Function and Biology Details
Reaction catalysed:
Hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L-rhamnosides
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Galactose-binding-like domain superfamily
- Alpha-L-rhamnosidase
- Alpha-L-rhamnosidase C-terminal domain
- Six-hairpin glycosidase superfamily
- Alpha-L-rhamnosidase, six-hairpin glycosidase domain
- Six-hairpin glycosidase-like superfamily
- Alpha-L-rhamnosidase, concanavalin-like domain
- Bacterial alpha-L-rhamnosidase N-terminal
2 more domains
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Alpha-L-rhamnosidase (preferred)
PDBe Complex ID:
PDB-CPX-182676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-L-rhamnosidase
Molecule details ›
Chain: A
Length: 1043 amino acids
Theoretical weight: 113.53 KDa
Source organism: Streptomyces avermitilis MA-4680 = NBRC 14893
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 1043 amino acids
Theoretical weight: 113.53 KDa
Source organism: Streptomyces avermitilis MA-4680 = NBRC 14893
Expression system: Escherichia coli
UniProt:
- Canonical:
Q82PP4 (Residues: 1-1030; Coverage: 100%)
Sequence domains:
- Alpha-L-rhamnosidase N-terminal domain
- Bacterial alpha-L-rhamnosidase concanavalin-like domain
- Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain
- Bacterial alpha-L-rhamnosidase C-terminal domain
