UniProt functional annotation for P0A9J8

UniProt code: P0A9J8.

Organism: Escherichia coli (strain K12).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
 
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. {ECO:0000269|PubMed:4261395}.
 
Catalytic activity: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:4261395};
Catalytic activity: Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O; Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51; Evidence={ECO:0000269|PubMed:4261395};
Activity regulation: Both activities are inhibited by L-phenylalanine. {ECO:0000269|PubMed:4261395}.
Biophysicochemical properties: Kinetic parameters: KM=45 uM for chorismate (at pH 7.8 and at 37 degrees Celsius) {ECO:0000269|PubMed:4261395}; KM=1.0 mM for prephenate (at pH 7.8 and at 37 degrees Celsius) {ECO:0000269|PubMed:4261395}; KM=147 uM for chorismate (at pH 4.9) {ECO:0000269|Ref.8}; KM=296 uM for chorismate (at pH 7.5) {ECO:0000269|Ref.8}; Note=kcat is 72 sec(-1) at pH 7.5. kcat is 31 sec(-1) at pH 4.9. {ECO:0000269|Ref.8}; pH dependence: Optimum pH is 7.3 for chorismate mutase activity. {ECO:0000269|PubMed:4261395};
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1. {ECO:0000305}.
Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. {ECO:0000305}.
Subunit: Homodimer. {ECO:0000269|Ref.10}.
Subcellular location: Cytoplasm {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.