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Database: UniProt
Entry: A0A0A8B996_9ACTN
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ID   A0A0A8B996_9ACTN        Unreviewed;       244 AA.
AC   A0A0A8B996;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   08-MAY-2019, entry version 23.
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=JI75_02320 {ECO:0000313|EMBL:AJC11687.1};
OS   Coriobacteriaceae bacterium 68-1-3.
OC   Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae.
OX   NCBI_TaxID=1531429 {ECO:0000313|EMBL:AJC11687.1};
RN   [1] {ECO:0000313|EMBL:AJC11687.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68-1-3 {ECO:0000313|EMBL:AJC11687.1};
RX   PubMed=26450725;
RA   Looft T., Bayles D.O., Alt D.P., Stanton T.B.;
RT   "Complete Genome Sequence of Coriobacteriaceae Strain 68-1-3, a Novel
RT   Mucus-Degrading Isolate from the Swine Intestinal Tract.";
RL   Genome Announc. 3:e01143-15(2015).
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; CP009302; AJC11687.1; -; Genomic_DNA.
DR   RefSeq; WP_039688419.1; NZ_CP009302.1.
DR   EnsemblBacteria; AJC11687; AJC11687; JI75_02320.
DR   KEGG; cbac:JI75_02320; -.
DR   KO; K00943; -.
DR   OrthoDB; 1585072at2; -.
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,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:AJC11687.1};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN       18    209       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      20     27       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   244 AA;  27197 MW;  5C6F6CCFCEECBABD CRC64;
     MSFDSHAETP GRGIFITFEG GDGAGKTTHI RFLAQHLREQ GREVVCLREP GGTPIGERLR
     DVVLDPACAE MSDRAELFVY EAARAQIVAE VIAPALERGA VVLCDRFCDS TVAYQAFGRG
     LPRAFVEQAN EFSTQGLVPD RTILMTTGER AQVGLERATR HHEADRMELA GLEFHERVME
     GFRSLAQSES DRVRIVVSAD RKSETSRMIF SELSDLFPWM GDDEVCGEDL FAPLDRARHE
     GRPR
//
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