ID   KTHY_RICPR              Reviewed;         203 AA.
AC   Q9ZCN9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=tmk; OrderedLocusNames=RP684;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235272; CAA15121.1; -; Genomic_DNA.
DR   PIR; G71674; G71674.
DR   RefSeq; NP_221045.1; NC_000963.1.
DR   RefSeq; WP_004596365.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCN9; -.
DR   SMR; Q9ZCN9; -.
DR   STRING; 272947.RP684; -.
DR   EnsemblBacteria; CAA15121; CAA15121; CAA15121.
DR   GeneID; 57569809; -.
DR   KEGG; rpr:RP684; -.
DR   PATRIC; fig|272947.5.peg.706; -.
DR   eggNOG; COG0125; Bacteria.
DR   HOGENOM; CLU_049131_0_2_5; -.
DR   OMA; VMTREPG; -.
DR   Proteomes; UP000002480; 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_0000155331"
FT   BINDING         14..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   203 AA;  23375 MW;  5248DCB79759704A CRC64;
     MNKLTQGKFI TFEGVDGIGK STQSKMLYEY LKSQKIPVIL TREVGGTTVA EKMREILVNE
     ELLPMSELLQ AMAARYDHMA RKIIPALKDG YIVICDRFID STACYQGLEL ENGIDLVYSL
     HKTLMPSLMP DITFFIDVEP HTAIKRVNAR NMSNKFDIRS IDFYKKIYTC FKELSNRFPE
     RIKTIKASHL SPLEVHELIQ KHL