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Database: UniProt
Entry: A0A2A2HQ80_9GAMM
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ID   A0A2A2HQ80_9GAMM        Unreviewed;       211 AA.
AC   A0A2A2HQ80;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-NOV-2019, entry version 10.
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=CBG25_00030 {ECO:0000313|EMBL:PAV11649.1};
OS   Arsenophonus sp. ENCA.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Arsenophonus; unclassified Arsenophonus.
OX   NCBI_TaxID=1987579 {ECO:0000313|EMBL:PAV11649.1, ECO:0000313|Proteomes:UP000217542};
RN   [1] {ECO:0000313|EMBL:PAV11649.1, ECO:0000313|Proteomes:UP000217542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ENCA {ECO:0000313|EMBL:PAV11649.1};
RX   PubMed=28854637; DOI=10.1093/gbe/evx134;
RA   Mao M., Yang X., Poff K., Bennett G.;
RT   "Comparative Genomics of the Dual-Obligate Symbionts from the
RT   Treehopper, Entylia carinata (Hemiptera: Membracidae), Provide Insight
RT   into the Origins and Evolution of an Ancient Symbiosis.";
RL   Genome Biol. Evol. 9:1803-1815(2017).
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: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PAV11649.1}.
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DR   EMBL; NHNG01000001; PAV11649.1; -; Genomic_DNA.
DR   Proteomes; UP000217542; Unassembled WGS sequence.
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:UP000217542};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:PAV11649.1};
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:UP000217542};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN        8    198       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      10     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   211 AA;  23703 MW;  B11D964123A875F4 CRC64;
     MKSRYIVIEG LEGAGKTTAI KTVVETLAKV GITEIDFTRE PGGTPLAEKL RQLIKHGIAE
     EKVTDKAELL MLYAARIQLI ENVIKPALAK GRWVIGDRHD LSSQAYQGGG RGLSAELMQV
     LRNTILGDFR PDLTLYLDIE PTLGLQRARD RGELDRIEKE SLDFFERTRQ RYLELAAEDD
     TIITIDANKS LEEVQKTIRQ TLSNWLVAQG K
//
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