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Database: UniProt
Entry: KTHY_BRADU
LinkDB: KTHY_BRADU
Original site: KTHY_BRADU 
ID   KTHY_BRADU              Reviewed;         228 AA.
AC   Q89LM5;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=Thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165}; OrderedLocusNames=bll4518;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC
OS   14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
RA   Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA   Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA   Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000255|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:0000255|HAMAP-
CC         Rule:MF_00165};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00165}.
DR   EMBL; BA000040; BAC49783.1; -; Genomic_DNA.
DR   RefSeq; NP_771158.1; NC_004463.1.
DR   RefSeq; WP_011087289.1; NZ_CP011360.1.
DR   SMR; Q89LM5; -.
DR   STRING; 224911.27352781; -.
DR   PRIDE; Q89LM5; -.
DR   EnsemblBacteria; BAC49783; BAC49783; BAC49783.
DR   GeneID; 1052595; -.
DR   KEGG; bja:bll4518; -.
DR   PATRIC; fig|224911.44.peg.4297; -.
DR   eggNOG; ENOG4108ZMD; Bacteria.
DR   eggNOG; COG0125; LUCA.
DR   HOGENOM; HOG000229078; -.
DR   InParanoid; Q89LM5; -.
DR   KO; K00943; -.
DR   OMA; FLYTADH; -.
DR   PhylomeDB; Q89LM5; -.
DR   BioCyc; BDIA224911:G1G3J-4548-MONOMER; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central.
DR   GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central.
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; Complete proteome; Kinase; Nucleotide biosynthesis;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    228       Thymidylate kinase.
FT                                /FTId=PRO_0000155246.
FT   NP_BIND      20     27       ATP. {ECO:0000255|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   228 AA;  24540 MW;  5F5AE27E08AEDCE3 CRC64;
     MSDSAVQRSS GRGRFITFEG GEGTGKSTQI KKLADRLKAA RMRTLVTREP GGSPGAEIMR
     HLVLSGMGKL LGPEAETLLF AAARDDHVHT VIEPALKQGI WVLCDRFADS TRAYQGSLGS
     VSPGLINAMQ RVTIGDLKPD LTIILDLPVE IGLQRAAARR GSGTPDRFEG EQLSFHQGLR
     EAYRKIAADE PARCVLIDAN SDPDTVAGRV WSALRDRLLP TPASVVSV
//
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