Function and Biology Details
Reactions catalysed:
[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
O-GlcNAcase NagJ and Hyaluronoglucosaminidase (preferred)
PDBe Complex ID:
PDB-CPX-150858 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
O-GlcNAcase NagJ
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 17.49 KDa
Source organism: Clostridium perfringens ATCC 13124
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Cohesin domain
Structure domains: Immunoglobulin-like
Length: 165 amino acids
Theoretical weight: 17.49 KDa
Source organism: Clostridium perfringens ATCC 13124
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q0TR53 (Residues: 768-909; Coverage: 15%)
Sequence domains: Cohesin domain
Structure domains: Immunoglobulin-like
Hyaluronoglucosaminidase
Molecule details ›
Chain: B
Length: 140 amino acids
Theoretical weight: 15.51 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains:
Structure domains:
Length: 140 amino acids
Theoretical weight: 15.51 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli BL21
UniProt:
- Canonical: P26831 (Residues: 1498-1628; Coverage: 8%)
Sequence domains:
Structure domains:
