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InterPro: IPR008902 Bacterial alpha-L-rhamnosidase

Protein matchesHelp
UniProtKB
Matches:
674 proteins
AccessionHelp IPR008902 Bac_rhamnosid
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR008928 Six-hairpin glycosidase-like
Found in IPR016007 Alpha-L-rhamnosidase
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria [1].

Database linksHelp
PANDIT: PF05592
Pfam Clan: CL0211.5

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR008902 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P42592 Uncharacterized protein ygjK

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR008928 Six-hairpin glycosidase-like
IPR008902 Bacterial alpha-L-rhamnosidase
PDB Chain
ModBase

PublicationsHelp
1. Zverlov VV, Hertel C, Bronnenmeier K, Hroch A, Kellermann J, Schwarz WH.
The thermostable alpha-L-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial alpha-L-rhamnoside hydrolase, a new type of inverting glycoside hydrolase.
Mol. Microbiol. 35 173-9 2000 [PubMed: 10632887]
http://dx.doi.org/10.1046/j.1365-2958.2000.01691.x

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InterPro 23.1