| IED ID | IndEnz0011000275 |
| Enzyme Type ID | glucanase000275 |
| Protein Name |
Glucan endo-1,3-beta-glucosidase EC 3.2.1.39 1- 3 -beta-glucan endohydrolase 1- 3 -beta-glucanase Beta-1,3-endoglucanase |
| Gene Name | GLC1 |
| Organism | Triticum aestivum (Wheat) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Triticinae Triticum Triticum aestivum (Wheat) |
| Enzyme Sequence | MPLLILLMLLAAGAAGAESATPSLHIGVNYGANADNLPSPTSVATFLATKTTIDRVKLFDANPTFISAFAGTPISLAVSLPNSALPALADKATGLDAARSWIRANLSPYVPATNVTLLLAGNEILLSTDTNLILSLLPAMRRLAQALKAEGLTGVRVTTPHYLGILAPSDGIPSNASFRAGYNTKLFPAMLQFHRDTGSPFMVNPYPYFSYRPETLNYALFRPNSGIYDPATKLNYTSMLDAQMDAIYTAMKKLGYGDVDIAVGEAGWPTQAEPGQIGVGVQEARDFNEGMIRVCSSGKGTPLMPNRTFETYLFSLFDENQKPGPIAERHFGLFNPDFTPVYDLGLLRDGASVAPTPSPNPSPNPSPKPAPSGGGKWCVAKDGANGTDLQNNINYACGFVDCKPIQSGGACFSPNSLQAHASYVMNAYYQANGHTDLACDFKGTGIVTSSDPSYGGCKYVS |
| Enzyme Length | 461 |
| Uniprot Accession Number | P52409 |
| Absorption | |
| Active Site | ACT_SITE 123; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O22317; ACT_SITE 265; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O22317 |
| Activity Regulation | |
| 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: Is thought to be an important plant defense-related product against fungal pathogens. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Disulfide bond (1); Region (1); Signal peptide (1) |
| Keywords | Disulfide bond;Glycosidase;Hydrolase;Plant defense;Reference proteome;Signal |
| Interact With | |
| Induction | INDUCTION: Associated with aluminum toxicity. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Contains two additional disulfide bonds. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,873 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |