ID A8LI40_DINSH Unreviewed; 199 AA. AC A8LI40; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 27-MAR-2024, entry version 77. 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:ABV94374.1}; GN OrderedLocusNames=Dshi_2641 {ECO:0000313|EMBL:ABV94374.1}; OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Roseobacteraceae; Dinoroseobacter. OX NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV94374.1, ECO:0000313|Proteomes:UP000006833}; RN [1] {ECO:0000313|Proteomes:UP000006833} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12 RC {ECO:0000313|Proteomes:UP000006833}; RX PubMed=19741735; DOI=10.1038/ismej.2009.94; RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I., RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C., RA Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W., RA Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T., RA Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S., RA Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A., RA Zech H., Simon M.; RT "The complete genome sequence of the algal symbiont Dinoroseobacter shibae: RT a hitchhiker's guide to life in the sea."; RL ISME J. 4:61-77(2010). 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; CP000830; ABV94374.1; -; Genomic_DNA. DR AlphaFoldDB; A8LI40; -. DR STRING; 398580.Dshi_2641; -. DR KEGG; dsh:Dshi_2641; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_2_1_5; -. DR Proteomes; UP000006833; 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:UP000006833}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}. FT ACT_SITE 91 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124, FT ECO:0000256|PIRSR:PIRSR035805-1" FT BINDING 12..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 90..93 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 150 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 199 AA; 22033 MW; 4027863C8B7481BF CRC64; MRAMAKLYFH YSTMNAGKST ALLQASHNYI ERGMQTHLMT ARLDHRAGEG RIGSRIGLSA PADTFGPETD LFDALALRLK GGPCACVFVD EAQFLTEDQV WQLARAVDDL NLPVMCYGLR VDFRGKLFPG SAALLALADE MREVRTICHC GRKATMVVRR DAEGRTVTDG AQVQVGGNET YLSLCRRHWR EATGDRPRG //