| IED ID | IndEnz0001000252 |
| Enzyme Type ID | amylase000252 |
| Protein Name |
Beta-amylase EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase Fragment |
| Gene Name | |
| Organism | Cytobacillus firmus (Bacillus firmus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Cytobacillus Cytobacillus firmus (Bacillus firmus) |
| Enzyme Sequence | MTLYRSLWKKGCMLLLSLVLSLTAFIGSPSNTASAAVADDIQASVMGPLAKINDWGSFKKQLQTLKNNGVYAITTDVWWGYVESAGDNQFDWSYYKTYADAVKEAGLKWVPIISTHKCGGNVGDDCNIPLPSWLSSKGSADEMQFKDESGYANNEALSPLWSGTGKQYDELYASFAQNFAGYKSIIPKIYLSGGPSGELRYPSYYPAAGWSYPGRGKFQAYTETAKNAFRTAMNDKYGSLDKINTAWGTKLTSLSQINPPTDGDGFYTNGGYNSAYGKDFLSWYQSVLEKHLGVIGAAAHKNFDSVFGVRIGAKISGLHWQMNNPAMPHSTEQAGGYYDYNRLIQKFKDADLDLTFTCLEMSDSGTAPNYSLPSTLVDTVSSIANAKGVRLNGENALQTGGSGFQKIEEKITKFGYHGFTLLRINNLVNNDGSPTGELSGFKQYIISKAKPDNNGGTGNKVTIYYKKG |
| Enzyme Length | 468 |
| Uniprot Accession Number | P96513 |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.2 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Disulfide bond (1); Metal binding (3); Non-terminal residue (1); Region (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Polysaccharide degradation;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..36; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,118 |
| 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 |