ID A0A0P0G951_9BACT Unreviewed; 223 AA.
AC A0A0P0G951;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 13-NOV-2019, entry version 18.
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:ALJ56207.1};
GN ORFNames=AMD24_00003 {ECO:0000313|EMBL:ALJ56207.1};
OS Candidatus Xiphinematobacter sp. Idaho Grape.
OC Bacteria; Verrucomicrobia; Spartobacteria;
OC Candidatus Xiphinematobacter;
OC unclassified Candidatus Xiphinematobacter.
OX NCBI_TaxID=1704307 {ECO:0000313|EMBL:ALJ56207.1};
RN [1] {ECO:0000313|EMBL:ALJ56207.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Idaho Grape {ECO:0000313|EMBL:ALJ56207.1};
RX PubMed=26362082; DOI=10.1093/gbe/evv176;
RA Brown A.M., Howe D.K., Wasala S.K., Peetz A.B., Zasada I.A.,
RA Denver D.R.;
RT "Comparative Genomics of a Plant-Parasitic Nematode Endosymbiont
RT Suggest a Role in Nutritional Symbiosis.";
RL Genome Biol. Evol. 7:2727-2746(2015).
RN [2] {ECO:0000313|EMBL:ALJ56207.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Idaho Grape {ECO:0000313|EMBL:ALJ56207.1};
RG Swine Surveillance;
RL Submitted (SEP-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; CP012665; ALJ56207.1; -; Genomic_DNA.
DR RefSeq; WP_062100118.1; NZ_CP012665.1.
DR EnsemblBacteria; ALJ56207; ALJ56207; AMD24_00003.
DR KEGG; xii:AMD24_00003; -.
DR PATRIC; fig|1704307.3.peg.3; -.
DR KO; K00943; -.
DR OrthoDB; 1585072at2; -.
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 Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:ALJ56207.1};
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:ALJ56207.1}.
FT DOMAIN 17 211 Thymidylate_kin. {ECO:0000259|Pfam:
FT PF02223}.
FT NP_BIND 19 26 ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ SEQUENCE 223 AA; 24731 MW; 6673861FE76C5E42 CRC64;
MYSHCSAVRP RGIFISFEGP EGCGKTTQIQ KLARVFQGCD RSFLVLREPG GTALGESVRH
LLKYATTAGP SNLSPEAELL LFAASRAQLV REKILPALLA GSFVVCDRFL DSTTVYQGTA
RNLPHNFVKY VNQQVVSGCI PDITFLLDID SELALQRISR RGTHVLDRIE QESLQFHTLV
RKGYLELAQA NPGRFIVLDA EQSADSLSKK IVMTLEERYG PFS
//