| UniProt functional annotation for P0A720 | |||
| UniProt code: P0A720. |
| Organism: | Escherichia coli (strain K12). | |
| Taxonomy: | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. | |
| Function: | Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. | |
| Catalytic activity: | Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; | |
| Biophysicochemical properties: | Kinetic parameters: KM=0.04 mM for ATP (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:11369858}; KM=15 uM for dTMP (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:11369858}; Vmax=50 umol/min/mg enzyme with ATP and dTMP as substrates (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:11369858}; | |
| Pathway: | Pyrimidine metabolism; dTTP biosynthesis. | |
| Subunit: | Homodimer. | |
| Domain: | The LID domain is a solvent-exposed domain that closes over the site of phosphoryl transfer upon ATP binding. | |
| Similarity: | Belongs to the thymidylate kinase family. {ECO:0000305}. | |
| Sequence caution: | Sequence=L01483; Type=Frameshift; Evidence={ECO:0000305}; | |
Annotations taken from UniProtKB at the EBI.