Detail Information for IndEnz0008000389
IED ID IndEnz0008000389
Enzyme Type ID cellulase000389
Protein Name Probable glucan 1,3-beta-glucosidase A
EC 3.2.1.58
Exo-1,3-beta-glucanase 1
Exo-1,3-beta-glucanase A
Gene Name exgA exg1 AFUB_004010
Organism Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Enzyme Sequence MIFKFSQKALVALYLVVGLAEAVPSKSRVVSRASTFDYNGIVRGVNIGGWLVLEPWITPSIFDNAGDAAVDEWTLTATLGQDQAKAVLSQHWSTFITQDDFQQIAQAGMNHVRIPIGYWAVSSLPDEPYVDGQLEYLDNAISWAREAGLKVVIDLHGAPGSQNGFDNSGRKGPIAWQQGDTVSQTVDAFRALAERYLPQSDVVTAIEALNEPNIPGGVSEAGLRDYYNQIADVVRQIDPDTSVFLSDGFLSTESWNGFKTGEDVVMDTHHYEMFDNYLISLDIDGHVKSACDFGKQIEGSDKPVVVGEWSGAVTDCTKHLNGKGVSTRYQGEYANNVKYGDCANTTQGSVADLSDQERTDTRRFIEAQLDAYEGKNGWLFWTWKTEGAPGWDMQDLLANGVFPSPLTDRQFPNQCA
Enzyme Length 416
Uniprot Accession Number B0XN12
Absorption
Active Site ACT_SITE 211; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 308; /note=Nucleophile; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; EC=3.2.1.58;
DNA Binding
EC Number 3.2.1.58
Enzyme Function FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Cell wall biogenesis/degradation;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Manganese;Metal-binding;Polysaccharide degradation;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 45,745
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda