| IED ID | IndEnz0001000425 |
| Enzyme Type ID | amylase000425 |
| Protein Name |
Beta-amylase EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase Fragment |
| Gene Name | BMY1 |
| Organism | Secale cereale (Rye) |
| 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 Secale Secale cereale (Rye) |
| Enzyme Sequence | SHAAEVTAGYYNLHDRDDYRPIARMLTRHHASLNFTCAEMRDSEQSSQAMSAPEELVQQVWSAGWREGLNIACENALPRYDPTAYNTILRNARPHGINHSSPTEHKLFGFTYLRLSNQLLEGQNYVNFKTFVDRMHANLPHDPSVDPVAPLQRSGPEIPIEVILQAAQPKLDPFPFEDHTDLPVQCLGGIGGGEVECPAGGIGGEVQQDPTGGMGGELPPAV |
| Enzyme Length | 222 |
| Uniprot Accession Number | P30271 |
| Absorption | |
| Active Site | ACT_SITE 74; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P10538 |
| Activity Regulation | |
| Binding Site | BINDING 36; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 114; /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 (1); Binding site (2); Chain (1); Non-terminal residue (1); Region (1) |
| Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,349 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |