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Database: UniProt
Entry: A0A0B5D1C7_9CORY
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ID   A0A0B5D1C7_9CORY        Unreviewed;       203 AA.
AC   A0A0B5D1C7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   31-JUL-2019, entry version 25.
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=B842_02790 {ECO:0000313|EMBL:AJE32411.1};
OS   Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE32411.1, ECO:0000313|Proteomes:UP000031524};
RN   [1] {ECO:0000313|EMBL:AJE32411.1, ECO:0000313|Proteomes:UP000031524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium humireducens DSM
RT   45392(T), isolated from a wastewater-fed microbial fuel cell.";
RL   Submitted (APR-2013) 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-
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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00165}.
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DR   EMBL; CP005286; AJE32411.1; -; Genomic_DNA.
DR   RefSeq; WP_040085079.1; NZ_CP005286.1.
DR   EnsemblBacteria; AJE32411; AJE32411; B842_02790.
DR   KEGG; chm:B842_02790; -.
DR   KO; K00943; -.
DR   OrthoDB; 1585072at2; -.
DR   Proteomes; UP000031524; 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   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:UP000031524};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:AJE32411.1};
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:AJE32411.1}.
FT   DOMAIN        5    181       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   REGION      135    159       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   203 AA;  22657 MW;  9D1A0D3AE955C76A CRC64;
     MIIAIEGIDG AGKNTLTRAI RERVDADMLA FPRYETSVPA QLVQEALHGR MGDLTDSAYA
     MATLFALDRH GAREQLAPYV DSDRIILLDR YVASNAAYSV ARLRDATVAD WVHDLEFGRL
     GLPQPDLQVL LATEPETASQ RAAQREAQDA SRERDRYERD ADLQQRTYDA YLGLAERSWA
     GRWLVTTSAD VVLQEIAHIT QGL
//
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