Detail Information for IndEnz0001000010
IED ID IndEnz0001000010
Enzyme Type ID amylase000010
Protein Name Pancreatic alpha-amylase
PA
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
Gene Name AMY2
Organism Sus scrofa (Pig)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig)
Enzyme Sequence MKLFLLLSAFGFCWAQYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVNGQDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWRQIRNMVWFRNVVDGQPFANWWANGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL
Enzyme Length 511
Uniprot Accession Number P00690
Absorption
Active Site ACT_SITE 212; /note=Nucleophile; ACT_SITE 248; /note=Proton donor
Activity Regulation
Binding Site BINDING 210; /note="Chloride"; /evidence="ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631"; BINDING 313; /note="Chloride"; /evidence="ECO:0000305"; BINDING 352; /note="Chloride"; /evidence="ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631"
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:P04746};
DNA Binding
EC Number 3.2.1.1
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (31); Binding site (3); Chain (1); Disulfide bond (5); Glycosylation (1); Helix (21); Metal binding (4); Modified residue (1); Sequence conflict (5); Signal peptide (1); Site (1); Turn (10)
Keywords 3D-structure;Calcium;Carbohydrate metabolism;Chloride;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space.
Modified Residue MOD_RES 16; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P04746
Post Translational Modification
Signal Peptide SIGNAL 1..15; /evidence=ECO:0000269|PubMed:3484639
Structure 3D X-ray crystallography (17)
Cross Reference PDB 1BVN; 1DHK; 1HX0; 1JFH; 1KXQ; 1KXT; 1KXV; 1OSE; 1PIF; 1PIG; 1PPI; 1UA3; 1VAH; 1WO2; 3L2L; 3L2M; 4X0N;
Mapped Pubmed ID 12962327; 15517985; 15736930; 20222716;
Motif
Gene Encoded By
Mass 57,086
Kinetics
Metal Binding METAL 115; /note="Calcium"; /evidence="ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631"; METAL 173; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631"; METAL 182; /note="Calcium"; /evidence="ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631"; METAL 216; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631"
Rhea ID
Cross Reference Brenda 3.2.1.1;