| IED ID | IndEnz0001000251 |
| Enzyme Type ID | amylase000251 |
| Protein Name |
Acid alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | |
| Organism | Aspergillus niger |
| 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 niger |
| Enzyme Sequence | LSAASWRTQSIYFLLTDRFGRTDNSTTATCNTGNEIYCGGSWQGIIDHLDYIEGMGFTAIWISPITEQLPQDTADGEAYHGYWQQKIYDVNSNFGTADNLKSLSDALHARGMYLMVDVVPDHMGYAGNGNDVDYSVFDPFDSSSYFHPYCLITDWDNLTMVEDCWEGDTIVSLPDLDTTETAVRTIWYDWVADLVSNYSVDGLRIDSVLEVQPDFFPGYNKASGVYCVGEIDNGNPASDCPYQKVLDGVLNYPIYWQLLYAFESSSGSISNLYNMIKSVASDCSDPTLLGNFIENHDNPRFAKYTSDYSQAKNVLSYIFLSDGIPIVYAGEEQHYAGGKVPYNREATWLSGYDTSAELYTWIATTNAIRKLAIAADSAYITYANDAFYTDSNTIAMAKGTSGSQVITVLSNKGSSGSSYTLTLSGSGYTSGTKLIEAYTCTSVTVDSSGDIPVPMASGLPRVLLPASVVDSSSLCGGSGRLYVE |
| Enzyme Length | 484 |
| Uniprot Accession Number | P56271 |
| Absorption | |
| Active Site | ACT_SITE 206; /note=Nucleophile; /evidence=ECO:0000269|PubMed:2207069; ACT_SITE 230; /note=Proton donor; /evidence=ECO:0000269|PubMed:2207069 |
| Activity Regulation | |
| Binding Site | BINDING 83; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 122; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 204; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 234; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 297; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 344; /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:0000269|PubMed:2207069}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (22); Binding site (6); Chain (1); Disulfide bond (4); Glycosylation (3); Helix (23); Metal binding (6); Region (1); Site (1); Turn (8) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2207069}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2AAA; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,935 |
| Kinetics | |
| Metal Binding | METAL 121; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:2207069, ECO:0007744|PDB:2AAA"; METAL 162; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:2207069, ECO:0007744|PDB:2AAA"; METAL 175; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:2207069, ECO:0007744|PDB:2AAA"; METAL 206; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:2207069, ECO:0007744|PDB:2AAA"; METAL 210; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:2207069, ECO:0007744|PDB:2AAA"; METAL 230; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:2207069, ECO:0007744|PDB:2AAA" |
| Rhea ID | |
| Cross Reference Brenda |