| IED ID | IndEnz0001000250 |
| Enzyme Type ID | amylase000250 |
| Protein Name |
Alpha-amylase A EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase A |
| Gene Name | amyA |
| Organism | Aspergillus awamori (Black koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus awamori (Black koji mold) |
| Enzyme Sequence | MMVAWWSLFLYGLQVAAPALAATPADWRSQSIYFLLTDRFARTDGSTTATCNTADQKYCGGTWQGIIDKLDYIQGMGFTAIWITPVTAQLPQTTAYGDAYHGYWQQDIYSLNENYGTADDLKALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFCFIQNYEDQTQVEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSIDGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTCPYQNVMDGVLNYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPRFASYTNDIALAKNVAAFIILNDGIPIIYAGQEQHYAGGNDPANREATWLSGYPTDSELYKLIASRNAIRNYAISKDTGFVTYKNWPIYKDDTTIPMRKGTDGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGNVPVPMAGGLPRVLYPTEKLAGSKICYG |
| Enzyme Length | 498 |
| Uniprot Accession Number | Q02905 |
| Absorption | |
| Active Site | ACT_SITE 227; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P56271; ACT_SITE 251; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P56271 |
| Activity Regulation | |
| Binding Site | BINDING 56; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 104; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 143; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 225; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 255; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 318; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 365; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3 |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Disulfide bond (4); Glycosylation (1); Metal binding (6); Region (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 54,880 |
| Kinetics | |
| Metal Binding | METAL 142; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 183; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56271; METAL 196; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P56271; METAL 227; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 231; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 251; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P0C1B3 |
| Rhea ID | |
| Cross Reference Brenda |