7F3A
Arabidopsis thaliana GH1 beta-glucosidase AtBGlu42
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006952 | biological_process | defense response |
A | 0008422 | molecular_function | beta-glucosidase activity |
A | 0009617 | biological_process | response to bacterium |
A | 0009866 | biological_process | induced systemic resistance, ethylene mediated signaling pathway |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0019748 | biological_process | secondary metabolic process |
A | 0030245 | biological_process | cellulose catabolic process |
A | 0031349 | biological_process | positive regulation of defense response |
A | 0102483 | molecular_function | scopolin beta-glucosidase activity |
A | 1990641 | biological_process | response to iron ion starvation |
Functional Information from PROSITE/UniProt
site_id | PS00653 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FtFGvAtSAYQiEgG |
Chain | Residue | Details |
A | PHE25-GLY39 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q8L7J2 |
Chain | Residue | Details |
A | GLU183 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q8L7J2 |
Chain | Residue | Details |
A | GLU388 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q8L7J2 |
Chain | Residue | Details |
A | GLN35 | |
A | HIS137 | |
A | TYR317 | |
A | TRP437 | |
A | GLU444 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q8GU20 |
Chain | Residue | Details |
A | ASN182 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9 |
Chain | Residue | Details |
A | GLU388 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q1XH05 |
Chain | Residue | Details |
A | PHE453 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: Important for substrate chain length specificity => ECO:0000269|PubMed:34965581 |
Chain | Residue | Details |
A | ARG342 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN420 |