| IED ID | IndEnz0001000570 |
| Enzyme Type ID | amylase000570 |
| Protein Name |
Beta-amylase EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase |
| Gene Name | BMY1 AMYB |
| 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 | MEVNVKGNYVQVYVMLPLDAVSVNNRFEKGDELRAQLRKLVEAGVDGVMVDVWWGLVEGKGPKAYDWSAYKQLFELVQKAGLKLQAIMSFHQCGGNVGDAVNIPIPQWVRDVGTRDPDIFYTDGHGTRNIEYLTLGVDNQPLFHGRSAVQMYADYMTSFRENMKDFLDAGVIVDIEVGLGPAGEMRYPSYPQSHGWSFPGIGEFICYDKYLQADFKAAAAAVGHPEWEFPNDVGQYNDTPERTQFFRDNGTYLSEKGRFFLAWYSNNLIKHGDRILDEANKVFLGYKVQLAIKISGIHWWYKVPSHAAELTAGYYNLHDRDGYRTIARMLKRHRASINFTCAEMRDLEQSSQAMSAPEELVQQVLSAGWREGLNVACENALPRYDPTAYNTILRNARPHGINQSGPPEHKLFGFTYLRLSNQLVEGQNYVNFKTFVDRMHANLPRDPYVDPMAPLPRSGPEISIEMILQAAQPKLQPFPFQEHTDLPVGPTGGMGGQAEGPTCGMGGQVKGPTGGMGGQAEDPTSGIGGELPATM |
| Enzyme Length | 535 |
| Uniprot Accession Number | P16098 |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.2 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (15); Binding site (7); Chain (1); Helix (22); Region (3); Repeat (4); Sequence conflict (6); Turn (7) |
| Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat |
| Interact With | Itself |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 1B1Y; 2XFF; 2XFR; 2XFY; 2XG9; 2XGB; 2XGI; |
| Mapped Pubmed ID | 21085740; |
| Motif | |
| Gene Encoded By | |
| Mass | 59,647 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.2; |