| IED ID | IndEnz0001000562 |
| Enzyme Type ID | amylase000562 |
| Protein Name |
Alpha-amylase type B isozyme EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase Clones GRAMY56 and 963 |
| Gene Name | AMY1.6 |
| 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 | MANKHMSLSLFIVLLGLSCSLASGQVLFQGFNWESWKHNGGWYNFLMGKVDDIAAAGVTHVWLPPASQSVAEQGYMPGRLYDLDASKYGNKAQLKSLIGALHGKAVKAIADIVINHRTAERKDGRGIYCIFEGGTPDARLDWGPHMICRDDRPYPDGTGNRPTRTRADFGAAPDIDHLNPRVQKELVEWLNWLRTDDGFDGWRFDFAKGYSADVAKIYVDRSEPSFAVAEIWTSLAYGGDGKPNLNQDPHRQELVNWVNKVGGSGPATTFDFTTKGILNVAVEGELWRLRGTDGKAPGMIGWWPAKAVTFVDNHDTGSTQHMWPFPSDRVMQGYAYILTHPGNPCIFYDHFFDWGLKEEIDRLVSIRTRQGIHSESKLQIMEADADLYLAEIEGKVIVKLGPRYDVGHLIPEGFKVVAHGNDYAVWEKV |
| Enzyme Length | 429 |
| Uniprot Accession Number | P04750 |
| Absorption | |
| Active Site | ACT_SITE 205; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00693; ACT_SITE 230; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P00693 |
| Activity Regulation | |
| Binding Site | BINDING 232; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 234; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P04063; BINDING 252; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 295; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 314; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 320; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 399; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 426; /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 (13); Region (6); 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 | 16470656; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,937 |
| Kinetics | |
| Metal Binding | METAL 115; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00693; METAL 132; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00693; METAL 135; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 137; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 141; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00693; METAL 151; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P00693; METAL 167; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 168; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P00693; METAL 169; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 172; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 174; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00693; METAL 174; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P00693; METAL 209; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693 |
| Rhea ID | |
| Cross Reference Brenda |