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Database: UniProt
Entry: S5Z8E1_BACPJ
LinkDB: S5Z8E1_BACPJ
Original site: S5Z8E1_BACPJ 
ID   S5Z8E1_BACPJ            Unreviewed;       226 AA.
AC   S5Z8E1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   08-MAY-2019, entry version 34.
DE   RecName: Full=Thymidylate kinase {ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165};
GN   ORFNames=M493_00375 {ECO:0000313|EMBL:AGT30485.1};
OS   Bacillus sp. (strain JF8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1921421 {ECO:0000313|EMBL:AGT30485.1, ECO:0000313|Proteomes:UP000015500};
RN   [1] {ECO:0000313|EMBL:AGT30485.1, ECO:0000313|Proteomes:UP000015500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF8 {ECO:0000313|EMBL:AGT30485.1,
RC   ECO:0000313|Proteomes:UP000015500};
RX   PubMed=24459274;
RA   Shintani M., Ohtsubo Y., Fukuda K., Hosoyama A., Ohji S., Yamazoe A.,
RA   Fujita N., Nagata Y., Tsuda M., Hatta T., Kimbara K.;
RT   "Complete Genome Sequence of the Thermophilic Polychlorinated Biphenyl
RT   Degrader Geobacillus sp. Strain JF8 (NBRC 109937).";
RL   Genome Announc. 2:e01213-13(2014).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_00165}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC         ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070220}.
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DR   EMBL; CP006254; AGT30485.1; -; Genomic_DNA.
DR   RefSeq; WP_020958280.1; NC_022080.4.
DR   EnsemblBacteria; AGT30485; AGT30485; M493_00375.
DR   KEGG; gjf:M493_00375; -.
DR   PATRIC; fig|1345697.3.peg.26; -.
DR   KO; K00943; -.
DR   Proteomes; UP000015500; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000015500};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:AGT30485.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070211};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070205};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN        8    196       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      10     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   226 AA;  25756 MW;  CBDEA486C52A7EB8 CRC64;
     MNGYFVSFEG PEGAGKTTMI GKLESFLRER SFDVMVTREP GGVRIAEAIR ALILNREYTE
     MDGRTEALLY AAARRQHLLE KIVPALEAGR IVLCDRFVDS SLAYQGFARG LGIEDVWKIN
     EFAIDGYMPS LTVYFDIDPQ TGLERIRKNR EREVNRLDLE SLSFHDKVRE GYRELAKRFA
     DRIIVIDAGR PLDVVFAETA AVVLSRLKGR SKCDFHESGR DDSRWT
//
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