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Database: UniProt
Entry: A0A0M3RFT7_9BACI
LinkDB: A0A0M3RFT7_9BACI
Original site: A0A0M3RFT7_9BACI 
ID   A0A0M3RFT7_9BACI        Unreviewed;       211 AA.
AC   A0A0M3RFT7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   11-DEC-2019, entry version 17.
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   ORFNames=AM500_00715 {ECO:0000313|EMBL:ALC92596.1};
OS   Bacillus sp. FJAT-18017.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC92596.1, ECO:0000313|Proteomes:UP000060713};
RN   [1] {ECO:0000313|EMBL:ALC92596.1, ECO:0000313|Proteomes:UP000060713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC92596.1,
RC   ECO:0000313|Proteomes:UP000060713};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) 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: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; 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; CP012602; ALC92596.1; -; Genomic_DNA.
DR   RefSeq; WP_053601579.1; NZ_CP012602.1.
DR   EnsemblBacteria; ALC92596; ALC92596; AM500_00715.
DR   PATRIC; fig|1705566.3.peg.136; -.
DR   OrthoDB; 1585072at2; -.
DR   Proteomes; UP000060713; 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   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070206,
KW   ECO:0000313|EMBL:ALC92596.1};
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:UP000060713};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN          9..199
FT                   /note="Thymidylate_kin"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   NP_BIND         11..18
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   211 AA;  24160 MW;  31AAD7F768F9D5F7 CRC64;
     MVKGLFITIE GPEGAGKSTV ALMVAEHLKK CGYDALITRE PGGIDIAEQI RKVILEPKNI
     AMDPRTEALL YAAARRQHLM EKVRPALEKG RIVICDRFID SSLAYQGYAR GLGIEEVYKI
     NQFAIETMMP DLTIYFDIEP QEGLERIAKH KDREINRLDL EELSFHSKVR EGYLILLERF
     PDRIKRVDAS LELEDVFRSV KTIIETFLPQ K
//
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