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Database: UniProt
Entry: J9YEQ0_LEUGJ
LinkDB: J9YEQ0_LEUGJ
Original site: J9YEQ0_LEUGJ 
ID   J9YEQ0_LEUGJ            Unreviewed;       214 AA.
AC   J9YEQ0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   26-FEB-2020, entry version 44.
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:AFS39797.1};
GN   OrderedLocusNames=C269_01750 {ECO:0000313|EMBL:AFS39797.1};
OS   Leuconostoc gelidum (strain JB7).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=1229756 {ECO:0000313|EMBL:AFS39797.1, ECO:0000313|Proteomes:UP000006279};
RN   [1] {ECO:0000313|EMBL:AFS39797.1, ECO:0000313|Proteomes:UP000006279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB7 {ECO:0000313|EMBL:AFS39797.1,
RC   ECO:0000313|Proteomes:UP000006279};
RX   PubMed=23144409; DOI=10.1128/JB.01806-12;
RA   Jung J.Y., Lee S.H., Jeon C.O.;
RT   "Complete genome sequence of Leuconostoc gelidum strain JB7, isolated from
RT   Kimchi.";
RL   J. Bacteriol. 194:6665-6665(2012).
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}.
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DR   EMBL; CP003839; AFS39797.1; -; Genomic_DNA.
DR   RefSeq; WP_010016432.1; NC_018631.1.
DR   STRING; 1229756.C269_01750; -.
DR   EnsemblBacteria; AFS39797; AFS39797; C269_01750.
DR   KEGG; lge:C269_01750; -.
DR   PATRIC; fig|1229756.3.peg.358; -.
DR   HOGENOM; CLU_049131_0_2_9; -.
DR   KO; K00943; -.
DR   OMA; FLYTADH; -.
DR   OrthoDB; 1585072at2; -.
DR   BioCyc; LGEL1229756:G1HAC-363-MONOMER; -.
DR   Proteomes; UP000006279; 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; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_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:AFS39797.1};
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, ECO:0000313|EMBL:AFS39797.1}.
FT   DOMAIN          9..199
FT                   /note="Thymidylate_kin"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   NP_BIND         11..18
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   214 AA;  23775 MW;  70D27D7864A03B4F CRC64;
     MTKPLFITFE GPEGAGKTSV LEILISELKP LLGGELITTR EPGGNPISEA IRAILQPAED
     NGMDERTEAL LYTAARRQHL VEIILPALKS GKVVISDRYI DSSLAYQGGG RGLGVDNIWQ
     INQFATEGLM PDLTIYFDVP PELGLARVKA NRQGKIDRLD KEDLSFHQTV RQTYLQLQHD
     FSDRIKLIDA AQPLDQVVAD TRALLLKTLK TRKE
//
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