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Database: UniProt/SWISS-PROT
Entry: KITH_BACV8
LinkDB: KITH_BACV8
Original site: KITH_BACV8 
ID   KITH_BACV8              Reviewed;         199 AA.
AC   A6L1E7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   07-JUN-2017, entry version 60.
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=BVU_1836;
OS   Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / NBRC
OS   14291 / NCTC 11154).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / NBRC 14291 / NCTC 11154;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M.,
RA   Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P.,
RA   Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A.,
RA   Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(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   -!- 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; CP000139; ABR39511.1; -; Genomic_DNA.
DR   RefSeq; WP_005842663.1; NC_009614.1.
DR   ProteinModelPortal; A6L1E7; -.
DR   SMR; A6L1E7; -.
DR   STRING; 435590.BVU_1836; -.
DR   EnsemblBacteria; ABR39511; ABR39511; BVU_1836.
DR   GeneID; 5302802; -.
DR   KEGG; bvu:BVU_1836; -.
DR   eggNOG; ENOG4107T8J; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   Proteomes; UP000002861; 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; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    199       Thymidine kinase.
FT                                /FTId=PRO_1000018151.
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;  22372 MW;  5DCADD40923670E6 CRC64;
     MVVFSEDHIQ ETRRRGRIEV ICGSMFSGKT EELIRRLKRA KFARQRVEIF KPAIDTRYSE
     EEVVSHDSNS IASTPIDSSA SILLFSSDKD VVGIDEAQFF DEGLVDVCNK LADNGIRVIV
     AGLDMDFRRV PFGPIPALLA IADEVTKVHA ICVKCGNLAY ATHRITKSEK RVLLGEKADY
     EPLCRTCYME ALKEETENK
//
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