| IED ID | IndEnz0011000009 |
| Enzyme Type ID | glucanase000009 |
| Protein Name |
Glucan endo-1,3-beta-glucosidase, basic vacuolar isoform EC 3.2.1.39 1- 3 -beta-glucan endohydrolase 1- 3 -beta-glucanase Beta-1,3-endoglucanase allergen Hev b 2 Cleaved into: Glucan endo-1,3-beta-glucosidase minor form 3; Glucan endo-1,3-beta-glucosidase minor form 2; Glucan endo-1,3-beta-glucosidase minor form 1; Glucan endo-1,3-beta-glucosidase major form |
| Gene Name | HGN1 |
| Organism | Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Malpighiales Euphorbiaceae Crotonoideae Micrandreae Hevea Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) |
| Enzyme Sequence | MAISSSTSGTSSSFPSRTTVMLLLFFFAASVGITDAQVGVCYGMQGNNLPPVSEVIALYKKSNITRMRIYDPNRAVLEALRGSNIELILGVPNSDLQSLTNPSNAKSWVQKNVRGFWSSVLFRYIAVGNEISPVNRGTAWLAQFVLPAMRNIHDAIRSAGLQDQIKVSTAIDLTLVGNSYPPSAGAFRDDVRSYLDPIIGFLSSIRSPLLANIYPYFTYAYNPRDISLPYALFTSPSVVVWDGQRGYKNLFDATLDALYSALERASGGSLEVVVSESGWPSAGAFAATFDNGRTYLSNLIQHVKGGTPKRPNRAIETYLFAMFDENKKQPEVEKHFGLFFPNKWQKYNLNFSAEKNWDISTEHNATILFLKSDM |
| Enzyme Length | 374 |
| Uniprot Accession Number | P52407 |
| Absorption | |
| Active Site | ACT_SITE 130; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O22317; ACT_SITE 276; /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|Ref.3}; |
| DNA Binding | |
| EC Number | 3.2.1.39 |
| Enzyme Function | FUNCTION: Possesses beta-1,3-endoglucanase activity in vitro (PubMed:25700348). Is thought to be an important plant defense-related product against fungal pathogens (Probable). {ECO:0000269|PubMed:25700348, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5.0. The enzyme from cv. GT.1 displays a second optimum pH at 6.7. {ECO:0000269|Ref.3}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (4); Glycosylation (3); Modified residue (1); Natural variant (2); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Allergen;Direct protein sequencing;Glycoprotein;Glycosidase;Hydrolase;Plant defense;Pyrrolidone carboxylic acid;Signal;Vacuole |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole {ECO:0000305}. |
| Modified Residue | MOD_RES 37; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P15797 |
| Post Translational Modification | PTM: Glycosylated in cv. GT.1 and cv. RRIM 600 but not in cv. PR 261. Asn-350 is glycosylated only in cv. GT.1 due to the presence of Ser-352. In cv. PR 261 and cv. RRIM 600, Ser-352 is replaced by Gly so Asn-350 is not glycosylated. {ECO:0000269|Ref.3}.; PTM: In cv. GT.1, four different forms of the enzyme have been detected with differently processed C-termini. In cv. PR 261 and cv. RRIM 600, only 2 forms are detected, a major form which is processed at residue 352 and a minor form which is processed at residue 354. {ECO:0000269|Ref.3}. |
| Signal Peptide | SIGNAL 1..36; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,396 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |