IED Industry Enzyme Database

Detail Information for IndEnz0001000012
IED ID IndEnz0001000012
Enzyme Type ID amylase000012
Protein Name Alpha-amylase
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
BLA
Gene Name amyS amyL
Organism Bacillus licheniformis
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus licheniformis
Enzyme Sequence MKQQKRLYARLLTLLFALIFLLPHSAAAAANLNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQADVGYGAYDLYDLGEFHQKGTVRTKYGTKGELQSAIKSLHSRDINVYGDVVINHKGGADATEDVTAVEVDPADRNRVISGEHRIKAWTHFHFPGRGSTYSDFKWHWYHFDGTDWDESRKLNRIYKFQGKAWDWEVSNENGNYDYLMYADIDYDHPDVAAEIKRWGTWYANELQLDGFRLDAVKHIKFSFLRDWVNHVREKTGKEMFTVAEYWQNDLGALENYLNKTNFNHSVFDVPLHYQFHAASTQGGGYDMRKLLNSTVVSKHPLKAVTFVDNHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQVFYGDMYGTKGDSQREIPALKHKIEPILKARKQYAYGAQHDYFDHHDIVGWTREGDSSVANSGLAALITDGPGGAKRMYVGRQNAGETWHDITGNRSEPVVINSEGWGEFHVNGGSVSIYVQR
Enzyme Length 512
Uniprot Accession Number P06278
Absorption
Active Site ACT_SITE 260; /note=Nucleophile; ACT_SITE 290; /note=Proton donor
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:0000269|PubMed:11997021, ECO:0000269|PubMed:12915728, ECO:0000269|PubMed:14632998};
DNA Binding
EC Number 3.2.1.1
Enzyme Function
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Active up to 100 degrees Celsius.;
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active up to pH 11.;
Pathway
nucleotide Binding
Features Active site (2); Beta strand (28); Chain (1); Helix (17); Metal binding (18); Mutagenesis (32); Sequence conflict (30); Signal peptide (1); Site (1); Turn (7)
Keywords 3D-structure;Calcium;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14632998}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..29; /evidence=ECO:0000269|PubMed:6172418
Structure 3D X-ray crystallography (8)
Cross Reference PDB 1BLI; 1BPL; 1E3X; 1E3Z; 1E40; 1E43; 1OB0; 1VJS;
Mapped Pubmed ID 9163741;
Motif
Gene Encoded By
Mass 58,549
Kinetics
Metal Binding METAL 133; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 190; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 190; /note="Sodium"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551"; METAL 210; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 212; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 212; /note="Sodium"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551"; METAL 223; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 223; /note="Sodium"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551"; METAL 229; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 229; /note="Sodium"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551"; METAL 231; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 233; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 264; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 329; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 331; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 435; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 436; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"; METAL 459; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"
Rhea ID
Cross Reference Brenda 3.2.1.1;