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Entry: A0A1F6K794_9BACT
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ID   A0A1F6K794_9BACT        Unreviewed;       230 AA.
AC   A0A1F6K794;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   11-DEC-2019, entry version 24.
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=A3B53_03475 {ECO:0000313|EMBL:OGH42942.1};
OS   Candidatus Levybacteria bacterium RIFCSPLOWO2_01_FULL_42_15.
OC   Bacteria; Candidatus Levybacteria.
OX   NCBI_TaxID=1798626 {ECO:0000313|EMBL:OGH42942.1, ECO:0000313|Proteomes:UP000177490};
RN   [1] {ECO:0000313|EMBL:OGH42942.1, ECO:0000313|Proteomes:UP000177490}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGH42942.1}.
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DR   EMBL; MFOZ01000015; OGH42942.1; -; Genomic_DNA.
DR   Proteomes; UP000177490; Unassembled WGS sequence.
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};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070206,
KW   ECO:0000313|EMBL:OGH42942.1};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN          23..217
FT                   /note="Thymidylate_kin"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   NP_BIND         25..32
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   230 AA;  25703 MW;  6B738FA6364C0D0C CRC64;
     MKYHIAFDLD LRRNPYRGLY IALEGVDGSG KTTQAEALTR YFEGIGKTVV QTREPRKAGL
     IGDLVQKILT GEQKIPPVAL QYLFSTDRVI NHEEVIIPSL KAGHVVISDR SFWSAVVYGV
     LDRSKGAYDK SAADLLLITQ SILSMYHQFI VPDFTCYLSI SLQTALSRIA GKDDVKEIYE
     DKGKLAKIIE GYNFLQERFS GEITPVSGER SVAEVTNLLI DIVEKREKSA
//
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