Detail Information for IndEnz0001000594
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