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Database: UniProt
Entry: A0A1J4WK68_9BACT
LinkDB: A0A1J4WK68_9BACT
Original site: A0A1J4WK68_9BACT 
ID   A0A1J4WK68_9BACT        Unreviewed;       221 AA.
AC   A0A1J4WK68;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-MAY-2019, entry version 10.
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   ORFNames=AUJ39_00750 {ECO:0000313|EMBL:OIO49586.1};
OS   Parcubacteria group bacterium CG1_02_42_13.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1805309 {ECO:0000313|EMBL:OIO49586.1};
RN   [1] {ECO:0000313|EMBL:OIO49586.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_42_13 {ECO:0000313|EMBL:OIO49586.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C.,
RA   Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO
RT   concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00165}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OIO49586.1}.
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DR   EMBL; MNWJ01000017; OIO49586.1; -; Genomic_DNA.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN        8    202       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
SQ   SEQUENCE   221 AA;  25687 MW;  8489C636417B8E66 CRC64;
     MTGRLIAFEG IDGVGKDTQL KLFQERLETE GIKYKTASFP RHGEKSAYFV DKYLELDGPY
     GDSGKLDPYQ ASVFYSVDRY DASFEIKKWL NDGFTVVLDR YTGSNIGHQG GKIDNEERAK
     YADWLLNFEY NLLQIPKPIF SIVLWLPPEV AHSRITSRGR EMDGHEVNLE HLKKAQLAYL
     WASKHYPDDF KVVKCFEEER ELSEKEVHEK IWQIVKEVLK S
//
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