ID   KTHY_FINM2              Reviewed;         203 AA.
AC   B0S2F7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=FMG_1129;
OS   Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS   (Peptostreptococcus magnus).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=334413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX   PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA   Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA   Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT   "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT   pathogen.";
RL   DNA Res. 15:39-47(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; AP008971; BAG08547.1; -; Genomic_DNA.
DR   RefSeq; WP_012290847.1; NC_010376.1.
DR   AlphaFoldDB; B0S2F7; -.
DR   SMR; B0S2F7; -.
DR   STRING; 334413.FMG_1129; -.
DR   EnsemblBacteria; BAG08547; BAG08547; FMG_1129.
DR   KEGG; fma:FMG_1129; -.
DR   eggNOG; COG0125; Bacteria.
DR   HOGENOM; CLU_049131_0_2_9; -.
DR   OMA; VMTREPG; -.
DR   OrthoDB; 1585072at2; -.
DR   Proteomes; UP000001319; 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   Reference proteome; Transferase.
FT   CHAIN           1..203
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_1000097395"
FT   BINDING         7..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   203 AA;  23056 MW;  2312837C52433CF5 CRC64;
     MFITFEGPDG SGKSTIIQKV YDYLIENNYD VIKTREPGGS PIAEKIRNLI LDTENIKMGY
     RTEALLYAAS RAQHVEETIL PALNENKIVL CDRFLISSLA YQGVGRGLGI ENVRNINEFA
     INGVFPDFVL FFDVDPITTL KRKSSLDTAD RLEKEGNNFH ERVYNGYKEI LNSEKNIEII
     DATQSVEDVF SQCIEVLKRR NVL