Detail Information for IndEnz0011000192
IED ID IndEnz0011000192
Enzyme Type ID glucanase000192
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 ACLA_031040
Organism Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus clavatus Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Enzyme Sequence MLSRLSQTALVALSLMTVLTEAVPSRMRIQTRDSVNYQSEIVRGVNLGGWLVLEPWITPSIFENGGGAAVDEWTLAEVLGKDKARAILSQHWSSFITQDDFNQIAQAGMNHVRIPVGYWAVSAPDEPYVDGQLEFLDNAISWARAAGLKVMIDLHGAPGSQNGFDNSGRKGPIAWQQGDTVARTVDAFKALAERYLPESDVVTAIEAVNEPNIPGGVNEGQLKEYYNQVLEVVHSINPDAGVFLSDGFLATASWNGYANGENVVMDTHHYHMFDNTLISLDINAHVRAACEFGNQIKGSDKPVVVGEWTGALTDCTKHLNGKDIPTRYEGQWANSPRYGDCGNKRQGSSSGLSEQERSDTRRFIEAQLDAYEGKNGWLFWTWKTEGAPGWDMQDLLANGLFPNPPTERQYGNQCA
Enzyme Length 415
Uniprot Accession Number A1CRV0
Absorption
Active Site ACT_SITE 210; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 307; /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); Erroneous gene model prediction (1); Region (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Cell wall biogenesis/degradation;Disulfide bond;Glycosidase;Hydrolase;Manganese;Metal-binding;Polysaccharide degradation;Reference proteome;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 45,665
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda