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Database: UniProt
Entry: B9IRW3
LinkDB: B9IRW3
Original site: B9IRW3 
ID   KITH_BACCQ              Reviewed;         195 AA.
AC   B9IRW3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   05-DEC-2018, entry version 54.
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=BCQ_5171;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/JB.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L.,
RA   Xu X., Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain
RT   Q1 with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM15571.1; -; Genomic_DNA.
DR   RefSeq; WP_000280862.1; NC_011969.1.
DR   ProteinModelPortal; B9IRW3; -.
DR   SMR; B9IRW3; -.
DR   EnsemblBacteria; ACM15571; ACM15571; BCQ_5171.
DR   KEGG; bcq:BCQ_5171; -.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; CAGLDQD; -.
DR   BioCyc; BCER361100:G1G5I-5398-MONOMER; -.
DR   Proteomes; UP000000441; 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; Transferase; Zinc.
FT   CHAIN         1    195       Thymidine kinase.
FT                                /FTId=PRO_1000122652.
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       183    183       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       186    186       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   195 AA;  21716 MW;  9A421C56F23B5D99 CRC64;
     MYLINQNGWI EVICGSMFSG KSEELIRRVR RTQFAKQHAI VFKPCIDNRY SEEDVVSHNG
     LKVKAVPVSA SKDIFEHITE EMDVIAIDEV QFFDGDIVEV VQVLANRGYR VIVAGLDQDF
     RGLPFGQVPQ LMAIAEHVTK LQAVCSACGS PASRTQRLID GEPAAFDDPI ILVGASESYE
     PRCRHCHAVP TNKDK
//
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