ID KTHY_NEOSM Reviewed; 199 AA. AC Q2GDL6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 22-FEB-2023, entry version 88. DE RecName: Full=Thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165}; DE EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165}; DE AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165}; GN Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165}; OrderedLocusNames=NSE_0547; OS Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama) (Ehrlichia OS sennetsu). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Neorickettsia. OX NCBI_TaxID=222891; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-367 / Miyayama; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(2006). CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and CC salvage pathways of dTTP synthesis. {ECO:0000255|HAMAP-Rule:MF_00165}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, CC ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00165}; CC -!- SIMILARITY: Belongs to the thymidylate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00165}. 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; CP000237; ABD46241.1; -; Genomic_DNA. DR RefSeq; WP_011451936.1; NC_007798.1. DR AlphaFoldDB; Q2GDL6; -. DR SMR; Q2GDL6; -. DR STRING; 222891.NSE_0547; -. DR EnsemblBacteria; ABD46241; ABD46241; NSE_0547. DR KEGG; nse:NSE_0547; -. DR eggNOG; COG0125; Bacteria. DR HOGENOM; CLU_049131_0_2_5; -. DR OMA; VMTREPG; -. DR OrthoDB; 9774907at2; -. DR Proteomes; UP000001942; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro. DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd01672; TMPK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00165; Thymidylate_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR039430; Thymidylate_kin-like_dom. DR InterPro; IPR018095; Thymidylate_kin_CS. DR InterPro; IPR018094; Thymidylate_kinase. DR PANTHER; PTHR10344; THYMIDYLATE KINASE; 1. DR PANTHER; PTHR10344:SF4; UMP-CMP KINASE 2, MITOCHONDRIAL; 1. DR Pfam; PF02223; Thymidylate_kin; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR00041; DTMP_kinase; 1. DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding; KW Transferase. FT CHAIN 1..199 FT /note="Thymidylate kinase" FT /id="PRO_1000023233" FT BINDING 7..14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165" SQ SEQUENCE 199 AA; 22235 MW; 4A120565EF106D4D CRC64; MFIVLEGIDG SGKSTQVKLL SKFLAKDGYP CVLTREPGGT SFAESLRSMI LHDPIDPMAR LLLIVSARVD HYNKVILPAL KEGKVVVCDR FIYSTLAYQG YGDKIDLQTI LDLHRLSGCL VEPDLTLLLL GSGHKKLGRD NFERMPREYL SNVCMGYEKI ARMYPNIHVI KCMGVGRTSE EIVKIVQGKI SEKQTSSCR //