KTHY_ECO45
ID KTHY_ECO45 Reviewed; 213 AA.
AC B7MJ85;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165};
DE EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165};
DE AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165};
GN Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165}; OrderedLocusNames=ECS88_1112;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000255|HAMAP-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:0000255|HAMAP-
CC Rule:MF_00165};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00165}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU928161; CAR02438.1; -; Genomic_DNA.
DR RefSeq; WP_001257012.1; NC_011742.1.
DR AlphaFoldDB; B7MJ85; -.
DR SMR; B7MJ85; -.
DR EnsemblBacteria; CAR02438; CAR02438; ECS88_1112.
DR KEGG; ecz:ECS88_1112; -.
DR HOGENOM; CLU_049131_0_1_6; -.
DR OMA; VMTREPG; -.
DR Proteomes; UP000000747; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
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; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..213
FT /note="Thymidylate kinase"
FT /id="PRO_1000190763"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ SEQUENCE 213 AA; 23702 MW; 6B8F0A7035525918 CRC64;
MRSKYIVIEG LEGAGKTTAR NVVVETLEQL GIRDMVFTRE PGGTQLAEKL RSLVLDIKSV
GDEVITDKAE VLMFYAARVQ LVETVIKPAL ANGTWVIGDR HDLSTQAYQG GGRGIDQHML
ATLRDAVLGG FRPDLTLYLD VTPEVGLKRA RARGELDRIE QESFDFFNRT RARYLELAAQ
DKSIHTIDAT QPLEAVMDAI RTTVTNWVKE LDA
