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Database: UniProt
Entry: E3D8F9_GARV3
LinkDB: E3D8F9_GARV3
Original site: E3D8F9_GARV3 
ID   E3D8F9_GARV3            Unreviewed;       233 AA.
AC   E3D8F9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Thymidylate kinase {ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165,
GN   ECO:0000313|EMBL:ADP38353.1};
GN   OrderedLocusNames=HMPREF0421_20269 {ECO:0000313|EMBL:ADP38353.1};
OS   Gardnerella vaginalis (strain ATCC 14019 / 317).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Gardnerella.
OX   NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP38353.1, ECO:0000313|Proteomes:UP000001453};
RN   [1] {ECO:0000313|EMBL:ADP38353.1, ECO:0000313|Proteomes:UP000001453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX   PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA   Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA   Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA   Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA   Wilson B.A.;
RT   "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT   differences in metabolic and virulence potential.";
RL   PLoS ONE 5:E12411-E12411(2010).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001008, ECO:0000256|HAMAP-
CC         Rule:MF_00165};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00009776, ECO:0000256|HAMAP-Rule:MF_00165}.
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DR   EMBL; CP002104; ADP38353.1; -; Genomic_DNA.
DR   RefSeq; WP_004118180.1; NC_014644.1.
DR   RefSeq; YP_003985376.1; NC_014644.1.
DR   AlphaFoldDB; E3D8F9; -.
DR   KEGG; gvg:HMPREF0421_20269; -.
DR   PATRIC; fig|525284.18.peg.264; -.
DR   HOGENOM; CLU_049131_0_0_11; -.
DR   OrthoDB; 9774907at2; -.
DR   Proteomes; UP000001453; 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   CDD; cd01672; TMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00041; DTMP_kinase; 1.
DR   PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR   PANTHER; PTHR10344:SF4; THYMIDYLATE KINASE; 1.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00165};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:ADP38353.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00165};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:ADP38353.1}.
FT   DOMAIN          21..204
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   233 AA;  25362 MW;  64BE8EAF701F17A8 CRC64;
     MAIGLKNSGL SGLNKGLFIS FEGIDGVGKT TQVEALRDFL QARGLEVVVT REPGGTPLGE
     QLRNILLHGG AISARTEALL FAADRAQHAA QIIIPALRRG AVVITDRYID SSLAYQSGGR
     ELTMQDVRDL SEWASNCLWP NRTYLLDMSE KDAAVRLHGQ ADRMESAGLD FARRTREAFL
     DLAKQNAQRF CVLDATLPAC DLSKLIAKDM CELMDNAGIG DKKSPEAPEN QGF
//
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