| IED ID | IndEnz0011000392 |
| Enzyme Type ID | glucanase000392 |
| Protein Name |
Glucan endo-1,3-beta-glucosidase GII EC 3.2.1.39 1- 3 -beta-glucan endohydrolase GII 1- 3 -beta-glucanase isoenzyme GII Beta-1,3-endoglucanase GII |
| Gene Name | |
| Organism | Hordeum vulgare (Barley) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Hordeinae Hordeum Hordeum vulgare (Barley) |
| Enzyme Sequence | MARKDVASMFAAALFIGAFAAVPTSVQSIGVCYGVIGNNLPSRSDVVQLYRSKGINGMRIYFADGQALSALRNSGIGLILDIGNDQLANIAASTSNAASWVQNNVRPYYPAVNIKYIAAGNEVQGGATQSILPAMRNLNAALSAAGLGAIKVSTSIRFDEVANSFPPSAGVFKNAYMTDVARLLASTGAPLLANVYPYFAYRDNPGSISLNYATFQPGTTVRDQNNGLTYTSLFDAMVDAVYAALEKAGAPAVKVVVSESGWPSAGGFAASAGNARTYNQGLINHVGGGTPKKREALETYIFAMFNENQKTGDATERSFGLFNPDKSPAYNIQF |
| Enzyme Length | 334 |
| Uniprot Accession Number | P15737 |
| Absorption | |
| Active Site | ACT_SITE 122; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O22317; ACT_SITE 259; /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; Evidence={ECO:0000269|PubMed:8514770}; |
| DNA Binding | |
| EC Number | 3.2.1.39 |
| Enzyme Function | FUNCTION: May provide a degree of protection against microbial invasion of germinated barley grain through its ability to degrade fungal cell wall polysaccharides (PubMed:1899089). Hydrolyzes laminarin in vitro (PubMed:8514770). {ECO:0000269|PubMed:1899089, ECO:0000269|PubMed:8514770}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 (at 37 degrees Celsius). {ECO:0000269|PubMed:8514770}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (12); Chain (1); Helix (16); Sequence conflict (2); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Direct protein sequencing;Glycosidase;Hydrolase;Plant defense;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence="ECO:0000269|PubMed:2562758, ECO:0000269|Ref.4" |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1GHS; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 35,194 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |