CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.58 | Methane Monooxygenase Hydroxylase; Chain G, domain 1 |
|
1.20.58.2190 |
Domain Context
CATH Clusters
| Superfamily | 1.20.58.2190 |
| Functional Family | peptide-N(4)-(N-acetyl-beta- glucosaminyl)asparagine amidase |
Enzyme Information
| 3.5.1.52 |
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase.
based on mapping to UniProt Q9JI78
Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
-!- Does not act on (GlcNAc)-Asn, because it requires the presence of more than two amino-acid residues in the substrate (cf. EC 3.5.1.26). -!- Formerly EC 3.2.2.18.
|
UniProtKB Entries (1)
| Q9JI78 |
NGLY1_MOUSE
Mus musculus
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
|
PDB Structure
| PDB | 2HPL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation.
Proc.Natl.Acad.Sci.Usa
|
