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Database: UniProt/SWISS-PROT
Entry: KITH_BACFR
LinkDB: KITH_BACFR
Original site: KITH_BACFR 
ID   KITH_BACFR              Reviewed;         199 AA.
AC   Q64YL9;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   07-JUN-2017, entry version 69.
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=BF0659;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA
RT   inversions regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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}.
DR   EMBL; AP006841; BAD47407.1; -; Genomic_DNA.
DR   RefSeq; WP_005784663.1; NC_006347.1.
DR   RefSeq; YP_097941.1; NC_006347.1.
DR   ProteinModelPortal; Q64YL9; -.
DR   SMR; Q64YL9; -.
DR   EnsemblBacteria; BAD47407; BAD47407; BF0659.
DR   GeneID; 3081847; -.
DR   KEGG; bfr:BF0659; -.
DR   PATRIC; fig|295405.11.peg.671; -.
DR   HOGENOM; HOG000122165; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   OrthoDB; POG091H0659; -.
DR   Proteomes; UP000002197; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 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    199       Thymidine kinase.
FT                                /FTId=PRO_0000174958.
FT   NP_BIND      23     30       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      95     98       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     96     96       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       152    152       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       155    155       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       184    184       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       187    187       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   199 AA;  22207 MW;  39B1FA503FA9E16A CRC64;
     MVLFSEDHIQ ETRRRGRIEV ICGSMFSGKT EELIRRMKRA KFARQRVEIF KPAIDTRYSE
     GDVVSHDSNS ISSTPIDSSA SILLFTSEID VVGIDEAQFF DSGLIDVCNQ LANNGVRVII
     AGLDMDFKGV PFGPMPALCA IADEVSKVHA ICVKCGQLAS FSHRTVKNDK QVLLGETAQY
     EPLCRECYQR ALQEDREKS
//
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