| IED ID | IndEnz0001000263 |
| Enzyme Type ID | amylase000263 |
| Protein Name |
Pancreatic alpha-amylase PA EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | Amy2 |
| Organism | Rattus norvegicus (Rat) |
| 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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MKFVLLLSLIGFCWAQYDPHTADGRTAIVHLFEWRWADIAKECERYLAPKGFGGVQVSPPNENIIINNPSRPWWERYQPISYKICSRSGNENEFKDMVTRCNNVGVRIYVDAVINHMCGSGNSAGTHSTCGSYFNPNNREFSAVPYSAWYFNDNKCNGEINNYNDANQVRNCRLSGLLDLALDKDYVRTKVADYMNNLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAIKGSEYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFVPTDRALVFVDNHDNQRGHGAGGASILTFWDARMYKMAVGFMLAHPYGFTRVMSSYRRTRNFQNGKDVNDWIGPPNNNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVAFRNVVNGQPFANWWDNGSNQVAFSRGNRGFIVFNNDDWALSSTLQTGLPAGTYCDVISGDKVNGNCTGLKVNVGSDGKAHFSISNSAEDPFIAIHADSKL |
| Enzyme Length | 508 |
| Uniprot Accession Number | P00689 |
| Absorption | |
| Active Site | ACT_SITE 209; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 245; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746 |
| Activity Regulation | |
| Binding Site | BINDING 207; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746; BINDING 310; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746; BINDING 349; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746 |
| 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); Binding site (3); Chain (1); Disulfide bond (5); Metal binding (4); Modified residue (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Chloride;Disulfide bond;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 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10933808; 20391537; 23007066; |
| Motif | |
| Gene Encoded By | |
| Mass | 57,177 |
| Kinetics | |
| Metal Binding | METAL 115; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P04746; METAL 170; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04746; METAL 179; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P04746; METAL 213; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04746 |
| Rhea ID | |
| Cross Reference Brenda |