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Database: UniProt
Entry: D5MEN7_9BACT
LinkDB: D5MEN7_9BACT
Original site: D5MEN7_9BACT 
ID   D5MEN7_9BACT            Unreviewed;       243 AA.
AC   D5MEN7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 39.
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   ECO:0000313|EMBL:CBE68216.1};
GN   ORFNames=DAMO_1156 {ECO:0000313|EMBL:CBE68216.1};
OS   Candidatus Methylomirabilis oxyfera.
OC   Bacteria; candidate division NC10; Candidatus Methylomirabilis.
OX   NCBI_TaxID=671143 {ECO:0000313|EMBL:CBE68216.1, ECO:0000313|Proteomes:UP000006898};
RN   [1] {ECO:0000313|EMBL:CBE68216.1, ECO:0000313|Proteomes:UP000006898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20336137; DOI=10.1038/nature08883;
RA   Ettwig K.F., Butler M.K., Le Paslier D., Pelletier E., Mangenot S.,
RA   Kuypers M.M.M., Schreiber F., Dutilh B.E., Zedelius J., de Beer D.,
RA   Gloerich J., Wessels H.J.C.T., van Allen T., Luesken F., Wu M.,
RA   van de Pas-Schoonen K.T., Op den Camp H.J.M., Janssen-Megens E.M.,
RA   Francoijs K-J., Stunnenberg H., Weissenbach J., Jetten M.S.M.,
RA   Strous M.;
RT   "Nitrite-driven anaerobic methane oxidation by oxygenic bacteria.";
RL   Nature 464:543-548(2010).
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; FP565575; CBE68216.1; -; Genomic_DNA.
DR   STRING; 671143.DAMO_1156; -.
DR   KEGG; mox:DAMO_1156; -.
DR   PATRIC; fig|671143.5.peg.1015; -.
DR   KO; K00943; -.
DR   Proteomes; UP000006898; 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:UP000006898};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:CBE68216.1};
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, ECO:0000313|EMBL:CBE68216.1}.
FT   DOMAIN       25    223       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      27     34       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   243 AA;  26755 MW;  A0B3C9F0E6D57D96 CRC64;
     MIADSESKNV QRDERGAMRG IFVTFEGGEG SGKTTQLKLL ANRIRASGKE VIETHDPGGT
     AIGKEIRTLL LDPGSAPIAS TTELLLYEAS RAQLVRELIA PTLRQGVVVL CDRFTDSTLA
     YQGFGRSLDL DLIQRLNRCA TDGVVPDLTI LFDLDPEIGL TRCRRDTSLD AVTGSGAEPA
     CWDRIEAEPL EFHRRIREGY LALARENRDR MIVIDAGVGV TEIETIVWNQ FIRLQGRCVN
     AVS
//
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