ID A0A0G0PH36_9BACT Unreviewed; 227 AA.
AC A0A0G0PH36;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-MAY-2019, entry version 20.
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=UT56_C0014G0012 {ECO:0000313|EMBL:KKR24536.1};
OS Candidatus Levybacteria bacterium GW2011_GWB1_39_7.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1618464 {ECO:0000313|EMBL:KKR24536.1};
RN [1] {ECO:0000313|EMBL:KKR24536.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT large radiation of phyla.";
RL Nature 0:0-0(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}.
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:KKR24536.1}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC -----------------------------------------------------------------------
DR EMBL; LBXG01000014; KKR24536.1; -; Genomic_DNA.
DR EnsemblBacteria; KKR24536; KKR24536; UT56_C0014G0012.
DR PATRIC; fig|1618464.3.peg.469; -.
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,
KW ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:KKR24536.1};
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 Thymidylate_kin. {ECO:0000259|Pfam:
FT PF02223}.
FT NP_BIND 25 32 ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ SEQUENCE 227 AA; 26007 MW; AD3107E46AD429AE CRC64;
MKYPIDFELE FQRHNYPGKL IALEGIDGSG KTTQALELVE SLKKEGIKTV YTKEPTDGEI
GKMIRRILTG EKNFEPVSFQ YLFAADRVEH QEEIIGFLKK GKIVVSDRYF WSSIPYGATD
RGIDFKKSQD EANILLVCYS ILSLYHQFIA PDITAYLEVS ADAALKRLSA IRHNVDIYDK
LEKLKSIARG YEWLIRKFPR ELTVIDGSKS IDKVSEELFE KVVKITS
//
