KTHY_BIFLD
ID KTHY_BIFLD Reviewed; 206 AA.
AC B3DUA1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165};
DE EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165};
DE AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165};
GN Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165}; OrderedLocusNames=BLD_1275;
OS Bifidobacterium longum (strain DJO10A).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=205913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A;
RX PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT reveals loci susceptible to deletion during pure culture growth.";
RL BMC Genomics 9:247-247(2008).
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00165};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00165}.
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DR EMBL; CP000605; ACD98720.1; -; Genomic_DNA.
DR RefSeq; WP_010081362.1; NZ_AABM02000012.1.
DR AlphaFoldDB; B3DUA1; -.
DR SMR; B3DUA1; -.
DR EnsemblBacteria; ACD98720; ACD98720; BLD_1275.
DR KEGG; blj:BLD_1275; -.
DR HOGENOM; CLU_049131_0_0_11; -.
DR OMA; VMTREPG; -.
DR Proteomes; UP000002419; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
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; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..206
FT /note="Thymidylate kinase"
FT /id="PRO_1000097376"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ SEQUENCE 206 AA; 22547 MW; 3A337E8CDA8B716F CRC64;
MSGLFVSFEG VDGVGKTTQV ERLRAYLEAQ GRTVVVTREP GGTALGKAIR QLLLHGVDGG
AVDIAPRAEA LLFAADRAQH VAETIRPALE RGEVVITDRY LDSSLAYQAG GRELTPEEIR
SLSMWATNNL LPDRTYLLDM DPALSHNRLE HAEDRMESAG SDFQSRTRQA FLDLAAAEPN
RFRVIDASQS IEAVWAAIES DIKELA