ID D1BEF3_SANKS Unreviewed; 202 AA. AC D1BEF3; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAR-2024, entry version 67. DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544}; DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544}; GN OrderedLocusNames=Sked_12890 {ECO:0000313|EMBL:ACZ21231.1}; OS Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae; OC Sanguibacter. OX NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ21231.1, ECO:0000313|Proteomes:UP000000322}; RN [1] {ECO:0000313|EMBL:ACZ21231.1, ECO:0000313|Proteomes:UP000000322} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74 RC {ECO:0000313|Proteomes:UP000000322}; RX PubMed=21304646; RA Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C., RA Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A., RA Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R., RA Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Sanguibacter keddieii type strain (ST-74)."; RL Stand. Genomic Sci. 1:110-118(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|RuleBase:RU000544}; CC -!- SIMILARITY: Belongs to the thymidine kinase family. CC {ECO:0000256|ARBA:ARBA00007587, 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; CP001819; ACZ21231.1; -; Genomic_DNA. DR RefSeq; WP_012866300.1; NC_013521.1. DR AlphaFoldDB; D1BEF3; -. DR STRING; 446469.Sked_12890; -. DR KEGG; ske:Sked_12890; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_2_2_11; -. DR OrthoDB; 9781579at2; -. DR Proteomes; UP000000322; Chromosome. DR GO; GO:0005524; F:ATP 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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|RuleBase:RU000544}; KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634, KW ECO:0000256|RuleBase:RU000544}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000544}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}. FT ACT_SITE 94 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1" SQ SEQUENCE 202 AA; 22208 MW; EC1BAD97FE56F3EC CRC64; MAKLYFRYGA MNSGKSTALL QAAYNYEERG HQVLLAKPGI DTKAGRAIQS RLGFDRDVDF MVGEGQDAYA LFQQHRAHVQ TESGRDVSCL LVDESQFLSA GQVNDLLRIA TLDSIPVICY GIRTDFQTAA FPGSRRLLEI AHSLEELKTI CRCGRKAIFN ARSVDGVFTF DGAQVAIDGV EVGYESLCAA CYLRESGGHL TR //