1UYQ

mutated b-glucosidase A from Paenibacillus polymyxa showing increased stability

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0008152	biological_process	metabolic process
A	0008422	molecular_function	beta-glucosidase activity
A	0016052	biological_process	carbohydrate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0030245	biological_process	cellulose catabolic process
A	0102483	molecular_function	scopolin beta-glucosidase activity

Functional Information from PROSITE/UniProt

site_id	PS00572
Number of Residues	9
Details	GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGAC

Chain	Residue	Details
A	ILE348-CYS356

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site_id	PS00653
Number of Residues	15
Details	GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FmWGtAtAAYQiEgA

Chain	Residue	Details
A	PHE10-ALA24

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255

Chain	Residue	Details
A	GLU166

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055

Chain	Residue	Details
A	GLU352

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