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Database: UniProt
Entry: C7LSK1_DESBD
LinkDB: C7LSK1_DESBD
Original site: C7LSK1_DESBD 
ID   C7LSK1_DESBD            Unreviewed;       211 AA.
AC   C7LSK1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
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   OrderedLocusNames=Dbac_0085 {ECO:0000313|EMBL:ACU88215.1};
OS   Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378)
OS   (Desulfovibrio baculatus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfomicrobiaceae; Desulfomicrobium.
OX   NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU88215.1, ECO:0000313|Proteomes:UP000002216};
RN   [1] {ECO:0000313|EMBL:ACU88215.1, ECO:0000313|Proteomes:UP000002216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4028 / VKM B-1378 {ECO:0000313|Proteomes:UP000002216};
RX   PubMed=21304634; DOI=10.4056/sigs.13134;
RA   Copeland A., Spring S., Goker M., Schneider S., Lapidus A.,
RA   Del Rio T.G., Tice H., Cheng J.F., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavrommatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Meincke L., Sims D., Brettin T., Detter J.C., Han C.,
RA   Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lucas S.;
RT   "Complete genome sequence of Desulfomicrobium baculatum type strain
RT   (X).";
RL   Stand. Genomic Sci. 1:29-37(2009).
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; CP001629; ACU88215.1; -; Genomic_DNA.
DR   RefSeq; WP_012805300.1; NC_013173.1.
DR   STRING; 525897.Dbac_0085; -.
DR   EnsemblBacteria; ACU88215; ACU88215; Dbac_0085.
DR   KEGG; dba:Dbac_0085; -.
DR   eggNOG; ENOG4108ZMD; Bacteria.
DR   eggNOG; COG0125; LUCA.
DR   HOGENOM; HOG000229078; -.
DR   KO; K00943; -.
DR   OMA; FLYTADH; -.
DR   OrthoDB; 1585072at2; -.
DR   BioCyc; DBAC525897:G1GEX-86-MONOMER; -.
DR   Proteomes; UP000002216; 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:UP000002216};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:ACU88215.1};
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:UP000002216};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:ACU88215.1}.
FT   DOMAIN        5    201       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND       7     14       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   211 AA;  23681 MW;  9B979C4754108055 CRC64;
     MFLTFEGMEG CGKSTQCKKL IEHFVRQGHD VLHTLEPGGS RLGKELRRIL LDPKNSDLSS
     TSELFLYLAD RAQHVSSVIR PAMEDGRTVI CDRFADSTVV YQGYGRGLDP SLLHHLNDVA
     VQGLWPDMTI LLDVEPEIGL RRALTRNMQD NKTATEGRFE AESMAFHTRI REGYLTWAAL
     HRGRFLVVDA GRNPDAVFDS ILRGLEEKGL G
//
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