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Database: UniProt
Entry: A0A0S2HUH6_9BACT
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ID   A0A0S2HUH6_9BACT        Unreviewed;       231 AA.
AC   A0A0S2HUH6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   08-MAY-2019, entry version 15.
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:ALO13711.1};
GN   ORFNames=L21SP5_00029 {ECO:0000313|EMBL:ALO13711.1};
OS   Salinivirga cyanobacteriivorans.
OC   Bacteria; Bacteroidetes; Bacteroidia; Marinilabiliales;
OC   Salinivirgaceae; Salinivirga.
OX   NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO13711.1, ECO:0000313|Proteomes:UP000064893};
RN   [1] {ECO:0000313|EMBL:ALO13711.1, ECO:0000313|Proteomes:UP000064893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO13711.1,
RC   ECO:0000313|Proteomes:UP000064893};
RA   Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT   "Description and complete genome sequence of a novel strain
RT   predominating in hypersaline microbial mats and representing a new
RT   family of the Bacteriodetes phylum.";
RL   Submitted (NOV-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-
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; CP013118; ALO13711.1; -; Genomic_DNA.
DR   RefSeq; WP_057951350.1; NZ_CP013118.1.
DR   EnsemblBacteria; ALO13711; ALO13711; L21SP5_00029.
DR   KEGG; blq:L21SP5_00029; -.
DR   PATRIC; fig|1307839.3.peg.28; -.
DR   KO; K00943; -.
DR   OrthoDB; 1585072at2; -.
DR   Proteomes; UP000064893; 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   Complete proteome {ECO:0000313|Proteomes:UP000064893};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:ALO13711.1};
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:UP000064893};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:ALO13711.1}.
FT   DOMAIN        7    203       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND       9     16       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   231 AA;  26741 MW;  F18D1D452E96203E CRC64;
     MNKFIVLEGL DGSGKSTQVD LLKGFFDEQG INYKFLHFPQ TETPYFGEMI ARFLRGEFGP
     IDAVDPYLVA MLYAGDRYSA SNDIKEWLSI GTVVVVDRYV LSNIAFQCAK LTSEAEKEKL
     RNWIFQFEYN YYQIPKPGLS IFLDVPMNFV KHNLENERKG NDREYLQGKQ DIHEAKSSFQ
     EIVRKEYLEA IKLDSTFERL NCSENGEMKS ADDIFNEIHA LLIKYGIISH E
//
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