beta-glucosidase 2, glycosyl-hydrolase family 116 N-term. This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 320 to 354 amino acids in length. This domain is found associated with pfam04685. It is found just after the extreme N-terminus. The N-terminal is thought to be the luminal domain while the C terminal is the cytosolic domain. The catalytic domain of GBA-2 is unknown. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335 in the downstream family pfam04685.

Glycosyl-hydrolase family 116, catalytic region. This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.

Uncharacterized protein, contains GBA2_N and DUF608 domains [Function unknown].

oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.

Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family 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.

ChainA, Glucosylceramidase [Thermoanaerobacterium xylanolyticum LX-11]

ChainA, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKW_B Chain B, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKX_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKY_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11]

Bacterialbeta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2) [Thermoanaerobacterium xylanolyticum LX-11],5FJS_B Bacterial beta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2) [Thermoanaerobacterium xylanolyticum LX-11],5O0S_A Crystal structure of txGH116 (beta-glucosidase from Thermoanaerobacterium xylolyticum) in complex with unreacted beta Cyclophellitol Cyclosulfate probe ME711 [Thermoanaerobacterium xylanolyticum LX-11]

Crystalstructure of txGH116 (beta-glucosidase from Thermoanaerobacterium xylolyticum) in complex with beta Cyclophellitol Cyclosulfate probe ME594 [Thermoanaerobacterium xylanolyticum]

Crystalstructure of Thermoanaerobacterium xylolyticum GH116 beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],5BX2_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with 2-deoxy-2-fluoroglucoside [Thermoanaerobacterium xylanolyticum LX-11],5BX3_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with deoxynojirimycin [Thermoanaerobacterium xylanolyticum LX-11],5BX4_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with Glucoimidazole [Thermoanaerobacterium xylanolyticum LX-11],5BX5_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with glucose [Thermoanaerobacterium xylanolyticum LX-11],5NCX_A Crystal structure of Thermoanaerobacterium xylolyticum GH116 beta-glucosidase with an covalent inhibitor [Thermoanaerobacterium xylanolyticum LX-11],5OST_A Beta-glucosidase from Thermoanaerobacterium xylolyticum GH116 in complex with Gluco-1H-imidazole [Thermoanaerobacterium xylanolyticum LX-11]

Non-lysosomal glucosylceramidase OS=Mus musculus OX=10090 GN=Gba2 PE=1 SV=2

Non-lysosomal glucosylceramidase OS=Homo sapiens OX=9606 GN=GBA2 PE=1 SV=2

Non-lysosomal glucosylceramidase OS=Rattus norvegicus OX=10116 GN=Gba2 PE=2 SV=2