CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.2330 | arginine biosynthesis bifunctional protein fold |
|
3.30.2330.10 | arginine biosynthesis bifunctional protein suprefamily |
Domain Context
CATH Clusters
| Superfamily | arginine biosynthesis bifunctional protein suprefamily |
| Functional Family | Arginine biosynthesis bifunctional protein ArgJ |
Enzyme Information
| 2.3.1.1 |
Amino-acid N-acetyltransferase.
based on mapping to UniProt P9WPZ3
Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
-!- Also acts with L-aspartate and, more slowly, with some other amino acids.
|
| 2.3.1.35 |
Glutamate N-acetyltransferase.
based on mapping to UniProt P9WPZ3
N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L- glutamate.
-!- Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity.
|
UniProtKB Entries (1)
| P9WPZ3 |
ARGJ_MYCTU
Mycobacterium tuberculosis H37Rv
Arginine biosynthesis bifunctional protein ArgJ
|
PDB Structure
| PDB | 3IT6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The molecular structure of ornithine acetyltransferase from Mycobacterium tuberculosis bound to ornithine, a competitive inhibitor.
J.Mol.Biol.
|
