IED ID | IndEnz0011000047 |
Enzyme Type ID | glucanase000047 |
Protein Name |
Glucan 1,3-beta-glucosidase EC 3.2.1.58 Exo-1,3-beta-glucanase |
Gene Name | |
Organism | Pichia angusta (Yeast) (Hansenula polymorpha) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Pichiaceae Ogataea Pichia angusta (Yeast) (Hansenula polymorpha) |
Enzyme Sequence | MLFPVLHLPKAMKFSSFSLIASSLLSLVAAAPVTLLKRDSRWDYANDKIYGVNIGGWLVLEPFITPSLFEAVSSDVPVDEYHYTEALGKEEAEKRLQEHWSTWIKEEDFKGMANAGLNFVRIPIGYWAFQLAEGDPYVQGQQEYLDKALEWCAKYGLKAWVDLHGAPGSQNGFDNSGKRGEIGWQNTTGYVDLTVQVLDQLTSKYGGSNYSDVIIGIELLNEPLGSYLDFDQLVDFYNKGYQLVRNNGNAPVIIHDAYLPDHTFDNVLNTEQDPNVWEVIVDHHHYQVFDEGSLSQSIDEHVSTACGWGQSENTEYHYSLCGEWTAALTDCAKWLNGAGRGARYDATFGGGNYIGSCDQLYTANYDYFTPEVISNYRRYVEAQMDSFLYGKNAGWVFWCWKTENTIEWDMQRLLGLGIIPQPLDDRQYPNQCGFS |
Enzyme Length | 435 |
Uniprot Accession Number | Q12626 |
Absorption | |
Active Site | ACT_SITE 222; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 323; /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); 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..30; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 49,264 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |