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Entry: A0A0A8H460_9PROT
LinkDB: A0A0A8H460_9PROT
Original site: A0A0A8H460_9PROT 
ID   A0A0A8H460_9PROT        Unreviewed;       194 AA.
AC   A0A0A8H460;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   13-NOV-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:AJC87689.1};
GN   ORFNames=CINS_0720 {ECO:0000313|EMBL:AJC87689.1};
OS   Campylobacter insulaenigrae NCTC 12927.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=1031564 {ECO:0000313|EMBL:AJC87689.1, ECO:0000313|Proteomes:UP000031163};
RN   [1] {ECO:0000313|EMBL:AJC87689.1, ECO:0000313|Proteomes:UP000031163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 12927 {ECO:0000313|EMBL:AJC87689.1,
RC   ECO:0000313|Proteomes:UP000031163};
RX   PubMed=25381664; DOI=10.1093/gbe/evu249;
RA   Miller W.G., Yee E., Chapman M.H., Smith T.P., Bono J.L., Huynh S.,
RA   Parker C.T., Vandamme P., Luong K., Korlach J.;
RT   "Comparative Genomics of the Campylobacter lari Group.";
RL   Genome Biol. Evol. 6:3252-3266(2014).
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; CP007770; AJC87689.1; -; Genomic_DNA.
DR   RefSeq; WP_039649911.1; NZ_CP007770.1.
DR   EnsemblBacteria; AJC87689; AJC87689; CINS_0720.
DR   KEGG; cis:CINS_0720; -.
DR   KO; K00943; -.
DR   OrthoDB; 1585072at2; -.
DR   Proteomes; UP000031163; 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; 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:UP000031163};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:AJC87689.1};
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, ECO:0000313|EMBL:AJC87689.1}.
FT   DOMAIN        5    188       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND       7     14       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   194 AA;  22296 MW;  1021DDAF73939A9C CRC64;
     MYVAIEGIDC VGKSTQIEIL KKSFKDAIFT KEPGATKLGE KVRELLLQSE VKISKKAELL
     LFLADRANHI DLVLSQYKNK LIISDRSFIS GIAYARNEFN KETLFDLNFF ATSGNFPNKV
     VFLHANKELI GERLASKKLD TIEKRGIKYF LEIQDELENT LNFLKDKIDF EILKLDASFS
     IQDIHKQIKE FIDD
//
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