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 15-DEC-2009, entry version 38. DE RecName: Full=Thymidylate kinase; DE EC=2.7.4.9; DE AltName: Full=dTMP kinase; GN Name=tmk; OrderedLocusNames=lmo2693; OS Listeria monocytogenes. OC Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1639; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-679 / EGD-e / Serovar 1/2a; RX MEDLINE=21537279; PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., RA 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 (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + dTMP = ADP + dTDP. CC -!- SIMILARITY: Belongs to the thymidylate kinase family. 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; -. DR GeneID; 987131; -. DR GenomeReviews; AL591824_GR; lmo2693. DR KEGG; lmo:lmo2693; -. DR ListiList; LMO02693; -. DR HOGENOM; HBG626009; -. DR OMA; VVTTREP; -. DR BioCyc; LMON169963:LMO2693-MON; -. DR BRENDA; 2.7.4.9; 96770. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004798; F:thymidylate kinase activity; IEA:HAMAP. DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro. DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00165; -; 1. DR InterPro; IPR018094; Thymidylate_kin. DR InterPro; IPR000062; Thymidylate_kin-like. DR InterPro; IPR018095; Thymidylate_kin_CS. DR PANTHER; PTHR10344; Thymidylate_kin; 1. DR Pfam; PF02223; Thymidylate_kin; 1. DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide biosynthesis; KW Nucleotide-binding; Transferase. FT CHAIN 1 208 Thymidylate kinase. FT /FTId=PRO_0000155297. FT NP_BIND 10 17 ATP (Potential). 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 //