ID   KTHY_STRZP              Reviewed;         212 AA.
AC   C1CK20;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=SPP_0941;
OS   Streptococcus pneumoniae (strain P1031).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=488223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1031;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000920; ACO21241.1; -; Genomic_DNA.
DR   RefSeq; WP_000033388.1; NC_012467.1.
DR   AlphaFoldDB; C1CK20; -.
DR   SMR; C1CK20; -.
DR   KEGG; spp:SPP_0941; -.
DR   HOGENOM; CLU_049131_0_2_9; -.
DR   OMA; VMTREPG; -.
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..212
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_1000123594"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   212 AA;  23352 MW;  FE7B9816C474273E CRC64;
     MSKGFLVSLE GPEGAGKTSV LEALLPILEE KGVKVLTTRE PGGVLIGEKI REVILDPSHT
     QMDAKTELLL YIASRRQHLV EKVLPALEAG KLVIMDRFID SSVAYQGFGR GLDIEAIDWL
     NQFATDGLKP DLTLYFDIEV EEGLARIAAN SDREVNRLDL EGLDLHKKVR QGYLSLLDKE
     GNRIVKIDAS LPLEQVVETT KAVLFDGMGL AK