Detail Information for IndEnz0011000423
IED ID IndEnz0011000423
Enzyme Type ID glucanase000423
Protein Name Glucan 1,3-beta-glucosidase 1
EC 3.2.1.58
Exo-1,3-beta-glucanase 1
Gene Name EXG1
Organism Wickerhamomyces anomalus (Yeast) (Hansenula anomala)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Phaffomycetaceae Wickerhamomyces Wickerhamomyces anomalus (Yeast) (Hansenula anomala)
Enzyme Sequence MLFNILILSALSLQLCTCFHIKRNLNGSNDVIWDYYDDSKKVQGVSLGGWFVLEPYITPSLFEQFGEDEKKIPVDEYTFTEQLGKDEAQKQLDKHWATYFTESDFKDIKDYGLNLVRIPIGYWAFYLLEDDPYVQGQEPYLDKALEWAKQNDLKVWIDLHGVPGSQNGFDNSGKRGNVTWQDDEENIELSYKTLNYIFGKYGGENLTDTVIGIEIVNEPFHSKLNETDMLDFYYNSYYDFRIKHNSRNFFLIQEAFEPIGFWNTHLNNDYTNVSKPFLNDELLEEGVPKNYFHDIVLDHHHYEVFSVDQLDKSENARIQDIKNYGESVAKEQEYHPSLVGEWSGAITDCAKWLNGVGTGARYDGTFDESQLVRTNAINGTAESQFKFKDKKRSCENVTFVEDFSKQHKENIRKFIEIQLLTYENSNSGWIFWNYKTENAIEWDFKKLVEHKLFPHPFNEYKYFYENGTQIVESAASGNPQNLLFITLSALLVSLSTLL
Enzyme Length 498
Uniprot Accession Number O93939
Absorption
Active Site ACT_SITE 218; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 341; /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 (1); Signal peptide (1)
Keywords Cell wall biogenesis/degradation;Disulfide bond;Glycosidase;Hydrolase;Secreted;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 58,063
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda