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Database: UniProt
Entry: S0FZS8_9DELT
LinkDB: S0FZS8_9DELT
Original site: S0FZS8_9DELT 
ID   S0FZS8_9DELT            Unreviewed;       209 AA.
AC   S0FZS8;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   08-MAY-2019, entry version 29.
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:EMS78479.1};
GN   ORFNames=Dpo_3c03090 {ECO:0000313|EMBL:EMS80165.1}, Dpo_8c01460
GN   {ECO:0000313|EMBL:EMS78479.1};
OS   Desulfotignum phosphitoxidans DSM 13687.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfotignum.
OX   NCBI_TaxID=1286635 {ECO:0000313|EMBL:EMS80165.1, ECO:0000313|Proteomes:UP000014216};
RN   [1] {ECO:0000313|EMBL:EMS80165.1, ECO:0000313|Proteomes:UP000014216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13687 {ECO:0000313|EMBL:EMS80165.1,
RC   ECO:0000313|Proteomes:UP000014216};
RX   PubMed=23704177;
RA   Poehlein A., Daniel R., Simeonova D.D.;
RT   "Draft Genome Sequence of Desulfotignum phosphitoxidans DSM 13687
RT   Strain FiPS-3.";
RL   Genome Announc. 1:E00227-13(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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EMS80165.1}.
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DR   EMBL; APJX01000008; EMS78479.1; -; Genomic_DNA.
DR   EMBL; APJX01000003; EMS80165.1; -; Genomic_DNA.
DR   RefSeq; WP_006965505.1; NZ_APJX01000008.1.
DR   EnsemblBacteria; EMS78479; EMS78479; Dpo_8c01460.
DR   EnsemblBacteria; EMS80165; EMS80165; Dpo_3c03090.
DR   PATRIC; fig|1286635.3.peg.1874; -.
DR   Proteomes; UP000014216; Unassembled WGS sequence.
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; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_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:UP000014216};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:EMS80165.1};
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:UP000014216};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:EMS80165.1}.
FT   DOMAIN        9    198       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      11     18       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   209 AA;  23472 MW;  4170A635B81B4339 CRC64;
     MKTGRFVVFE GLDGSGKTTQ MARVQQRLTH MGIGADTTCE PTDGPVGTLI RQILEGRVSM
     DPRTLAALFA ADRTDHLVAP DTGVKALMEK GRTVLCDRYY FSSYAYHAMD MDLEWVMTLN
     AVNAQILKPD LTLFIDVAPN TCLERIRAGR THLDLFEKID ILTRVRDNYF AAFERLKDQE
     TVKVVDGNAS EDAVEQAIWH GISHMFTKE
//
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