ID A0Q6T2_FRATN Unreviewed; 197 AA. AC A0Q6T2; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124}; DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124}; GN Name=tdk {ECO:0000256|HAMAP-Rule:MF_00124, GN ECO:0000313|EMBL:ABK89947.1}; GN OrderedLocusNames=FTN_1060 {ECO:0000313|EMBL:ABK89947.1}; GN ORFNames=AW25_948 {ECO:0000313|EMBL:AJI61381.1}; OS Francisella tularensis subsp. novicida (strain U112). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=401614 {ECO:0000313|EMBL:ABK89947.1, ECO:0000313|Proteomes:UP000000762}; RN [1] {ECO:0000313|EMBL:ABK89947.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=U112 {ECO:0000313|EMBL:ABK89947.1}; RA Brittnacher M., Rohmer L., Zhou Y., Abmayr S., D'Argenio D., Bovee D., RA Chang J., Chen J., Drees B., Ernst R., Fong C., Forsman M., Gallagher L., RA Gallis B., Gillett W., Goodlett D., Guina T., Guenthner D., Haugen E., RA Hayden H., Jacobs M., Kang A., Larson Freeman T., Levy R., Lim R., RA Manoil C., Olson M.V., Radey M., Shaffer S., Svensson K., Taylor G., RA Wasnick M., Kaul R., Miller S.I.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000762} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=U112 {ECO:0000313|Proteomes:UP000000762}; RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102; RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M., RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C., RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J., RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A., RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V., RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.; RT "Comparison of Francisella tularensis genomes reveals evolutionary events RT associated with the emergence of human pathogenic strains."; RL Genome Biol. 8:R102.1-R102.16(2007). RN [3] {ECO:0000313|EMBL:AJI61381.1, ECO:0000313|Proteomes:UP000031872} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=U112 {ECO:0000313|EMBL:AJI61381.1, RC ECO:0000313|Proteomes:UP000031872}; RX PubMed=25931589; RA Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G., RA Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Chertkov O., RA Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N., Gibbons H.S., RA Palacios G.F., Redden C.L., Xu Y., Minogue T.D., Chain P.S.; RT "Genome sequencing of 18 francisella strains to aid in assay development RT and testing."; RL Genome Announc. 3:0-0(2015). 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:0000256|HAMAP-Rule:MF_00124, CC ECO:0000256|RuleBase:RU000544}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00124}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}. CC -!- SIMILARITY: Belongs to the thymidine kinase family. CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|HAMAP-Rule:MF_00124, CC ECO:0000256|RuleBase:RU004165}. 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; CP000439; ABK89947.1; -; Genomic_DNA. DR EMBL; CP009633; AJI61381.1; -; Genomic_DNA. DR RefSeq; WP_003018771.1; NZ_CP009633.1. DR AlphaFoldDB; A0Q6T2; -. DR SMR; A0Q6T2; -. DR KEGG; ftn:FTN_1060; -. DR KEGG; ftx:AW25_948; -. DR BioCyc; FTUL401614:G1G75-1103-MONOMER; -. DR Proteomes; UP000000762; Chromosome. DR Proteomes; UP000031872; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00124}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}; KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634, ECO:0000256|HAMAP- KW Rule:MF_00124}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00124}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00124}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00124}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}. FT ACT_SITE 88 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124, FT ECO:0000256|PIRSR:PIRSR035805-1" FT BINDING 9..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 87..90 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 187 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 190 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|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 //