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Database: UniProt
Entry: Q6KH30
LinkDB: Q6KH30
Original site: Q6KH30 
ID   KITH_MYCMO              Reviewed;         200 AA.
AC   Q6KH30;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 79.
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=MMOB6150;
OS   Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=267748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX   PubMed=15289470; DOI=10.1101/gr.2674004;
RA   Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S.,
RA   Butler J., Calvo S., Elkins T., FitzGerald M.G., Hafez N.,
RA   Kodira C.D., Major J., Wang S., Wilkinson J., Nicol R., Nusbaum C.,
RA   Birren B., Berg H.C., Church G.M.;
RT   "The complete genome and proteome of Mycoplasma mobile.";
RL   Genome Res. 14:1447-1461(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         EC=2.7.1.21; Evidence={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}.
DR   EMBL; AE017308; AAT28101.1; -; Genomic_DNA.
DR   RefSeq; WP_011265135.1; NC_006908.1.
DR   ProteinModelPortal; Q6KH30; -.
DR   SMR; Q6KH30; -.
DR   STRING; 267748.MMOB6150; -.
DR   EnsemblBacteria; AAT28101; AAT28101; MMOB6150.
DR   KEGG; mmo:MMOB6150; -.
DR   eggNOG; ENOG4107T8J; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   OrthoDB; 1279539at2; -.
DR   BioCyc; MMOB267748:G1G0Z-672-MONOMER; -.
DR   Proteomes; UP000009072; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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    200       Thymidine kinase.
FT                                /FTId=PRO_0000174996.
FT   NP_BIND      15     22       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      88     91       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       145    145       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       148    148       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       177    177       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       180    180       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   200 AA;  22842 MW;  C972FCEC92FA32DD CRC64;
     MYRKYSDGII EVITGPMYSG KSEELIKRIK ILQFANIKTL IVKQKFDTRF SHNEIVSRSG
     TKLNTIVASN VEEIKKVWNN TYKAIAIDEV QFFDKDIINY IDELASKGIR VIISGLDTDF
     ARKPFGIMPE LLAIADDVLK LKAVCFSCKN AGTHTFRITN DKDQKLLGDT ESYQARCRKC
     HLEGEEQKIQ MDNLKLNLSL
//
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