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Database: UniProt
Entry: E1QG97_DESB2
LinkDB: E1QG97_DESB2
Original site: E1QG97_DESB2 
ID   E1QG97_DESB2            Unreviewed;       226 AA.
AC   E1QG97;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   08-MAY-2019, entry version 49.
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=Deba_0232 {ECO:0000313|EMBL:ADK83609.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / VKM B-1802 /
OS   2st14).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK83609.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK83609.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Han C., Rohde M., Brambilla E., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain
RT   (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
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; CP002085; ADK83609.1; -; Genomic_DNA.
DR   RefSeq; WP_013257065.1; NC_014365.1.
DR   STRING; 644282.Deba_0232; -.
DR   EnsemblBacteria; ADK83609; ADK83609; Deba_0232.
DR   KEGG; dbr:Deba_0232; -.
DR   eggNOG; ENOG4108ZMD; Bacteria.
DR   eggNOG; COG0125; LUCA.
DR   HOGENOM; HOG000229078; -.
DR   KO; K00943; -.
DR   OMA; FLYTADH; -.
DR   OrthoDB; 1585072at2; -.
DR   BioCyc; DBAA644282:G1GM5-230-MONOMER; -.
DR   Proteomes; UP000009047; 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:UP000009047};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:ADK83609.1};
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:UP000009047};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:ADK83609.1}.
FT   DOMAIN       16    210       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      18     25       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   226 AA;  24771 MW;  6207AF88586E2FA9 CRC64;
     MSAKPAKTPR APFITLEGGE GCGKSTQASM LGRRIRGLGL KVVLTREPGG ASLGQTIREL
     LLGPGQEPVD PVTELLLFLA DRSHHVRAKI EPALLRGEVV VCDRFADSSE VYQGLARGLG
     LERVRRLNQW VCGQCWPDLT LLLDLNPGLG LARAAQRQGE LGQGPSPMEK EKLEFHERLR
     EGFLAQAQAE PGRIKPVDAA RPAEEVAEAI WAHVEPLLRE WRRCGL
//
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