| IED ID | IndEnz0001000007 |
| Enzyme Type ID | amylase000007 |
| Protein Name |
Beta/alpha-amylase Includes: Beta-amylase EC 3.2.1.2 ; Alpha-amylase EC 3.2.1.1 |
| Gene Name | |
| Organism | Paenibacillus polymyxa (Bacillus polymyxa) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Paenibacillus Paenibacillus polymyxa (Bacillus polymyxa) |
| Enzyme Sequence | MTLYRSLWKKGCMLLLSLVLSLTAFIGSPSNTASAAVADDFQASVMGPLAKINDWGSFKKQLQTLKNNGVYAITTDVWWGYVESAGDNQFDWSYYKTYANAVKEAGLKWVPIISTHKCGGNVGDDCNIPLPSWLSSKGSADEMQFKDESGYANSEALSPLWSGTGKQYDELYASFAENFAGYKSIIPKIYLSGGPSGELRYPSYYPAAGWSYPGRGKFQAYTETAKNAFRTAMNDKYGSLDKINAAWGTKLTSLSQINPPTDGDGFYTNGGYNSAYGKDFLSWYQSVLEKHLGVIGAAAHKNFDSVFGVRIGAKISGLHWQMNNPAMPHGTEQAGGYYDYNRLIQKFKDADLDLTFTCLEMSDSGTAPNYSLPSTLVDTVSSIANAKGVRLNGENALPTGGSGFQKIEEKITKFGYHGFTLLRINNLVNNDGSPTGELSGFKQYIISKAKPDNNGGTGNKVTIYYKKGFNSPYIHYRPAGGSWTAAPGVKMQDAEISGYAKITVDIGSASQLEAAFNDGNNNWDSNNTKNYSFSTGTSTYTPGNSGNAGTITSGAPAGANPGDGGGTTNKVTVYYKKGFNSPYIHYRPAGGSWTAAPGVKMQDAEISGYAKITVDIGSASQLEAAFNDGNNNWDSNNTKNYLFSTGTSTYTPGSNGAAGTIRTGAPSGSVLSVVTSTYATDLNEVTGPIQTEKLSGVSLNVSTSTYAPNSNGVEVTAQTEAPSGAFTSMDLGTLSNPTSLNTDWSKQSIYFIMTDRFSNGDPSNDNYGGFNSNNSDQRKWHGGDFQGIINKLDYIKNMGFTAIWITPVTMQKSEYAYHGYHTYDFYAVDGHLGTMDKLQELVRKAHDKNIAVMVDVVVNHTGDFQPGNGFAKAPFDKADWYHHNGDITDGDYNSNNQWKIENGDVAGLDDLNHENPATANELKNWIKWLLNETGIDGLRLDTVKHVPKGFLKDFDQAANTFTMGEIFHGDPAYVGDYTRYLDAALDFPMYYTIKDVFGHDQSMRKIKDRYSDDRYYRDAQTNGVFIDNHDVKRFLNDASGKPGANYDKWPQLKAALGFTLTSRGIPIIYQGTEQGYSGGDDPANRENMNFNANHDLYQYIAKLNYVRNNHPALQNGSQREKWVDDSFYSFQRSKNGDEAIVFINNSWNSQTRTIGNFDNLSNGTRLTNQLSNDSVQINNGSITVTLAPKEVKVFTK |
| Enzyme Length | 1196 |
| Uniprot Accession Number | P21543 |
| Absorption | |
| Active Site | ACT_SITE 198; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10050; ACT_SITE 394; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P36924 |
| Activity Regulation | |
| Binding Site | BINDING 76; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36924; BINDING 116; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36924; BINDING 124; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36924; BINDING 314; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36924; BINDING 319; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36924; BINDING 357; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36924; BINDING 423; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36924 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.; EC=3.2.1.2; 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 | 3.2.1.2; 3.2.1.1 |
| Enzyme Function | FUNCTION: The precursor protein is proteolytically cleaved to produce multiform beta-amylases and a 48 kDa alpha-amylase after secretion. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (36); Binding site (7); Chain (1); Disulfide bond (1); Helix (20); Metal binding (3); Mutagenesis (3); Region (4); Repeat (2); Sequence conflict (18); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Multifunctional enzyme;Polysaccharide degradation;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..35 |
| Structure 3D | NMR spectroscopy (2); X-ray crystallography (1) |
| Cross Reference PDB | 2LAA; 2LAB; 3VOC; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 130,893 |
| Kinetics | |
| Metal Binding | METAL 83; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P36924; METAL 87; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P36924; METAL 170; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P36924 |
| Rhea ID | |
| Cross Reference Brenda |