IED ID | IndEnz0001000440 |
Enzyme Type ID | amylase000440 |
Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase AmyHha |
Gene Name | Amy |
Organism | Hypothenemus hampei (Coffee berry borer) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Coleoptera Polyphaga Cucujiformia Curculionoidea Curculionidae (weevils) Scolytinae (bark beetles) Hypothenemus Hypothenemus hampei (Coffee berry borer) |
Enzyme Sequence | MQHLSILLVVLGSSIAFAQHDPHFADGRNTIVHLFGWKWGDIASECENWLRKKGFAGVQISPPSENPIVSGRPWWENYQPVSYDLKNRNGDEDSLSDMIKRCNNVGVRIYADLVVNHMATSIGQGTADHSYDPGSKSYPAVPYSNENFHASCDIDYNDAASIRNCELSGLKDLDQSQDYVRGKIVDYMNHLVSLGVAGFRVDAAKHMWPADLAAIFGSVNDLNTDFFPSGSRAYIYQEVIDTGSDPIDNKDYTGFGSVCEFKYGIQLATCFRGSNPLKYLENWGTGWGLLDGGNTLVFIDNHDTERSSGSYLNYKESRAYKAANAFMLAHPYDGITKIMSSYDFSDNDQSPPSDGDNILSPGFKEDGTCTNGWICQHRWSPIFNMVEFRSVVSGIELTNWWSGGDYQIAFSRGTKGTIAISINDSLDSDVPTGLPDGTYCDVISGSLSNGSCTGKSITVSGGKAHISIASDDREAAVAIHANAKL |
Enzyme Length | 485 |
Uniprot Accession Number | A0A096XJN4 |
Absorption | |
Active Site | ACT_SITE 202; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P56634; ACT_SITE 238; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P56634 |
Activity Regulation | |
Binding Site | BINDING 200; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 301; /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:0000255|RuleBase:RU361134}; |
DNA Binding | |
EC Number | 3.2.1.1 |
Enzyme Function | FUNCTION: Involved in the digestion of starch (Probable). {ECO:0000305|PubMed:25264343}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Binding site (2); Chain (1); Disulfide bond (4); Glycosylation (2); Metal binding (4); Modified residue (1); Signal peptide (1); Site (1) |
Keywords | Calcium;Carbohydrate metabolism;Chloride;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | MOD_RES 19; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P56634 |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 53,124 |
Kinetics | |
Metal Binding | METAL 116; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 163; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634; METAL 172; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 206; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634 |
Rhea ID | |
Cross Reference Brenda |