| IED ID | IndEnz0001000255 |
| Enzyme Type ID | amylase000255 |
| Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | AMY1.1 |
| Organism | Vigna mungo (Black gram) (Phaseolus mungo) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade indigoferoid/millettioid clade Phaseoleae Vigna Vigna mungo (Black gram) (Phaseolus mungo) |
| Enzyme Sequence | MDSFSRLSIFCLFISLLPLFSSPALLFQGFNWESSKKGGWYNSLKNSIPDLANAGITHVWLPPPSQSVSPEGYLPGRLYDLDASKYGSKNELKSLIAAFHEKGIKCLADIVINHRTAERKDGRGIYCIFEGGTPDSRQDWGPSFICRDDTAYSDGTGNNDSGEGYDAAPDIDHLNPQVQRELSEWMNWLKTEIGFDGWRFDFVKGYAPSISKIYMEQTKPDFAVGEKWDSISYGQDGKPNYNQDSHRGALVNWVESAGGAITAFDFTTKGILQAAVQGELWRLIDPNGKPPGMIGVKPENAVTFIDNHDTGSTQRLWPFPSDKVMQGYAYILTHPGTPSIFYDHFFDWGLKEQIAKLSSIRLRNGINEKSTVKIMASEGDLYVAKIDNKIMVKIGPKMDLGNLIPSNLHVATSGQDYAVWE |
| Enzyme Length | 421 |
| Uniprot Accession Number | P17859 |
| Absorption | |
| Active Site | ACT_SITE 201; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00693; ACT_SITE 226; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P00693 |
| Activity Regulation | |
| Binding Site | BINDING 228; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 230; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P04063; BINDING 255; /note=Substrate; /evidence=ECO:0000250; BINDING 289; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 308; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 314; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 393; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 420; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693 |
| 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:P00693}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (8); Chain (1); Metal binding (11); Region (2); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Glycosidase;Hydrolase;Metal-binding;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000305 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,889 |
| Kinetics | |
| Metal Binding | METAL 113; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00693; METAL 130; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00693; METAL 133; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 135; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 139; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P04063; METAL 149; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P04063; METAL 160; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P04063; METAL 168; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063; METAL 170; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P04063; METAL 170; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P04063; METAL 205; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063 |
| Rhea ID | |
| Cross Reference Brenda |