| IED ID | IndEnz0001000133 |
| Enzyme Type ID | amylase000133 |
| Protein Name |
Alpha-amylase 2 EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | aah2 SPAC23D3.14c |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MNYRRNICLRIGWMLLFAFIPAYAGHSAEEWKRRSIYQIITDRFSLEEGATERIPCDPVRFMYCGGTWNGIRNHLDYIQGMGFDAIWISPIFENVEGNDIDGSSYHGYWTTNLYELNHHFGTKEEFMELIQELHKRDIWILLDVAINSMAINGPLEQMSFEKVIPFNDASFFHPHCWVDYESNDIESVQNCWLGDENLLLADVDTENEVVLSVLEKWIKNVVQEYDIDGIRFDAIKHAPIEFWLRMSKAADIFTIGEYFTGSPAEACDYQNSGLDSFLNFPLYWPITWAFNNTGLQCEALAIAINQINEECNDINVLGTFIGNHDLPRISHNNTDQARIMNAITFVMMWDGIPIIYYGTEQNFNSYHDPFNREALWLSNFDMENVYYKLIGILNRFRKSVQRQEENYVNTRSTILSVKIHHIVVQKLNVITVLNNYGIHNEERLSIVFKPLGASPKDTFFDIINNQKYVVNTDGTLKVVITNGFPIVLYPTSKIETSLPQFTATLLPEITFVPSITVTTHYVLPTLLAPLGYDIREHPGGQQFWNTLTAKSEAKTIRSFTKLKLFILLIAVPFALPMIILI |
| Enzyme Length | 581 |
| Uniprot Accession Number | Q09840 |
| Absorption | |
| Active Site | ACT_SITE 233; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P56271; ACT_SITE 257; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P56271 |
| Activity Regulation | |
| Binding Site | BINDING 109; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 231; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 261; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 325; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 372; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3 |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (5); Chain (1); Disulfide bond (3); Glycosylation (2); Lipidation (1); Metal binding (5); Propeptide (1); Region (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Cell membrane;Disulfide bond;GPI-anchor;Glycoprotein;Glycosidase;Hydrolase;Lipoprotein;Membrane;Metal-binding;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20519959; 21340088; |
| Motif | |
| Gene Encoded By | |
| Mass | 67,005 |
| Kinetics | |
| Metal Binding | METAL 147; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 202; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P56271; METAL 233; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 237; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 257; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P0C1B3 |
| Rhea ID | |
| Cross Reference Brenda |