InterPro domain: IPR042195

ArgJ (also known as Ornithine acetyltransferase/OAT) is a bifunctional protein that catalyses the first 2.3.1.35 and fifth steps 2.3.1.1 in arginine biosynthesis [ 1 ], coupling acetylation of glutamate with deacetylation of N-acetylornithine, which allows recycling of the acetyl group in the arginine biosynthetic pathway. The structure has been determined for glutamate N-acetyltransferase 2 (ornithine acetyltransferase; 2.3.1.35 ), an ArgJ-like protein from Streptomyces clavuligerus [ 2 ].

When active, ArgJ is a heterotetramer of two alpha and two beta chains, where the alpha and beta chains are the result of autocatalytic cleavage.

This superfamily represents the C-terminal domain found in ArgJ beta chain.

1. Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase. J. Gen. Microbiol. 139, 393-402
2. X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster. Biochem. J. 385, 565-73