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Database: UniProt
Entry: A0A0C5J8Q7_9RHOO
LinkDB: A0A0C5J8Q7_9RHOO
Original site: A0A0C5J8Q7_9RHOO 
ID   A0A0C5J8Q7_9RHOO        Unreviewed;       202 AA.
AC   A0A0C5J8Q7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   08-MAY-2019, entry version 22.
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   ECO:0000313|EMBL:AJP48355.1};
GN   ORFNames=PG1C_07565 {ECO:0000313|EMBL:AJP48355.1};
OS   Rugosibacter aromaticivorans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Rugosibacter.
OX   NCBI_TaxID=1565605 {ECO:0000313|EMBL:AJP48355.1, ECO:0000313|Proteomes:UP000061603};
RN   [1] {ECO:0000313|EMBL:AJP48355.1, ECO:0000313|Proteomes:UP000061603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1-Ca6 {ECO:0000313|Proteomes:UP000061603};
RX   PubMed=25858839;
RA   Singleton D.R., Dickey A.N., Scholl E.H., Wright F.A., Aitken M.D.;
RT   "Complete Genome Sequence of a Novel Bacterium within the Family
RT   Rhodocyclaceae That Degrades Polycyclic Aromatic Hydrocarbons.";
RL   Genome Announc. 3:0-0(2015).
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; CP010554; AJP48355.1; -; Genomic_DNA.
DR   EnsemblBacteria; AJP48355; AJP48355; PG1C_07565.
DR   KEGG; rbu:PG1C_07565; -.
DR   PATRIC; fig|1565605.3.peg.1596; -.
DR   KO; K00943; -.
DR   Proteomes; UP000061603; 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 {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000061603};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:AJP48355.1};
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:UP000061603};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:AJP48355.1}.
FT   DOMAIN        8    193       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      10     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
FT   COILED      136    156       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   202 AA;  22735 MW;  D97A67873485F14D CRC64;
     MRGRFITFEG IDGAGKSTQH AWLAAHLRSL GHEVVATREP GGTPLGEQLR GLLLAEPMHI
     ETEALLMFAA RREHIAQVIE PALTRGAWVA CDRFADASFA YQSGGRGLAW EKIAALRDWT
     LGHLQPDITF IFDIPVATAQ ERLAKINNQR DRFEQEQTAF FERVRAAYHR IATENPQRVT
     LIDATQSTEE INKLLEKSIA RY
//
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