| IED ID | IndEnz0001000577 |
| Enzyme Type ID | amylase000577 |
| Protein Name |
Alpha-amylase-related protein EC 3.2.1.1 |
| Gene Name | Amyrel |
| Organism | Drosophila bipectinata (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 ananassae subgroup bipectinata species complex Drosophila bipectinata (Fruit fly) |
| Enzyme Sequence | MFKFATAVILCLVAASSTLAQHNPHWWGNRNTIVHLFEWKWSDIAAECENFLGPRGFAGVQVSPVNENIVSAGRPWWERYQPISYKLTTRSGNEKEFADMVRRCNEVGVRIYVDVLLNHMSGDFDGIAVGTAGSEAEPSKKSYPGVPYSALDFHPSCEITDWNDRFQVQQCELVGLKDLDQSSEWVRSKLIEFLDHLIELGVAGFRVDAAKHMAADDLSFIYSSLSDLNIEHGFPHNARPFIFQEVIDHGHETVSREEYNQLGAVTEFRFSEGIGNAFRGNNALKWLQSWGTGWGFLPSGQALTFVDNHDNQRDMGAVLNYKSPKQYKMATAFHLAYPYGISRVMSSFAFDDHDTAPPQDEQEKIISPEFDEEGACVNGWICEHRWRQIYAMVGFKNAVRDTELSNWWDNGDSQISFCRGNKGFLAVNNNLYDLSQELQTCLPAGVYCDVISGSLVDGSCTGKSVTVDDNGYGYAHIGSDDFDGVLALHVDAKV |
| Enzyme Length | 494 |
| Uniprot Accession Number | Q9NJN8 |
| Absorption | |
| Active Site | ACT_SITE 208; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 245; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746 |
| Activity Regulation | |
| Binding Site | BINDING 206; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 308; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 343; /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 21; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,339 |
| Kinetics | |
| Metal Binding | METAL 118; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 169; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634; METAL 178; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 212; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634 |
| Rhea ID | |
| Cross Reference Brenda |