| IED ID | IndEnz0001000557 |
| Enzyme Type ID | amylase000557 |
| Protein Name |
Alpha-amylase type B isozyme EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase Clone PHV19 Fragment |
| Gene Name | AMY1.3 |
| Organism | Hordeum vulgare (Barley) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Hordeinae Hordeum Hordeum vulgare (Barley) |
| Enzyme Sequence | MANKHLSLSLFLVLLGLSASLASGQVLFQGFNWESWKHNGGWYNFLMGKVDDIAAAGITHVWLPPASQSVAEQGYMPGRLYDLDASKYGNKAQLKSLIGALHGKGVKAIADIVINHRTAEHKDGRGIYCIFEGVTPDARLDWGPHMICRDDRPYADGTGNPDTGADFGAAPDIDHLNLRVQKELAEWLNWLKADIGFDGWRFDFAKGYSADVAKIYIDRSEPSFAVAEIWTSLAYGGDGKPNLNQDQHRQELVNWVDKVGGKGPATTFDFTTKGILNVAVEGELWRLRGTDGKAPGMIGWWPAKAVTFVDNHDTGSTQHMWPFPSDRVMQGYAYILTHPGTPCIFYDHFFDWGLKEEIDRLVSVRTGA |
| Enzyme Length | 368 |
| Uniprot Accession Number | P04747 |
| Absorption | |
| Active Site | ACT_SITE 203; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04063; ACT_SITE 228; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04063 |
| Activity Regulation | |
| Binding Site | BINDING 230; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 232; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P04063; BINDING 250; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 257; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 293; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 312; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 318; /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 (7); Chain (1); Metal binding (14); Non-terminal residue (1); Region (3); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Germination;Glycosidase;Hydrolase;Metal-binding;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,787 |
| Kinetics | |
| Metal Binding | METAL 115; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P04063; METAL 132; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P04063; METAL 135; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063; METAL 137; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063; METAL 141; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P04063; METAL 151; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P04063; METAL 162; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P04063; METAL 165; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063; METAL 166; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P04063; METAL 167; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063; METAL 170; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063; METAL 172; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P04063; METAL 172; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P04063; METAL 207; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063 |
| Rhea ID | |
| Cross Reference Brenda |