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Database: UniProt
Entry: D3SM76_THEAH
LinkDB: D3SM76_THEAH
Original site: D3SM76_THEAH 
ID   D3SM76_THEAH            Unreviewed;       199 AA.
AC   D3SM76;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
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   OrderedLocusNames=Thal_1224 {ECO:0000313|EMBL:ADC89856.1};
OS   Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX   NCBI_TaxID=638303 {ECO:0000313|EMBL:ADC89856.1, ECO:0000313|Proteomes:UP000002043};
RN   [1] {ECO:0000313|Proteomes:UP000002043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14484 / JCM 11386 / HI 11/12
RC   {ECO:0000313|Proteomes:UP000002043};
RX   DOI=10.4056/sigs.761490;
RA   Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., Copeland A.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., Anderson I.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA   Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Thermocrinis albus type strain (HI 11/12T).";
RL   Stand. Genomic Sci. 2:194-202(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; CP001931; ADC89856.1; -; Genomic_DNA.
DR   RefSeq; WP_012992262.1; NC_013894.1.
DR   AlphaFoldDB; D3SM76; -.
DR   STRING; 638303.Thal_1224; -.
DR   KEGG; tal:Thal_1224; -.
DR   eggNOG; COG0125; Bacteria.
DR   HOGENOM; CLU_049131_0_2_0; -.
DR   OrthoDB; 9774907at2; -.
DR   Proteomes; UP000002043; 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:ADC89856.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00165}; Reference proteome {ECO:0000313|Proteomes:UP000002043};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:ADC89856.1}.
FT   DOMAIN          5..186
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   BINDING         7..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   199 AA;  22593 MW;  29C7784B6D965E3D CRC64;
     MLISIEGIDG SGKTTVAHAL VDFLQKEGYP AVLFKDPGDT PLAEEIRSLL FKYEMDPITE
     LLLFEAARSS LTWEKILPAL SEGKIVILDR FIDSTVAYQG YGREINLGTV SILNHIATRG
     IKPNLTLLLN VPLHVALSRL SDRSRFEREE YLRKVRDAYI LLAHQEKERI KIVDASRSFE
     EVFEEVKTEV LSVLYNKET
//
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