| IED ID | IndEnz0001000254 |
| Enzyme Type ID | amylase000254 |
| Protein Name |
Beta-amylase EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase Beta-Amy1 |
| Gene Name | BMY1 |
| Organism | Hordeum vulgare subsp. spontaneum (Wild barley) (Hordeum spontaneum) |
| 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) Hordeum vulgare subsp. spontaneum (Wild barley) (Hordeum spontaneum) |
| Enzyme Sequence | MEVNVKGNYVQVYVMLPLDAVSVNNRFEKGDELRAQLRKLVEAGVDGVMVDVWWGLVEGKGPKAYDWSAYKQLFELVQKAGLKLQAIMSFHQCGGNVGDAVNIPIPQWVRDVGTRDPDIFYTDGHGTRNIEYLTLGVDNQPLFHGRSAVQMYADYMTSFRENMKEFLDAGVIVDIEVGLGPAGEMRYPSYPQSHGWSFPGIGEFICYDKYLQADFKAAAAAVGHPEWEFPNDAGQYNDTPERTQFFRDNGTYLTEKGRFFLAWYSNNLIKHGDRILDEANKVFLGYKVQLAIKISGIHWWYKVPSHAAELTAGYYNLHDRDGYRTIARMLKRHRASINFTCAEMRDSEQSSQAMSAPEELVQQVLSAGWREGLNVACENALPRYDPTAYNTILRNARPHGINQSGPPEHKLFGFTYLRLSNQLVEGQNYVNFKTFVDRMHANLPRDPYVDPMAPLPRSGPEISIEMILQAAKPKLQPFPFQEHTDLPVGPTGGMGGQAEGPTCGMGGQVKGPTGGMGGQAEDPTSGMGGELPATM |
| Enzyme Length | 535 |
| Uniprot Accession Number | P82993 |
| 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 | FUNCTION: Catalyzes the liberation of maltose from 1,4-alpha-D glucans. {ECO:0000269|PubMed:9625721, ECO:0000269|Ref.2}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Modified residue (1); Natural variant (3); Propeptide (2); Region (3); Repeat (4) |
| Keywords | Acetylation;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 3; /note=N-acetylvaline; /evidence=ECO:0000269|Ref.2 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 59,639 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |