ID   KTHY_MYCAP              Reviewed;         215 AA.
AC   A5IZC6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=MAG6850;
OS   Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS   agalactiae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=347257;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX   PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA   Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA   Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA   Blanchard A., Citti C.;
RT   "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT   bacterial genome.";
RL   PLoS Genet. 3:744-758(2007).
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; CU179680; CAL59385.1; -; Genomic_DNA.
DR   RefSeq; WP_011949838.1; NC_009497.1.
DR   AlphaFoldDB; A5IZC6; -.
DR   SMR; A5IZC6; -.
DR   STRING; 347257.MAG6850; -.
DR   EnsemblBacteria; CAL59385; CAL59385; MAG6850.
DR   KEGG; maa:MAG6850; -.
DR   HOGENOM; CLU_049131_0_2_14; -.
DR   OMA; VMTREPG; -.
DR   Proteomes; UP000007065; 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; 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; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..215
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_1000097412"
FT   BINDING         7..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   215 AA;  24911 MW;  6BBFBFABDF14BE79 CRC64;
     MFITFEGLDG SGKTTIVQKL VEKLLEKKPA LSFIVTREPG GKNVRESEKI RELILDKESR
     LSPISEALLY TASRRIHIEK VILPALKENK LVLCDRYIDS FYAYQGIVRG LGLSFAKQLT
     EMVIESTIPD ITIFIDITAE QSEYRRNVSR LISDRLDSES LEFHKKVFDA YKEVINLDPK
     RFIIVNGLQS IPEILDEIVE KLFQNKKFDE WWKNN