| IED ID | IndEnz0001000015 |
| Enzyme Type ID | amylase000015 |
| Protein Name |
Beta-amylase EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase |
| Gene Name | BMY1 |
| Organism | Glycine max (Soybean) (Glycine hispida) |
| 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 Glycine Glycine subgen. Soja Glycine max (Soybean) (Glycine hispida) |
| Enzyme Sequence | MATSDSNMLLNYVPVYVMLPLGVVNVDNVFEDPDGLKEQLLQLRAAGVDGVMVDVWWGIIELKGPKQYDWRAYRSLFQLVQECGLTLQAIMSFHQCGGNVGDIVNIPIPQWVLDIGESNHDIFYTNRSGTRNKEYLTVGVDNEPIFHGRTAIEIYSDYMKSFRENMSDFLESGLIIDIEVGLGPAGELRYPSYPQSQGWEFPRIGEFQCYDKYLKADFKAAVARAGHPEWELPDDAGKYNDVPESTGFFKSNGTYVTEKGKFFLTWYSNKLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWYKVENHAAELTAGYYNLNDRDGYRPIARMLSRHHAILNFTCLEMRDSEQPSDAKSGPQELVQQVLSGGWREDIRVAGENALPRYDATAYNQIILNAKPQGVNNNGPPKLSMFGVTYLRLSDDLLQKSNFNIFKKFVLKMHADQDYCANPQKYNHAITPLKPSAPKIPIEVLLEATKPTLPFPWLPETDMKVDG |
| Enzyme Length | 496 |
| Uniprot Accession Number | P10538 |
| Absorption | |
| Active Site | ACT_SITE 187; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10050, ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:2474529, ECO:0000269|PubMed:8011643, ECO:0000269|PubMed:8174545"; ACT_SITE 381; /note="Proton acceptor"; /evidence="ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:8011643" |
| Activity Regulation | |
| Binding Site | BINDING 54; /note=Substrate; /evidence=ECO:0000269|PubMed:15178253; BINDING 94; /note=Substrate; /evidence=ECO:0000269|PubMed:15178253; BINDING 102; /note=Substrate; /evidence=ECO:0000269|PubMed:15178253; BINDING 296; /note=Substrate; /evidence=ECO:0000269|PubMed:15178253; BINDING 301; /note=Substrate; /evidence=ECO:0000269|PubMed:15178253; BINDING 343; /note=Substrate; /evidence=ECO:0000269|PubMed:15178253; BINDING 421; /note=Substrate; /evidence=ECO:0000269|PubMed:15178253 |
| 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; Evidence={ECO:0000269|PubMed:15178253}; |
| DNA Binding | |
| EC Number | 3.2.1.2 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (16); Binding site (7); Chain (1); Frameshift (1); Helix (25); Initiator methionine (1); Modified residue (1); Mutagenesis (6); Region (1); Sequence conflict (5); Turn (6) |
| Keywords | 3D-structure;Acetylation;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000269|PubMed:2430952 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (19) |
| Cross Reference PDB | 1BFN; 1BTC; 1BYA; 1BYB; 1BYC; 1BYD; 1Q6C; 1Q6D; 1Q6E; 1Q6F; 1Q6G; 1UKO; 1UKP; 1V3H; 1V3I; 1WDP; 1WDQ; 1WDR; 1WDS; |
| Mapped Pubmed ID | 14631070; 14638688; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,143 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.2; |