IPR042195
ArgJ beta chain, C-terminal domain
InterPro entry
Short name | ArgJ_beta_C |
Overlapping entries |
Description
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.
References
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. Sakanyan V, Charlier D, Legrain C, Kochikyan A, Mett I, Pierard A, Glansdorff N. J. Gen. Microbiol. 139, 393-402, (1993). PMID: 8473852
2.X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster. Elkins JM, Kershaw NJ, Schofield CJ. Biochem. J. 385, 565-73, (2005). View articlePMID: 15352873
Cross References
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.10.20.340