UniProt functional annotation for P0A7E9

UniProt code: P0A7E9.

Organism: Escherichia coli (strain K12).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
 
Function: Catalyzes the reversible phosphorylation of UMP to UDP, with ATP as the most efficient phosphate donor. {ECO:0000269|PubMed:7711027}.
 
Catalytic activity: Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.22;
Activity regulation: Allosterically activated by GTP. Competitively inhibited by magnesium-free UTP. Magnesium-bound UTP is unable to inhibit enzyme activity. {ECO:0000269|PubMed:15857829, ECO:0000269|PubMed:17210578}.
Biophysicochemical properties: Kinetic parameters: KM=120 uM for ATP {ECO:0000269|PubMed:7711027}; KM=50 uM for UMP {ECO:0000269|PubMed:7711027}; Vmax=96 umol/min/mg enzyme {ECO:0000269|PubMed:7711027};
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subunit: Homohexamer. {ECO:0000269|PubMed:15857829, ECO:0000269|PubMed:7711027}.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9922246}. Note=Is predominantly localized near the bacterial membranes.
Miscellaneous: The peripheral distribution of PyrH is related most probably to its role in the synthesis of membrane sugar components.
Similarity: Belongs to the UMP kinase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.