| IED ID | IndEnz0001000043 |
| Enzyme Type ID | amylase000043 |
| Protein Name |
Alpha-amylase mde5 EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase Mei4-dependent protein 5 Meiotic expression up-regulated protein 30 |
| Gene Name | mde5 meu30 SPAC25H1.09 SPAC4A8.01 |
| 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 | MKHNEVFGWTLKVLSFLLVVIPANALDKHGWRKQSIYSLLTDRFASTNPKPCNPEDREYCGGNWRGIIDKLDYIQGMGFTAIWISPIIKNIEGRTKYGEAYHGYWPQDLYTLNPHFGTEQDLIDLADALHDRGMYLMVDTVVNHMGSSDPRNIDYGIYRPFNQSSHYHPMCPIEQDKPLSLEQCWIGTEDMTLPDIDTENPQIIETLYNFIHDQVKQFKIDGLRVDATKHVRRTFWPGFCESAGVYCQGEEWTGQADLFCEWQEYMDGLHNFPVQGVAAESVIPLNDRALRKTAIAMNLVAHHCKDSTLLGLFLESQDAPRLAALNNDYTVLKNAMTLNLMSDGIPIVFYGQEQMFNGSHDPVNRPALWDQGYNTDGPLYQYTSKVNKIRRDLINSEDGEIYIRSITHAIMIGDHVMVMYKGPVITFITNYGAVDKEYLIKMPGSETMIDLLTCTLIEVEGEVMRTSIKKGEPKILYPYQLAFRDGFCQEQITLQEIDDVFMGRNEINGPDRK |
| Enzyme Length | 513 |
| Uniprot Accession Number | O14154 |
| Absorption | |
| Active Site | ACT_SITE 226; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P56271; ACT_SITE 250; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P56271 |
| Activity Regulation | |
| Binding Site | BINDING 105; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 144; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 224; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 254; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 318; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 365; /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 (6); Chain (1); Disulfide bond (4); Glycosylation (2); Metal binding (6); Region (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20473289; 23697806; |
| Motif | |
| Gene Encoded By | |
| Mass | 58,716 |
| Kinetics | |
| Metal Binding | METAL 143; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 182; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56271; METAL 195; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P56271; METAL 226; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 230; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 250; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P0C1B3 |
| Rhea ID | |
| Cross Reference Brenda |