ID C6W223_DYAFD Unreviewed; 201 AA. AC C6W223; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 75. 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 OrderedLocusNames=Dfer_4396 {ECO:0000313|EMBL:ACT95598.1}; OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / OS KCTC 52180 / NS114). OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae; OC Dyadobacter. OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT95598.1, ECO:0000313|Proteomes:UP000002011}; RN [1] {ECO:0000313|EMBL:ACT95598.1, ECO:0000313|Proteomes:UP000002011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114 RC {ECO:0000313|Proteomes:UP000002011}; RX PubMed=21304649; DOI=10.4056/sigs.19262; RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C., RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M., RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N., RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114)."; RL Stand. Genomic Sci. 1:133-140(2009). 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; CP001619; ACT95598.1; -; Genomic_DNA. DR RefSeq; WP_015813841.1; NC_013037.1. DR AlphaFoldDB; C6W223; -. DR STRING; 471854.Dfer_4396; -. DR KEGG; dfe:Dfer_4396; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_3_0_10; -. DR OrthoDB; 9781579at2; -. DR Proteomes; UP000002011; 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; 3.30.60.20; -; 1. 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 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 {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}; Reference proteome {ECO:0000313|Proteomes:UP000002011}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}. FT ACT_SITE 97 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124, FT ECO:0000256|PIRSR:PIRSR035805-1" FT BINDING 24..31 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 96..99 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 153 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 156 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 188 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" SQ SEQUENCE 201 AA; 22771 MW; CB8394C86ED6918F CRC64; MFVEPSHRRE FQNPRTGWIE VICGSMFSGK TEELIRLLNR ARIARQRIQI FKPALDKRYH EENIVSHNDN SIPSIPVQSS QQISDLAQDC EVVGIDEAQF FDEGILAVCD QLANSGKRVI VAGLDMDYMG KPFGCMPQLM AIAEYVTKVH AVCMVCGEVA SHSYRLSPSN ERVLLGETDH YEARCRRCFN LGEKATELFS R //