ID KITH_FRATH Reviewed; 197 AA. AC Q2A3U3; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124}; DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124}; GN Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124}; GN OrderedLocusNames=FTL_0890; OS Francisella tularensis subsp. holarctica (strain LVS). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=376619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LVS; RA Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S., RA Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R., RA Garcia E.; RT "Complete genome sequence of Francisella tularensis LVS (Live Vaccine RT Strain)."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. 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:0000255|HAMAP-Rule:MF_00124}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00124}. 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; AM233362; CAJ79329.1; -; Genomic_DNA. DR RefSeq; WP_003018771.1; NZ_CP009694.1. DR AlphaFoldDB; Q2A3U3; -. DR SMR; Q2A3U3; -. DR KEGG; ftl:FTL_0890; -. DR Proteomes; UP000001944; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. 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; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00124; Thymidine_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001267; Thymidine_kinase. 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. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding; KW Nucleotide-binding; Transferase; Zinc. FT CHAIN 1..197 FT /note="Thymidine kinase" FT /id="PRO_0000242791" FT ACT_SITE 88 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 9..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 87..90 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 187 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 190 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" SQ SEQUENCE 197 AA; 22474 MW; B05840573A52BC7B CRC64; MAKLYFRYSA MDAGKTLDLL KVAYNYEDRG RKPLVLTSAI DKRAGLNKVK SRIGIDQDAY SLTDRDNIFE FVENYNSSNK IDCVLIDEIH FFTQEQVWQL AEIVDELNIP VICYGLRTNY LGQPFETAAL LLAIADTLEE VKTICHCGKK ASFNMMVQNG KAIKQGNPIV VDDDSLKEID TKYVSVCRKH WKEGVYE //