| IED ID | IndEnz0001000597 |
| Enzyme Type ID | amylase000597 |
| Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase Allergen Der p IV Mite group 4 allergen Der p 4 allergen Der p 4.0101 Fragment |
| Gene Name | |
| Organism | Dermatophagoides pteronyssinus (European house dust mite) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Chelicerata Arachnida Acari Acariformes Sarcoptiformes Astigmata Psoroptidia Analgoidea (feather mites) Pyroglyphidae (house-dust mites) Dermatophagoidinae Dermatophagoides Dermatophagoides pteronyssinus (European house dust mite) |
| Enzyme Sequence | KYHNPHFIGNRSVITHLMEWKYDDIGDECERFLGPYGYGGVQVSPVNEHAILDRRPWYERYQPVSYDIRTRSGDEQQFRRMVKRCNKAGVRIYVDIVLNHMTGAQSGKGTNGHHYDGNTLQYPGVPFGPNDFHGHESCPTQDLEIHDYTNPKEARNCRLSGLRDLKQQSEYVRQKQVDFLNHLIDIGVAGFRSDASTHQWPDDLRSIYSRLHNLNKEFFPENSQPFIYHETIYYGGNGINSNEYTSLGRIIEFRFYKEITNVFRGNNPLHWLKNFGTEWGLVPSGDALVMIDSHDLRVGHTGKLGFNINCFEGRLLKAATAFMLAWNYGVPRVMSSYFWNQIIKDGKDVNDWVGPPSDKNGNILSVHPNPDMTCNHEWICEHRWREIYNMVKFRMIAGQEPVHNWWDNGDYQIAFSRGNRAFIAINLQKNQQNLQQKLHTGLPAGTYCDIISGNLIDNKCTGKSIHVDKNGQADVYVGHDEFDAFVAYHIGARIVS |
| Enzyme Length | 496 |
| Uniprot Accession Number | P49274 |
| Absorption | |
| Active Site | ACT_SITE 194; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P56634; ACT_SITE 230; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P56634 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by alpha-amylase inhibitors from wheat and rye. The most effective inhibitors are the wheat tetrameric alpha-amylase inhibitor (WTAI) and the rye dimeric alpha-amylase inhibitor (RDAI-1). Not inhibited by alpha-amylase inhibitor from barley. {ECO:0000269|PubMed:8781672}. |
| Binding Site | BINDING 192; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 332; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634 |
| 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:1710630, ECO:0000269|PubMed:8781672}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | FUNCTION: Aids in the digestion of starch and glycogen derived from food, such as skin scales, fungi and bacteria. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.4. {ECO:0000269|PubMed:1710630}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (2); Chain (1); Disulfide bond (3); Metal binding (4); Non-terminal residue (1); Site (1) |
| Keywords | Allergen;Calcium;Carbohydrate metabolism;Chloride;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10545763, ECO:0000269|PubMed:1710630, ECO:0000269|PubMed:1718897, ECO:0000269|PubMed:8781672}. |
| Modified Residue | |
| Post Translational Modification | PTM: Disulfide bonds are present. {ECO:0000269|PubMed:1710630}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,150 |
| Kinetics | |
| Metal Binding | METAL 99; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 155; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634; METAL 164; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 198; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634 |
| Rhea ID | |
| Cross Reference Brenda |