| IED ID | IndEnz0001000578 |
| Enzyme Type ID | amylase000578 |
| Protein Name |
Alpha-amylase-related protein EC 3.2.1.1 |
| Gene Name | Amyrel |
| Organism | Drosophila elegans (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group elegans subgroup Drosophila elegans (Fruit fly) |
| Enzyme Sequence | MFKFALALTLCLAGSLSLAQHNPHWWGNRNTIVHLFEWKWSDIAEECESFLGPRGFAGVQVSPVNENIISAGRPWWERYQPISYKLTTRSGNEEEFGDMVRRCNEVGVRIYVDVLLNHMSGDFDGVAIGTAGTEAEPSKKSFPGVPFSAQDFPPSCEITDWNNRFQVQQCELVGLKDLDQSSDWVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYRSLSDLNTDHGFPHNARPFIFQEVIDHGHETVSRDEYKDLGAVTEFRFSEEIGNAFRGNNALRWLQSWGTGWGFLPSGQALTFVDNHDNQRDAGAVLNYKSPRQYKMATAFHLAYPYGISRVMSSFAFDDHDTPPPQDAQERIISPEFDEDGACVNGWICEHRWRQIYAMVGFKNAVRDTEMAEWWDNGDSQISFCRGNKGFLAVNNNQYDLSQELNTCLPAGEYCDVISGSLINGSCTGKSVTVKDNGYGYIHIGVDDFDGMMALHVDAKV |
| Enzyme Length | 493 |
| Uniprot Accession Number | Q9NJP0 |
| Absorption | |
| Active Site | ACT_SITE 207; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 244; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746 |
| Activity Regulation | |
| Binding Site | BINDING 205; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 307; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 342; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634 |
| 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:P04746}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (3); Chain (1); Disulfide bond (5); Metal binding (4); Modified residue (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Chloride;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | MOD_RES 20; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,572 |
| Kinetics | |
| Metal Binding | METAL 117; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 168; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634; METAL 177; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 211; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634 |
| Rhea ID | |
| Cross Reference Brenda |