| IED ID | IndEnz0001000594 |
| Enzyme Type ID | amylase000594 |
| Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | amyE amyA BSU03040 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MFAKRFKTSLLPLFAGFLLLFHLVLAGPAAASAETANKSNELTAPSIKSGTILHAWNWSFNTLKHNMKDIHDAGYTAIQTSPINQVKEGNQGDKSMSNWYWLYQPTSYQIGNRYLGTEQEFKEMCAAAEEYGIKVIVDAVINHTTSDYAAISNEVKSIPNWTHGNTQIKNWSDRWDVTQNSLLGLYDWNTQNTQVQSYLKRFLDRALNDGADGFRFDAAKHIELPDDGSYGSQFWPNITNTSAEFQYGEILQDSASRDAAYANYMDVTASNYGHSIRSALKNRNLGVSNISHYASDVSADKLVTWVESHDTYANDDEESTWMSDDDIRLGWAVIASRSGSTPLFFSRPEGGGNGVRFPGKSQIGDRGSALFEDQAITAVNRFHNVMAGQPEELSNPNGNNQIFMNQRGSHGVVLANAGSSSVSINTATKLPDGRYDNKAGAGSFQVNDGKLTGTINARSVAVLYPDDIAKAPHVFLENYKTGVTHSFNDQLTITLRADANTTKAVYQINNGPETAFKDGDQFTIGKGDPFGKTYTIMLKGTNSDGVTRTEKYSFVKRDPASAKTIGYQNPNHWSQVNAYIYKHDGSRVIELTGSWPGKPMTKNADGIYTLTLPADTDTTNAKVIFNNGSAQVPGQNQPGFDYVLNGLYNDSGLSGSLPH |
| Enzyme Length | 659 |
| Uniprot Accession Number | P00691 |
| Absorption | |
| Active Site | ACT_SITE 217; /note=Nucleophile; /evidence=ECO:0000305|PubMed:9514750; ACT_SITE 249; /note=Proton donor; /evidence=ECO:0000305|PubMed:9514750 |
| Activity Regulation | |
| Binding Site | |
| 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:P06278}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (23); Chain (1); Helix (20); Metal binding (6); Natural variant (2); Propeptide (1); Sequence conflict (12); Signal peptide (1); Site (1); Turn (6) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1BAG; 1UA7; |
| Mapped Pubmed ID | 14617662; |
| Motif | |
| Gene Encoded By | |
| Mass | 72,378 |
| Kinetics | |
| Metal Binding | METAL 142; /note=Calcium 1; /evidence=ECO:0000269|PubMed:9514750; METAL 178; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:9514750; METAL 187; /note=Calcium 1; /evidence=ECO:0000269|PubMed:9514750; METAL 210; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:9514750; METAL 212; /note=Calcium 2; /evidence=ECO:0000269|PubMed:9514750; METAL 221; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:9514750 |
| Rhea ID | |
| Cross Reference Brenda |