ID C6W9T9_ACTMD Unreviewed; 239 AA. AC C6W9T9; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 74. 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=Amir_3408 {ECO:0000313|EMBL:ACU37306.1}; OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101). OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Actinosynnema. OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU37306.1, ECO:0000313|Proteomes:UP000002213}; RN [1] {ECO:0000313|EMBL:ACU37306.1, ECO:0000313|Proteomes:UP000002213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 / RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213}; RX PubMed=21304636; DOI=10.4056/sigs.21137; RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G., RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K., RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T., RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Actinosynnema mirum type strain (101)."; RL Stand. Genomic Sci. 1:46-53(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; CP001630; ACU37306.1; -; Genomic_DNA. DR AlphaFoldDB; C6W9T9; -. DR STRING; 446462.Amir_3408; -. DR KEGG; ami:Amir_3408; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_2_0_11; -. DR Proteomes; UP000002213; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002213}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}. FT ACT_SITE 115 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1" SQ SEQUENCE 239 AA; 26277 MW; 9258D1B0B0B39205 CRC64; MEPTNPALDP TDALASVPAA GARRGVRAAG SLRFFFGPMD CGKSTLALQI DHNQARQGRC GLLLVRHDRS GTPTISSRMG LARRALEVHD EMDLGALVRE HWGRGQRVDY LIVDEAQFLD PEQVDQLAEL ADDAQIDVYC FGLATDFRST MFPGSRRLFE LADELNAIQV EVLCWCGLPG RFNGRVHDDV LVRDGSTVLV ADVVQVAADD VRYQVLCRKH YRTGDLGPSA VRDGQLSLT //