IED ID | IndEnz0001000561 |
Enzyme Type ID | amylase000561 |
Protein Name |
Alpha-amylase type B isozyme EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase Clone 168 Fragment |
Gene Name | AMY1.5 |
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 | KAPGMIGWWPAKAVTFVNNHDTGSTQHMWPFPSDRVMQGYAYILTHQGTPCIFYDHFFDWGPKEEIDRLVSVSTRHGIHSESKLQIIEADADLCLAEIDGKVIVKLGPRYDVGNLIPGGFEVAAHGNDYAVWEKI |
Enzyme Length | 135 |
Uniprot Accession Number | P04749 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 1; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 20; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 26; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 105; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 132; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P00693}; |
DNA Binding | |
EC Number | 3.2.1.1 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Binding site (5); Chain (1); Non-terminal residue (1); Region (1); Site (1) |
Keywords | Calcium;Carbohydrate metabolism;Germination;Glycosidase;Hydrolase |
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 | 15,140 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |