Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0016161 | molecular_function | beta-amylase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PROSITE/UniProt
site_id | PS00506 |
Number of Residues | 9 |
Details | BETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD |
Chain | Residue | Details |
A | HIS94-ASP102 | |
site_id | PS00679 |
Number of Residues | 11 |
Details | BETA_AMYLASE_2 Beta-amylase active site 2. GaAGELRYPSY |
Chain | Residue | Details |
A | GLY183-TYR193 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10050","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P10538","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P10538","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bya |
Chain | Residue | Details |
A | ASP102 | |
A | GLU187 | |