GenomeNet

Database: UniProt
Entry: KTHY_PSEE4
LinkDB: KTHY_PSEE4
Original site: KTHY_PSEE4 
ID   KTHY_PSEE4              Reviewed;         210 AA.
AC   Q1ICY2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
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};
GN   OrderedLocusNames=PSEEN1624;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B.,
RA   Wincker P., Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK14481.1; -; Genomic_DNA.
DR   RefSeq; WP_011532891.1; NC_008027.1.
DR   SMR; Q1ICY2; -.
DR   STRING; 384676.PSEEN1624; -.
DR   EnsemblBacteria; CAK14481; CAK14481; PSEEN1624.
DR   GeneID; 32804865; -.
DR   KEGG; pen:PSEEN1624; -.
DR   eggNOG; ENOG4108ZMD; Bacteria.
DR   eggNOG; COG0125; LUCA.
DR   HOGENOM; HOG000229078; -.
DR   KO; K00943; -.
DR   OMA; FLYTADH; -.
DR   OrthoDB; 1585072at2; -.
DR   BioCyc; PENT384676:PSEEN_RS07550-MONOMER; -.
DR   Proteomes; UP000000658; 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; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide biosynthesis;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    210       Thymidylate kinase.
FT                                /FTId=PRO_1000023255.
FT   NP_BIND      10     17       ATP. {ECO:0000255|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   210 AA;  22919 MW;  DFCA675CD5B40062 CRC64;
     MSGLFITLEG PEGAGKSTNR EYLAARLREQ GVDVVMTREP GGTPLAERIR ELLLAPSEEA
     MAVDTELLLM FAARAQHLAQ VIRPALARGA VVLCDRFTDA TYAYQGGGRG LSVERIAILE
     SFVQGELRPD LTLVFDLPVE VGLARAAARG RLDRFEQEGQ AFFEAVRQAY LQRAGQQPQR
     YSLLDAAQPL AAVQRAIDAL LPGILERCRG
//
DBGET integrated database retrieval system