ID   KTHY_LATSS              Reviewed;         214 AA.
AC   Q38YT6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=LCA_0340;
OS   Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS   subsp. sakei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Latilactobacillus.
OX   NCBI_TaxID=314315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23K;
RX   PubMed=16273110; DOI=10.1038/nbt1160;
RA   Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA   Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA   Zagorec M.;
RT   "The complete genome sequence of the meat-borne lactic acid bacterium
RT   Lactobacillus sakei 23K.";
RL   Nat. Biotechnol. 23:1527-1533(2005).
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; CR936503; CAI54641.1; -; Genomic_DNA.
DR   RefSeq; WP_011374049.1; NC_007576.1.
DR   AlphaFoldDB; Q38YT6; -.
DR   SMR; Q38YT6; -.
DR   STRING; 314315.LCA_0340; -.
DR   EnsemblBacteria; CAI54641; CAI54641; LCA_0340.
DR   KEGG; lsa:LCA_0340; -.
DR   eggNOG; COG0125; Bacteria.
DR   HOGENOM; CLU_049131_0_2_9; -.
DR   OMA; VMTREPG; -.
DR   OrthoDB; 1585072at2; -.
DR   BioCyc; LSAK314315:LCA_RS01615-MON; -.
DR   Proteomes; UP000002707; 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..214
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_1000071560"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   214 AA;  23637 MW;  5309BDF8A2EEDCB2 CRC64;
     MVGKLITFEG PDGAGKTSAL EAVVARLQKE VSQEIVVTRE PGGNPISEQI RQIILDVKNT
     AMDDRTEALL YAAARRQHIV EKIQPALAAD KLVICDRFVD SSIAYQGAGR GIGEEAVAQM
     NLFATDGLTP DLTLYLDVPS EVGLARIKQH RQNQYDRLDQ EKLAFHQKVR QSYLKLAQAH
     PDRIKTIDAS QPLEAVVTQC LQVIAQANLH LFEV