IED ID | IndEnz0001000573 |
Enzyme Type ID | amylase000573 |
Protein Name |
Beta-amylase EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase |
Gene Name | BMY1 |
Organism | Vigna unguiculata (Cowpea) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade indigoferoid/millettioid clade Phaseoleae Vigna Vigna unguiculata (Cowpea) |
Enzyme Sequence | MASLDKNMLLNYVPVYVMLPLGVVSVNNVFEDPEGLKEQLVQLREAGVDGVMVDVWWGIIEQKGPKQYDWSAYKSLFQLVQECGLKLQAIMSFHQCGGNVGDVVNIPIPQWVLDIGESDPDIFYTNRSGTRDKEYLTIGVDNKPIFHGRTAIEVYSDYMKSFRENMSDFLKSEVIIDIEVGLGPAGELRYPSYPQNQGWVFPGIGEFQCYDKYLKAEFKAAAARAGHSEWELPDDAGTYNDVPESTEFFKTNGTYLTEKGKFFLTWYSNQLLNHGDEILDEANKAFLGCKVNLAIKVSGIHWWYKAQNHAAELTAGYYNLDDRDGYRPIAKMVSRHHASLNFTCLEMRDSEQSSDAQSGPQELVQQVLSGGWRENIEVAGENALSRYDATAYNQIILNARPQGVNKDGPPKHRMYGVTYLRLSDELLQQSNFDIFKKFVVKMHADQDYCEDPQEYNHGIPPLKRSEPKIPVDVLNEATKPIPPFPWDSETDMKVDG |
Enzyme Length | 496 |
Uniprot Accession Number | O64407 |
Absorption | |
Active Site | ACT_SITE 187; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10050; ACT_SITE 381; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P10538 |
Activity Regulation | |
Binding Site | BINDING 54; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 94; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 102; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 296; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 301; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 343; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 421; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538 |
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); Region (1) |
Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 56,237 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |