IED ID | IndEnz0011000077 |
Enzyme Type ID | glucanase000077 |
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 | |
Organism | Glycine max (Soybean) (Glycine hispida) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade indigoferoid/millettioid clade Phaseoleae Glycine Glycine subgen. Soja Glycine max (Soybean) (Glycine hispida) |
Enzyme Sequence | MAKYHSSGKSSSMTAIAFLFILLITYTGTTDAQSGVCYGRLGNNLPTPQEVVALYNQANIRRMRIYGPSPEVLEALRGSNIELLLDIPNDNLRNLASSQDNANKWVQDNIKNYANNVRFRYVSVGNEVKPEHSFAQFLVPALENIQRAISNAGLGNQVKVSTAIDTGALAESFPPSKGSFKSDYRGAYLDGVIRFLVNNNAPLMVNVYSYFAYTANPKDISLDYALFRSPSVVVQDGSLGYRNLFDASVDAVYAALEKAGGGSLNIVVSESGWPSSGGTATSLDNARTYNTNLVRNVKQGTPKRPGAPLETYVFAMFDENQKQPEFEKFWGLFSPITKQPKYSINFN |
Enzyme Length | 347 |
Uniprot Accession Number | Q03773 |
Absorption | |
Active Site | ACT_SITE 127; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O22317; ACT_SITE 270; /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. Is capable of releasing soluble and highly active elicitor molecules from fungus cell walls. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Signal peptide (1) |
Keywords | Direct protein sequencing;Glycosidase;Hydrolase;Plant defense;Reference proteome;Signal;Vacuole |
Interact With | |
Induction | INDUCTION: By ethylene. |
Subcellular Location | SUBCELLULAR LOCATION: Vacuole {ECO:0000250}. Note=In intact tissues. {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: The N-terminus is blocked. |
Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 38,112 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |