ID   KTHY_NEIMA              Reviewed;         206 AA.
AC   Q9JVE7; A1IQS1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=tmk; OrderedLocusNames=NMA0869;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000250}.
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;
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR   EMBL; AL157959; CAM08105.1; -; Genomic_DNA.
DR   PIR; H81932; H81932.
DR   RefSeq; WP_002214191.1; NC_003116.1.
DR   AlphaFoldDB; Q9JVE7; -.
DR   SMR; Q9JVE7; -.
DR   EnsemblBacteria; CAM08105; CAM08105; NMA0869.
DR   KEGG; nma:NMA0869; -.
DR   HOGENOM; CLU_049131_0_2_4; -.
DR   OMA; VMTREPG; -.
DR   BioCyc; NMEN122587:NMA_RS04365-MON; -.
DR   Proteomes; UP000000626; 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   Transferase.
FT   CHAIN           1..206
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000155311"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   206 AA;  23028 MW;  FC36374225FFDF5D CRC64;
     MKPQFITLDG IDGAGKSTNL AVIKAWFERR GLPVLFTREP GGTPVGEALR EILLNPETKA
     GLRAETLMMF AARMQHIEDV ILPALSDGIH VVSDRFTDAT FAYQGGGRGM PSEDIEILEH
     WVQGGLRPDL TLLLDVPLEV SMARIGQTRE KDRFEQEQAD FFMRVRSVYL NRAAACPERY
     AVIDSNLGLD EVRNSIEKVL DRHFGC