| IED ID | IndEnz0001000565 |
| Enzyme Type ID | amylase000565 |
| Protein Name |
Beta-amylase EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase |
| Gene Name | spoII |
| Organism | Bacillus cereus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus cereus group Bacillus cereus |
| Enzyme Sequence | MKNQFQYCCIVILSVVMLFVSLLIPQASSAAVNGKGMNPDYKAYLMAPLKKIPEVTNWETFENDLRWAKQNGFYAITVDFWWGDMEKNGDQQFDFSYAQRFAQSVKNAGMKMIPIISTHQCGGNVGDDCNVPIPSWVWNQKSDDSLYFKSETGTVNKETLNPLASDVIRKEYGELYTAFAAAMKPYKDVIAKIYLSGGPAGELRYPSYTTSDGTGYPSRGKFQAYTEFAKSKFRLWVLNKYGSLNEVNKAWGTKLISELAILPPSDGEQFLMNGYLSMYGKDYLEWYQGILENHTKLIGELAHNAFDTTFQVPIGAKIAGVHWQYNNPTIPHGAEKPAGYNDYSHLLDAFKSAKLDVTFTCLEMTDKGSYPEYSMPKTLVQNIATLANEKGIVLNGENALSIGNEEEYKRVAEMAFNYNFAGFTLLRYQDVMYNNSLMGKFKDLLGVTPVMQTIVVKNVPTTIGDTVYITGNRAELGSWDTKQYPIQLYYDSHSNDWRGNVVLPAERNIEFKAFIKSKDGTVKSWQTIQQSWNPVPLKTTSHTSSW |
| Enzyme Length | 546 |
| Uniprot Accession Number | P36924 |
| Absorption | |
| Active Site | ACT_SITE 202; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10050, ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294"; ACT_SITE 397; /note="Proton acceptor"; /evidence="ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294" |
| Activity Regulation | |
| Binding Site | BINDING 79; /note="Substrate"; /evidence="ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294"; BINDING 119; /note="Substrate"; /evidence="ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294"; BINDING 127; /note="Substrate"; /evidence="ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294"; BINDING 317; /note="Substrate"; /evidence="ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294"; BINDING 322; /note="Substrate"; /evidence="ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294"; BINDING 360; /note="Substrate"; /evidence="ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294"; BINDING 427; /note="Substrate"; /evidence="ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294" |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.2 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (22); Binding site (7); Chain (1); Disulfide bond (1); Domain (1); Helix (22); Metal binding (5); Mutagenesis (4); Region (1); Signal peptide (1); Turn (7) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Polysaccharide degradation;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30 |
| Structure 3D | X-ray crystallography (15) |
| Cross Reference PDB | 1B90; 1B9Z; 1CQY; 1ITC; 1J0Y; 1J0Z; 1J10; 1J11; 1J12; 1J18; 1VEM; 1VEN; 1VEO; 1VEP; 5BCA; |
| Mapped Pubmed ID | 10348915; 12741813; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,629 |
| Kinetics | |
| Metal Binding | METAL 86; /note=Calcium; /evidence=ECO:0000269|PubMed:10353816; METAL 90; /note=Calcium; /evidence=ECO:0000269|PubMed:10353816; METAL 91; /note=Calcium; /evidence=ECO:0000269|PubMed:10353816; METAL 171; /note=Calcium; /evidence=ECO:0000269|PubMed:10353816; METAL 174; /note=Calcium; /evidence=ECO:0000269|PubMed:10353816 |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.2; |