UniProt functional annotation for P0DJQ5

UniProt codes: P0DJQ5, Q53940.

Organism: Streptomyces clavuligerus.
Taxonomy: Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; Streptomyces.
 
Function: Catalyzes the biosynthesis of ornithine by transacetylation between N(2)-acetylornithine and glutamate. It can also use L-arginine, L-glutamine and L-lysine as acetyl acceptors. {ECO:0000269|PubMed:11985581}.
 
Catalytic activity: Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N- acetyl-L-glutamate; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=2.3.1.35; Evidence={ECO:0000269|PubMed:11985581};
Biophysicochemical properties: Kinetic parameters: KM=3.6 mM for L-N-acetylornithine (at 37 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:11985581}; Vmax=87 nmol/min/mg enzyme {ECO:0000269|PubMed:11985581}; pH dependence: Optimum pH is between 7.5-8. {ECO:0000269|PubMed:11985581};
Pathway: Antibiotic biosynthesis; clavulanate biosynthesis.
Subunit: Heterotetramer of two alpha and two beta chains. {ECO:0000269|PubMed:11985581, ECO:0000269|PubMed:15352873, ECO:0000269|PubMed:19105697, ECO:0000269|PubMed:21796301, ECO:0000269|Ref.4}.
Subcellular location: Cytoplasm {ECO:0000250}.
Mass spectrometry: [Glutamate N-acetyltransferase 2 alpha chain]: Mass=18816.2; Method=Electrospray; Evidence={ECO:0000269|PubMed:11985581};
Mass spectrometry: [Glutamate N-acetyltransferase 2 beta chain]: Mass=22811.7; Method=Electrospray; Evidence={ECO:0000269|PubMed:11985581};
Miscellaneous: The role of this protein is probably directed towards producing increased intracellular concentrations of arginine for clavam biosynthesis, rather than primary metabolism. {ECO:0000305|PubMed:11985581}.
Similarity: Belongs to the ArgJ family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.