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:
- not assigned
Sequence domains:
- Glycoside hydrolase family 38, central domain
- Glycosyl hydrolases family 38, C-terminal beta sandwich domain
- Glycosyl hydrolase family 38, C-terminal
- Glycosyl hydrolases 38, beta-1 domain
- Galactose mutarotase-like domain superfamily
- Glycoside hydrolase families 57/38, central domain superfamily
- Glycoside hydrolase family 38, central domain superfamily
- Glycoside hydrolase family 38, N-terminal domain
2 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189412 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycoside hydrolase family 38 central domain-containing protein
Molecule details ›
Chains: A, B
Length: 923 amino acids
Theoretical weight: 105.24 KDa
Source organism: Streptococcus pyogenes M1 GAS
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 923 amino acids
Theoretical weight: 105.24 KDa
Source organism: Streptococcus pyogenes M1 GAS
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q99YP5 (Residues: 1-901; Coverage: 100%)
Sequence domains:
- Glycosyl hydrolases family 38 N-terminal domain
- Alpha mannosidase middle domain
- Glycosyl hydrolases family 38 C-terminal domain 1
- Glycosyl hydrolases family 38 C-terminal domain
- Glycosyl hydrolases family 38 C-terminal beta sandwich domain
