2FGL
An alkali thermostable F/10 xylanase from alkalophilic Bacillus sp. NG-27
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
A | 0045493 | biological_process | xylan catabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
B | 0045493 | biological_process | xylan catabolic process |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00591 |
Number of Residues | 11 |
Details | GH10_1 Glycosyl hydrolases family 10 (GH10) active site. GLDNqVTELDV |
Chain | Residue | Details |
A | GLY252-VAL262 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1exp |
Chain | Residue | Details |
A | GLU259 | |
A | GLU149 | |
A | ASP261 | |
A | HIS230 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1exp |
Chain | Residue | Details |
B | GLU259 | |
B | GLU149 | |
B | ASP261 | |
B | HIS230 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1exp |
Chain | Residue | Details |
A | GLU149 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1exp |
Chain | Residue | Details |
B | GLU149 |