Function and Biology Details
Reaction catalysed:
Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Glycoside hydrolase family 38, central domain
- Glycosyl hydrolases family 38, C-terminal beta sandwich domain
- Glycosyl hydrolase family 38, C-terminal
- Galactose mutarotase-like domain superfamily
- Glycoside hydrolase family 38, central domain superfamily
- Glycoside hydrolase families 57/38, central domain superfamily
- Glycoside hydrolase family 38, N-terminal domain
- Glycoside hydrolase/deacetylase, beta/alpha-barrel
1 more domain
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Alpha-mannosidase (preferred)
PDBe Complex ID:
PDB-CPX-149813 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-mannosidase
Molecule details ›
Chain: A
Length: 1096 amino acids
Theoretical weight: 125.76 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Komagataella pastoris
UniProt:
Sequence domains:
Length: 1096 amino acids
Theoretical weight: 125.76 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Komagataella pastoris
UniProt:
- Canonical:
P22855 (Residues: 1-1070; Coverage: 99%)
Sequence domains:
