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Database: UniProt
Entry: F2NM34_MARHT
LinkDB: F2NM34_MARHT
Original site: F2NM34_MARHT 
ID   F2NM34_MARHT            Unreviewed;       202 AA.
AC   F2NM34;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   08-MAY-2019, entry version 46.
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=Marky_0754 {ECO:0000313|EMBL:AEB11504.1};
OS   Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Marinithermus.
OX   NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB11504.1, ECO:0000313|Proteomes:UP000007030};
RN   [1] {ECO:0000313|EMBL:AEB11504.1, ECO:0000313|Proteomes:UP000007030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX   PubMed=22675595; DOI=10.4056/sigs.2435521;
RA   Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA   Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Pan C., Brambilla E.M., Rohde M.,
RA   Tindall B.J., Sikorski J., Goker M., Detter J.C., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Woyke T.;
RT   "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT   hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT   chimney.";
RL   Stand. Genomic Sci. 6:21-30(2012).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-
CC       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:0000256|HAMAP-
CC         Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070220}.
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DR   EMBL; CP002630; AEB11504.1; -; Genomic_DNA.
DR   RefSeq; WP_013703556.1; NC_015387.1.
DR   STRING; 869210.Marky_0754; -.
DR   EnsemblBacteria; AEB11504; AEB11504; Marky_0754.
DR   KEGG; mhd:Marky_0754; -.
DR   eggNOG; ENOG4108ZMD; Bacteria.
DR   eggNOG; COG0125; LUCA.
DR   KO; K00943; -.
DR   OMA; FLYTADH; -.
DR   OrthoDB; 1585072at2; -.
DR   BioCyc; MHYD869210:G1GSR-771-MONOMER; -.
DR   Proteomes; UP000007030; 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   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 {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007030};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:AEB11504.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070211};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070205};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007030};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:AEB11504.1}.
FT   DOMAIN        9    191       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      11     18       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   202 AA;  22766 MW;  DF57CA6ECA33F183 CRC64;
     MKPGFFITFE GPEGSGKSTQ AAHLAAWLRQ QGVSVVVTRE PGGTPLGRAV RQWLLSESMD
     PVTEFLLYTA DRAEHVRHVI RPALAAGQVV ISDRFVDSSY AYQGFGRGLD LEWLRAVSQP
     VLEGLVPDVT FLLDLPPEVG LARKAERDRL EQESLAFHRR VREGYRVLAR AEPQRFVVLD
     ATQPPEVIVE QVRIEVQRRW RA
//
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