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Database: UniProt
Entry: Q1QX49
LinkDB: Q1QX49
Original site: Q1QX49 
ID   KTHY_CHRSD              Reviewed;         212 AA.
AC   Q1QX49;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   01-OCT-2014, entry version 54.
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=Csal_1606;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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: ATP + dTMP = ADP + dTDP. {ECO:0000255|HAMAP-
CC       Rule:MF_00165}.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00165}.
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DR   EMBL; CP000285; ABE58959.1; -; Genomic_DNA.
DR   RefSeq; YP_573658.1; NC_007963.1.
DR   ProteinModelPortal; Q1QX49; -.
DR   STRING; 290398.Csal_1606; -.
DR   EnsemblBacteria; ABE58959; ABE58959; Csal_1606.
DR   GeneID; 4027568; -.
DR   KEGG; csa:Csal_1606; -.
DR   PATRIC; 21447008; VBIChrSal113723_1616.
DR   eggNOG; COG0125; -.
DR   HOGENOM; HOG000229078; -.
DR   KO; K00943; -.
DR   OMA; EGYIVIC; -.
DR   OrthoDB; EOG64JFSH; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR018094; Thymidylate_kinase.
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; Reference proteome; Transferase.
FT   CHAIN         1    212       Thymidylate kinase.
FT                                /FTId=PRO_1000023177.
FT   NP_BIND      11     18       ATP. {ECO:0000255|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   212 AA;  23342 MW;  0D4F022AC5AA3BA5 CRC64;
     MTPGRFITLE GGEGVGKSTN VAFVCDWLSA RGIEVVRTRE PGGTPRAEAI RELLLDPAPQ
     EPLDETAELL LMFAARAQHL AARIRPALAR GAWVVCDRFT DATFAYQGGG RGLDETRIAT
     LEALVQQGLQ PDLTLLLDMP VEAAQRRVER RGIERDRFER ERGAFFNAVR ESYLARAAQA
     PTRFAVIDAD RSLEAVQASI AAHLTERLAS WS
//
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