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Database: UniProt
Entry: N0AUT9_9BACI
LinkDB: N0AUT9_9BACI
Original site: N0AUT9_9BACI 
ID   N0AUT9_9BACI            Unreviewed;       208 AA.
AC   N0AUT9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   08-MAY-2019, entry version 34.
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:AGK51810.1};
GN   ORFNames=B1NLA3E_00130 {ECO:0000313|EMBL:AGK51810.1};
OS   Bacillus sp. 1NLA3E.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK51810.1, ECO:0000313|Proteomes:UP000013300};
RN   [1] {ECO:0000313|EMBL:AGK51810.1, ECO:0000313|Proteomes:UP000013300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1NLA3E {ECO:0000313|EMBL:AGK51810.1};
RX   PubMed=23833140;
RA   Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A.,
RA   Watson D., Brooks S., Kostka J.E., Green S.J.;
RT   "Genome sequences for three denitrifying bacterial strains isolated
RT   from a uranium- and nitrate-contaminated subsurface environment.";
RL   Genome Announc. 1:e00449-13(2013).
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; CP005586; AGK51810.1; -; Genomic_DNA.
DR   RefSeq; WP_015591877.1; NC_021171.1.
DR   STRING; 666686.B1NLA3E_00130; -.
DR   EnsemblBacteria; AGK51810; AGK51810; B1NLA3E_00130.
DR   KEGG; baci:B1NLA3E_00130; -.
DR   KO; K00943; -.
DR   OrthoDB; 1585072at2; -.
DR   BioCyc; BSP666686:G1H2R-38-MONOMER; -.
DR   Proteomes; UP000013300; 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:UP000013300};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:AGK51810.1};
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:UP000013300};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:AGK51810.1}.
FT   DOMAIN        9    199       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      11     18       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   208 AA;  23501 MW;  12882766375BE4F0 CRC64;
     MGKGVFITIE GPEGAGKTTI INMLAQHLES VGYPVMQTRE PGGIEIAEQI REVILATENT
     AMDPRTEALL YAAARRQHLI EKVKPALESG AVILCDRFID SSLAYQGYAR GLGIDEVYTI
     NEFAIEDMMP KLTLYFDIDP EQGLKRINQH KGREVNRLDL ETIDFHQKVR EGYQLLITRF
     PKRIQLIDAS KSVESVFNQA LIKIREIL
//
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