| IED ID | IndEnz0001000605 |
| Enzyme Type ID | amylase000605 |
| Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | |
| Organism | Tenebrio molitor (Yellow mealworm beetle) |
| 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 Tenebrionoidea Tenebrionidae (darkling ground beetles) Tenebrioninae Tenebrio Tenebrio molitor (Yellow mealworm beetle) |
| Enzyme Sequence | QKDANFASGRNSIVHLFEWKWNDIADECERFLQPQGFGGVQISPPNEYLVADGRPWWERYQPVSYIINTRSGDESAFTDMTRRCNDAGVRIYVDAVINHMTGMNGVGTSGSSADHDGMNYPAVPYGSGDFHSPCEVNNYQDADNVRNCELVGLRDLNQGSDYVRGVLIDYMNHMIDLGVAGFRVDAAKHMSPGDLSVIFSGLKNLNTDYGFADGARPFIYQEVIDLGGEAISKNEYTGFGCVLEFQFGVSLGNAFQGGNQLKNLANWGPEWGLLEGLDAVVFVDNHDNQRTGGSQILTYKNPKPYKMAIAFMLAHPYGTTRIMSSFDFTDNDQGPPQDGSGNLISPGINDDNTCSNGYVCEHRWRQVYGMVGFRNAVEGTQVENWWSNDDNQIAFSRGSQGFVAFTNGGDLNQNLNTGLPAGTYCDVISGELSGGSCTGKSVTVGDNGSADISLGSAEDDGVLAIHVNAKL |
| Enzyme Length | 471 |
| Uniprot Accession Number | P56634 |
| Absorption | |
| Active Site | ACT_SITE 185; /note=Nucleophile; /evidence=ECO:0000305|PubMed:9600843; ACT_SITE 222; /note=Proton donor; /evidence=ECO:0000305|PubMed:9600843 |
| Activity Regulation | |
| Binding Site | BINDING 183; /note="Chloride"; /evidence="ECO:0000269|PubMed:10508777, ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, ECO:0007744|PDB:1JAE"; BINDING 285; /note="Chloride"; /evidence="ECO:0000269|PubMed:10508777, ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, ECO:0007744|PDB:1JAE"; BINDING 321; /note="Chloride"; /evidence="ECO:0000269|PubMed:10508777, ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, ECO:0007744|PDB:1JAE" |
| 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); Beta strand (29); Binding site (3); Chain (1); Disulfide bond (4); Helix (19); Metal binding (4); Modified residue (1); Region (1); Site (1); Turn (9) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Chloride;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 1; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:9199514, ECO:0000269|PubMed:9687373" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1CLV; 1JAE; 1TMQ; 1VIW; |
| Mapped Pubmed ID | 10089450; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,240 |
| Kinetics | |
| Metal Binding | METAL 98; /note="Calcium"; /evidence="ECO:0000269|PubMed:10508777, ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, ECO:0007744|PDB:1JAE"; METAL 146; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10508777, ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, ECO:0007744|PDB:1JAE"; METAL 155; /note="Calcium"; /evidence="ECO:0000269|PubMed:10508777, ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, ECO:0007744|PDB:1JAE"; METAL 189; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10508777, ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, ECO:0007744|PDB:1JAE" |
| Rhea ID | |
| Cross Reference Brenda |