ID KITH_MYCPE Reviewed; 220 AA. AC Q8EU99; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 22-JUL-2015, entry version 74. DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124}; DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124}; GN Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124}; GN OrderedLocusNames=MYPE10320; OS Mycoplasma penetrans (strain HF-2). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272633; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HF-2; RX PubMed=12466555; DOI=10.1093/nar/gkf667; RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K., RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.; RT "The complete genomic sequence of Mycoplasma penetrans, an RT intracellular bacterial pathogen in humans."; RL Nucleic Acids Res. 30:5293-5300(2002). CC -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SIMILARITY: Belongs to the thymidine kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00124}. 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; BA000026; BAC44817.1; -; Genomic_DNA. DR RefSeq; WP_011077845.1; NC_004432.1. DR ProteinModelPortal; Q8EU99; -. DR STRING; 272633.MYPE10320; -. DR EnsemblBacteria; BAC44817; BAC44817; BAC44817. DR KEGG; mpe:MYPE10320; -. DR PATRIC; 20021252; VBIMycPen56664_1056. DR eggNOG; COG1435; -. DR HOGENOM; HOG000076390; -. DR KO; K00857; -. DR OMA; TMRKTEE; -. DR OrthoDB; EOG69D3J2; -. DR BioCyc; MPEN272633:GJBP-1059-MONOMER; -. DR Proteomes; UP000002522; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00124; Thymidine_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001267; Thymidine_kinase. DR InterPro; IPR020633; Thymidine_kinase_CS. DR PANTHER; PTHR11441; PTHR11441; 1. DR Pfam; PF00265; TK; 1. DR PIRSF; PIRSF035805; TK_cell; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; Kinase; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; KW Zinc. FT CHAIN 1 220 Thymidine kinase. FT /FTId=PRO_0000174998. FT NP_BIND 18 25 ATP. {ECO:0000255|HAMAP-Rule:MF_00124}. FT NP_BIND 93 96 ATP. {ECO:0000255|HAMAP-Rule:MF_00124}. FT ACT_SITE 94 94 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00124}. FT METAL 150 150 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 153 153 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 188 188 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 191 191 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. SQ SEQUENCE 220 AA; 25184 MW; 47CFA4901E74737F CRC64; MKNNAFGKEK GWIELIYGPM FAGKSEELLR KLKRLDYADV IYQVFKPKID TRTKNKIMSR DGRNMDSFEF DNPYEIFDKL LSLEVNPHVV AIDEAQFADE SIVDVCQALA DSGYIVYVSA LDKNFKNEPF MVTAKIACIA EYVEKLSAIC TDCGAPGTAT QRIINDKPSN YDEPVVQIGN YETYTVKCRH HHKIPGKPFP EEIKKFKSDL RNLLKNKENK //