4IM4

Multifunctional cellulase, xylanase, mannanase

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	0005975	biological_process	carbohydrate metabolic process
B	0000272	biological_process	polysaccharide catabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
C	0000272	biological_process	polysaccharide catabolic process
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
D	0000272	biological_process	polysaccharide catabolic process
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005975	biological_process	carbohydrate metabolic process
E	0000272	biological_process	polysaccharide catabolic process
E	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
E	0005975	biological_process	carbohydrate metabolic process
F	0000272	biological_process	polysaccharide catabolic process
F	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
F	0005975	biological_process	carbohydrate metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00659
Number of Residues	10
Details	GLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. LLFETMNEPR

Chain	Residue	Details
A	LEU186-ARG195

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor; for cellulase activity","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Nucleophile; for cellulase activity","evidences":[{"source":"UniProtKB","id":"A7LXT7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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