ID KTHY_LISMO Reviewed; 208 AA. AC Q8Y3Y6; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 13-SEP-2023, entry version 103. 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=lmo2693; OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e). OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=169963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-679 / EGD-e; RX PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D., RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). 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; AL591984; CAD00906.1; -; Genomic_DNA. DR PIR; AD1411; AD1411. DR RefSeq; NP_466215.1; NC_003210.1. DR RefSeq; WP_009930435.1; NZ_CP023861.1. DR AlphaFoldDB; Q8Y3Y6; -. DR SMR; Q8Y3Y6; -. DR STRING; 169963.lmo2693; -. DR PaxDb; Q8Y3Y6; -. DR EnsemblBacteria; CAD00906; CAD00906; CAD00906. DR GeneID; 987131; -. DR KEGG; lmo:lmo2693; -. DR PATRIC; fig|169963.11.peg.2759; -. DR eggNOG; COG0125; Bacteria. DR HOGENOM; CLU_049131_0_2_9; -. DR OMA; FLYTADH; -. DR OrthoDB; 9774907at2; -. DR PhylomeDB; Q8Y3Y6; -. DR BioCyc; LMON169963:LMO2693-MONOMER; -. DR Proteomes; UP000000817; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central. DR GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central. DR GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central. DR GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central. 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 NCBIfam; TIGR00041; DTMP_kinase; 1. 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 PROSITE; PS01331; THYMIDYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1..208 FT /note="Thymidylate kinase" FT /id="PRO_0000155297" FT BINDING 10..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165" SQ SEQUENCE 208 AA; 23083 MW; 36EE08314CAAC969 CRC64; MKAIFITLEG PDGSGKTTVG TLLNQKMTEA GIDFIKTREP GGSPISEKVR NIVLGIGNEE MDPKTEVLLI AGARRQHVVE TIRPALAAGK SVLCDRFMDS SLAYQGAGRD MNMEQVLQVN LYAIEDTLPD RTYYLDVPAE VGLARIAANK GREVNRLDKE DITYHEKVQA GYEKVINMFP ERFMRVDATK TPEEITETIL ADILRQLA //