IED ID | IndEnz0001000574 |
Enzyme Type ID | amylase000574 |
Protein Name |
Maltogenic alpha-amylase EC 3.2.1.133 Glucan 1,4-alpha-maltohydrolase |
Gene Name | blmA |
Organism | Bacillus licheniformis |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus licheniformis |
Enzyme Sequence | MIELAAIHHQPFNSDAYSYNGRTLHIKIRTKKDDAEHVAWFGAILTNTPAHMESERAYVAKIGRNKQPMITGLPKCGLHSGSAIRIYLTALMIETLFTEAMVHVRFRYRQTHVLNFRLFMRQTRLMHRLGQINRLVSNFSGAFRAGGKICSGKPLPWGRKDPEAHDFFGGHLQGIMTSWTIWKTWGEAGIYLTPIFAAPSNHKYDTLDYCSIDPHFGDEELFRTVVSRIHERGMKIMLDAVFNHIGTSQEWQDVVKNGETSRYKDWFIFILSLLKKAAMIHLRLVPRCRSSIAGTRKFRLICLILRCTGSANLISTAGVWMWQMKLIMRFGRNSGKPSPEKPDIFILGEIWHQADPWLRGDEFHIGHELPVHRTDDSLFFRRIDFSSQIASRINSQKMSGMKQVKEVMLNLLDSHERILTRCGGDQRKGARLFWHSCLLRQGRIYYPRKSGFTAAMIHCAGSAWFGKRKNRIKRCLAFMKPLIALRKQENDVLTYGALEWKLVDDQNDFVSFSRTHEGKELIYFFHQGREVRRVRLRDLKIASDKRIYDAWTEEALHDDDVVDIQPGDFSFLGRSKFC |
Enzyme Length | 578 |
Uniprot Accession Number | Q04977 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains.; EC=3.2.1.133; |
DNA Binding | |
EC Number | 3.2.1.133 |
Enzyme Function | FUNCTION: Converts starch into maltose. In contrary to other maltogenic alpha-amylases BlmA cannot hydrolyze 1,4-alpha-glucosidic linkage next to 1,6-alpha-glucosidic linkages. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1) |
Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 66,924 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |