Function and Biology Details
Reaction catalysed:
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
exo-alpha-sialidase (preferred)
PDBe Complex ID:
PDB-CPX-176792 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
exo-alpha-sialidase
Molecule details ›
Chains: A, B
Length: 452 amino acids
Theoretical weight: 50.41 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli
UniProt:
Sequence domains: BNR repeat-like domain
Structure domains:
Length: 452 amino acids
Theoretical weight: 50.41 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q59310 (Residues: 243-694; Coverage: 65%)
Sequence domains: BNR repeat-like domain
Structure domains:
