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Database: UniProt
Entry: Q606M0
LinkDB: Q606M0
Original site: Q606M0 
ID   KTHY_METCA              Reviewed;         208 AA.
AC   Q606M0;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   01-OCT-2014, entry version 58.
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=MCA1996;
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E.,
RA   Ravel J., Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R.,
RA   Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J.,
RA   Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S.,
RA   Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R.,
RA   Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU91791.1; -; Genomic_DNA.
DR   RefSeq; WP_010961241.1; NC_002977.6.
DR   RefSeq; YP_114428.1; NC_002977.6.
DR   ProteinModelPortal; Q606M0; -.
DR   STRING; 243233.MCA1996; -.
DR   EnsemblBacteria; AAU91791; AAU91791; MCA1996.
DR   GeneID; 3104386; -.
DR   KEGG; mca:MCA1996; -.
DR   PATRIC; 22607838; VBIMetCap22254_2026.
DR   eggNOG; COG0125; -.
DR   HOGENOM; HOG000229078; -.
DR   KO; K00943; -.
DR   OMA; EPGGCPI; -.
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    208       Thymidylate kinase.
FT                                /FTId=PRO_0000155300.
FT   NP_BIND      11     18       ATP. {ECO:0000255|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   208 AA;  22834 MW;  A100AAE9B48FEA27 CRC64;
     MTPGKFITLE GGEGVGKSTN VDFVVSRLRA RGLKVVATRE PGGTAFGEAV REIFLRQDTV
     RPEAELLLLF AARVHHLREV IEPALRRGDW VVCDRFTDAS YAYQGAGRGI APGVIDFLRD
     WIQAGLRPDL TLLLDAPVDT GLKRAHQRSG PDRLEREDSA FFARVREGYL ALARAEPGRI
     RVIDADRPLA LVQTAIATQV DSLLAGHV
//
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