GPMFSGKSTE LIRRVRRYQI AQYKCVTIKY SNDNRYGTGL WTHDKNNFEA LEATKLCDVL ESITDFSVIG IDEGQFFPDI VEFCERMANE GKIVIVAALD GTFQRKPFNN ILNLIPLSEM VVKLTAVCMK CFKEASFSKR LGEETEIEII GGNDMYQSVC RKCYVGS //