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Database: UniProt
Entry: G6Y3C6_9RHIZ
LinkDB: G6Y3C6_9RHIZ
Original site: G6Y3C6_9RHIZ 
ID   G6Y3C6_9RHIZ            Unreviewed;       224 AA.
AC   G6Y3C6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, 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   ORFNames=MEA186_02108 {ECO:0000313|EMBL:EHH13786.1};
OS   Mesorhizobium amorphae CCNWGS0123.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=1082933 {ECO:0000313|EMBL:EHH13786.1, ECO:0000313|Proteomes:UP000002949};
RN   [1] {ECO:0000313|EMBL:EHH13786.1, ECO:0000313|Proteomes:UP000002949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCNWGS0123 {ECO:0000313|EMBL:EHH13786.1,
RC   ECO:0000313|Proteomes:UP000002949};
RX   PubMed=22247533; DOI=10.1128/JB.06475-11;
RA   Hao X., Lin Y., Johnstone L., Baltrus D.A., Miller S.J., Wei G.,
RA   Rensing C.;
RT   "Draft Genome Sequence of Plant Growth-Promoting Rhizobium
RT   Mesorhizobium amorphae, Isolated from Zinc-Lead Mine Tailings.";
RL   J. Bacteriol. 194:736-737(2012).
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; AGSN01000019; EHH13786.1; -; Genomic_DNA.
DR   RefSeq; WP_006199808.1; NZ_CP015318.1.
DR   STRING; 1082933.MEA186_02108; -.
DR   EnsemblBacteria; EHH13786; EHH13786; MEA186_02108.
DR   GeneID; 32100189; -.
DR   KEGG; mamo:A6B35_19320; -.
DR   PATRIC; fig|1082933.3.peg.379; -.
DR   KO; K00943; -.
DR   OrthoDB; 1585072at2; -.
DR   BioCyc; GCF_001686985:G1EYV-3947-MONOMER; -.
DR   Proteomes; UP000002949; Unassembled WGS sequence.
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:UP000002949};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:EHH13786.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000002949};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:EHH13786.1}.
FT   DOMAIN        9    198       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      11     18       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   224 AA;  24085 MW;  71D0705D46B36412 CRC64;
     MASGFFITFE GGEGAGKSTQ IERLARKMRA KKYDVLVTRE PGGSPGAEAV RHVLLSGAAE
     PFGPKMEALL FAAARSDHVE QVIRPAVERG TIVLCDRFMD SSRVYQGVTG GLDPAFMEAL
     EEVAINGMVP DITLIFDIDP AEGLRRATAR RGAGDGPDRF EKETLDIHQR RREAFLAIAA
     AEPQRCIVVD ASADPDTVDH VVTAAVFAAL ETMTPAHKRQ AAPA
//
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