Detail Information for IndEnz0001000134
IED ID IndEnz0001000134
Enzyme Type ID amylase000134
Protein Name Cytoplasmic alpha-amylase
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
Gene Name amyA yedC b1927 JW1912
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MRNPTLLQCFHWYYPEGGKLWPELAERADGFNDIGINMVWLPPAYKGASGGYSVGYDSYDLFDLGEFDQKGSIPTKYGDKAQLLAAIDALKRNDIAVLLDVVVNHKMGADEKEAIRVQRVNADDRTQIDEEIIECEGWTRYTFPARAGQYSQFIWDFKCFSGIDHIENPDEDGIFKIVNDYTGEGWNDQVDDELGNFDYLMGENIDFRNHAVTEEIKYWARWVMEQTQCDGFRLDAVKHIPAWFYKEWIEHVQEVAPKPLFIVAEYWSHEVDKLQTYIDQVEGKTMLFDAPLQMKFHEASRMGRDYDMTQIFTGTLVEADPFHAVTLVANHDTQPLQALEAPVEPWFKPLAYALILLRENGVPSVFYPDLYGAHYEDVGGDGQTYPIDMPIIEQLDELILARQRFAHGVQTLFFDHPNCIAFSRSGTDEFPGCVVVMSNGDDGEKTIHLGENYGNKTWRDFLGNRQERVVTDENGEATFFCNGGSVSVWVIEEVI
Enzyme Length 495
Uniprot Accession Number P26612
Absorption
Active Site ACT_SITE 235; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 265; /note=Proton donor; /evidence=ECO:0000250
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:1400215};
DNA Binding
EC Number 3.2.1.1
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Metal binding (3); Sequence conflict (4); Site (1)
Keywords Calcium;Carbohydrate metabolism;Cytoplasm;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Sodium
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1400215}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 15690043; 16606699;
Motif
Gene Encoded By
Mass 56,639
Kinetics
Metal Binding METAL 104; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P00692; METAL 198; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P00692; METAL 239; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00692
Rhea ID
Cross Reference Brenda