IED ID | IndEnz0011000031 |
Enzyme Type ID | glucanase000031 |
Protein Name |
Glucan endo-1,3-beta-glucosidase BGN13.1 EC 3.2.1.39 1- 3 -beta-glucan endohydrolase BGN13.1 1- 3 -beta-glucanase BGN13.1 Basic beta-1,3-endoglucanase BGN13.1 |
Gene Name | bgn13.1 |
Organism | Trichoderma harzianum (Hypocrea lixii) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Trichoderma harzianum (Hypocrea lixii) |
Enzyme Sequence | MLKLTALVALLLGAASATPTPSPPASDEGITKRATSFYYPNMDHVNAPRGFAPDLDGDFNYPIYQTVNAGDGNALQNAITTDGKGGSRHPQWFASQPRVVYIPPGTYTISKTLRFNTDTILMGDPTNPPIIKAAAGFSGDQTLISAQDPSTNEKGELSFAVAIKNVVLDTTAIPGGNSFTALWWGVAQAAHLQNVRITMSSSSGGNGHTGIRMGRGSTLGLADVRVERGQNGIWIDGHQQASFHNIYFFQNTIGMLISSGNTFSIFSSTFDTCGTAFPTLAGSPWIALIDAKSINSGVTFTTNQFPSFMIENLTKDNGTPVVVVRGSTLVGASSHVNTYSYGNTVGRNPTYGDVTSSNTRPSALAPGGRYPYVAPPTYGDLPISSFLNVKDPAQNGNRQVKGDNTINEADTLNAILELAASQNKVAYFPFGKYRVDSTLFIPKGSRIVGEAWATITGNGNFFKNENSPQPVVSVGRAGDVGIAQLQDLRVTTNDVLPGAILVQFNMAGNNPGDVALWNSLVTVGGTRGAQALANACTNNSNECKGAFIGIHVAKGSSPYIQNVWELGLRDHIAENFSGGTSHRRERWNFGPIRRNATCLYPIGSGHWWLYQLNLHNAANVVVSLLQAETNYHQGANTQQIPPAPWVANVGTWGDPDFSWCNGGDKRCRMGPANFINGGSNIYTYASAAWAFFSGPGQGCAQFECQQTIHWIASTPSNLQAFGLCSKDSVNTLRLGDGTFINTQNGYTGGWTPGGGDVARYTT |
Enzyme Length | 762 |
Uniprot Accession Number | P53626 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by glucose. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; |
DNA Binding | |
EC Number | 3.2.1.39 |
Enzyme Function | FUNCTION: Involved in mycoparasitism, hydrolyzes yeast and fungal cell walls. Classified as a small-oligosaccharide-producing type based its the end products: glucose, laminaribiose or laminaritetraose. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. Inactive at 55 degrees Celsius.; |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) |
Keywords | Cleavage on pair of basic residues;Direct protein sequencing;Glycosidase;Hydrolase;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | PTM: Does not seem to be glycosylated. |
Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 81,247 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |