ID   KTHY_GEODF              Reviewed;         214 AA.
AC   B9M910;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-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=Geob_2152;
OS   Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS   daltonii).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=316067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22248 / JCM 15807 / FRC-32;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kostka J., Richardson P.;
RT   "Complete sequence of Geobacter sp. FRC-32.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001390; ACM20506.1; -; Genomic_DNA.
DR   RefSeq; WP_012647235.1; NC_011979.1.
DR   AlphaFoldDB; B9M910; -.
DR   SMR; B9M910; -.
DR   STRING; 316067.Geob_2152; -.
DR   EnsemblBacteria; ACM20506; ACM20506; Geob_2152.
DR   KEGG; geo:Geob_2152; -.
DR   eggNOG; COG0125; Bacteria.
DR   HOGENOM; CLU_049131_0_2_7; -.
DR   OMA; VMTREPG; -.
DR   OrthoDB; 1585072at2; -.
DR   Proteomes; UP000007721; 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   Reference proteome; Transferase.
FT   CHAIN           1..214
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_1000123574"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   214 AA;  23134 MW;  20FF43C1FF5867A5 CRC64;
     MGCFITFEGI EGCGKTTQIK LLEQHLAEKG FKVLLTREPG GCPIADQIRA ILLDAANSAM
     TPSAELLLYA AARAQHVEEV IKPALADDCI VLCDRFTDAT VAYQGYGRGL DLDSIGYLNQ
     LATSGLKPQL TILLDCPVEV GLKRALARIN GISAGAREER FELESTLFHQ KVRNGYLKLA
     ENEKGRFLIV DGGTNVDETR VAVTTAVIGR LNGN