| IED ID | IndEnz0008000037 |
| Enzyme Type ID | cellulase000037 |
| 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 |