| IED ID | IndEnz0001000571 |
| Enzyme Type ID | amylase000571 |
| Protein Name |
Beta-amylase Tri a 17 EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase allergen Tri a 17.0101 |
| Gene Name | BMY1 AMY1 |
| 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 | MAGNMLANYVQVYVMLPLDVVSVDNKFEKGDEIRAQLKKLTEAGVDGVMIDVWWGLVEGKGPKAYDWSAYKQVFDLVHEAGLKLQAIMSFHQCGGNVGDVVNIPIPQWVRDVGATDPDIFYTNRGGTRNIEYLTLGVDDQPLFHGRTAVQMYADYMASFRENMKKFLDAGTIVDIEVGLGPAGEMRYPSYPQSQGWVFPGIGEFICYDKYLEADFKAAAAKAGHPEWELPDDAGEYNDTPEKTQFFKDNGTYLTEKGKFFLSWYSNKLIKHGDKILDEANKVFLGCRVQLAIKISGIHWWYRVPNHAAELTAGYYNLDDRDGYRTIARMLTRHHASMNFTCAEMRDSEQSEEAKSAPEELVQQVLSAGWREGLHVACENALGRYDATAYNTILRNARPKGINKNGPPEHKLFGFTYLRLSNELLEGQNYATFQTFVEKMHANLGHDPSVDPVAPLERSKPEMPIEMILKAAQPKLEPFPFDKNTDLPVKDHTDVGDEVLVAPV |
| Enzyme Length | 503 |
| Uniprot Accession Number | P93594 |
| Absorption | |
| Active Site | ACT_SITE 184; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10050; ACT_SITE 378; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P10538 |
| Activity Regulation | |
| Binding Site | BINDING 51; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 91; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 99; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 293; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 298; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 340; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 418; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.; EC=3.2.1.2; Evidence={ECO:0000269|PubMed:30515829}; |
| DNA Binding | |
| EC Number | 3.2.1.2 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. Highly active at acidic pH range 4-7. Retains over 80% of maximum activity at 4.0. At higher pH values the activity decreases markedly, with more than 50% of activity lost at pH 8.0. {ECO:0000269|PubMed:30515829}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (10); Binding site (7); Chain (1); Helix (25); Region (1); Turn (5) |
| Keywords | 3D-structure;Allergen;Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6GER; |
| Mapped Pubmed ID | 22505256; 30845909; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,611 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |