| IED ID | IndEnz0001000249 |
| Enzyme Type ID | amylase000249 |
| Protein Name |
Alpha-amylase A type-3 EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase Taka-amylase A TAA |
| Gene Name | amy3 amyIII Taa-G3 AO090003001210 |
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Enzyme Sequence | MMVAWWSLFLYGLQVAAPALAATPADWRSQSIYFLLTDRFARTDGSTTATCNTADRKYCGGTWQGIIDKLDYIQGMGFTAIWITPVTAQLPQTTAYGDAYHGYWQQDIYSLNENYGTADDLKALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFCLIQNYEDQTQVEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSIDGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTCPYQNVMDGVLNYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPRFASYTNDIALAKNVAAFIILNDGIPIIYAGQEQHYAGGNDPANREATWLSGYPTDSELYKLIASANAIRNYAISKDTGFVTYKNWPIYKDDTTIAMRKGTDGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGNVPVPMAGGLPRVLYPTEKLAGSKICSSS |
| Enzyme Length | 499 |
| Uniprot Accession Number | P0C1B4 |
| 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 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 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; Evidence={ECO:0000305}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (5); Chain (1); Disulfide bond (4); Glycosylation (1); Metal binding (6); Region (1); Sequence conflict (3); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C1B3}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 54,804 |
| 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 |