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Database: UniProt/SWISS-PROT
Entry: KITH_BACCR
LinkDB: KITH_BACCR
Original site: KITH_BACCR 
ID   KITH_BACCR              Reviewed;         195 AA.
AC   Q814U0;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   23-MAY-2018, entry version 93.
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}; OrderedLocusNames=BC_5330;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 /
OS   NCIMB 9373 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL
RC   B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA   Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA   Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA   Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA   Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with
RT   Bacillus anthracis.";
RL   Nature 423:87-91(2003).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP   TTP, AND SUBUNIT.
RX   PubMed=17288553; DOI=10.1111/j.1742-4658.2006.05617.x;
RA   Kosinska U., Carnrot C., Sandrini M.P., Clausen A.R., Wang L.,
RA   Piskur J., Eriksson S., Eklund H.;
RT   "Structural studies of thymidine kinases from Bacillus anthracis and
RT   Bacillus cereus provide insights into quaternary structure and
RT   conformational changes upon substrate binding.";
RL   FEBS J. 274:727-737(2007).
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       ECO:0000269|PubMed:17288553}.
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; AE016877; AAP12193.1; -; Genomic_DNA.
DR   RefSeq; NP_834992.1; NC_004722.1.
DR   RefSeq; WP_000280859.1; NC_004722.1.
DR   PDB; 2JA1; X-ray; 2.80 A; A=1-195.
DR   PDBsum; 2JA1; -.
DR   ProteinModelPortal; Q814U0; -.
DR   SMR; Q814U0; -.
DR   STRING; 226900.BC5330; -.
DR   EnsemblBacteria; AAP12193; AAP12193; BC_5330.
DR   GeneID; 1207670; -.
DR   KEGG; bce:BC5330; -.
DR   PATRIC; fig|226900.8.peg.5503; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   KO; K00857; -.
DR   OMA; CAGLDQD; -.
DR   EvolutionaryTrace; Q814U0; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IBA:GO_Central.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006259; P:DNA metabolic process; IBA:GO_Central.
DR   GO; GO:0046104; P:thymidine metabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm;
KW   DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN         1    195       Thymidine kinase.
FT                                /FTId=PRO_0000174955.
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   REGION      170    174       Substrate binding.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       145    145       Zinc.
FT   METAL       148    148       Zinc.
FT   METAL       183    183       Zinc.
FT   METAL       186    186       Zinc.
FT   BINDING     120    120       Substrate; via amide nitrogen.
FT   BINDING     179    179       Substrate. {ECO:0000250}.
SQ   SEQUENCE   195 AA;  21696 MW;  937F6D890890302E CRC64;
     MYLINQNGWI EVICGSMFSG KSEELIRRVR RTQFAKQHAI VFKPCIDNRY SEEDVVSHNG
     LKVKAVPVSA SKDIFEHITE ELDVIAIDEV QFFDGDIVEV VQVLANRGYR VIVAGLDQDF
     RGLPFGQVPQ LMAIAEHVTK LQAVCSVCGS PASRTQRLID GEPAAFDDPI ILVGASESYE
     PRCRHCHAVP ANKDK
//
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