CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.70 | L-amino peptidase D-ALA esterase/amidase |
|
3.60.70.12 | L-amino peptidase D-ALA esterase/amidase |
Domain Context
CATH Clusters
| Superfamily | L-amino peptidase D-ALA esterase/amidase |
| Functional Family |
Enzyme Information
| 2.3.1.35 |
Glutamate N-acetyltransferase.
based on mapping to UniProt Q9K8V3
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.
|
| 2.3.1.1 |
Amino-acid N-acetyltransferase.
based on mapping to UniProt Q9K8V3
Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
-!- Also acts with L-aspartate and, more slowly, with some other amino acids.
|
UniProtKB Entries (1)
| Q9K8V3 |
ARGJ_BACHD
Bacillus halodurans C-125
Arginine biosynthesis bifunctional protein ArgJ
|
PDB Structure
| PDB | 1VRA |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of Arginine biosynthesis bifunctional protein argJ (10175521) from Bacillus halodurans at 2.00 A resolution
To be published
|
