Sulfatase, family S1-22; The family 1 of sulfatases is composed of enzymes that require the posttranslational oxidation of a conserved cysteine (or serine) to a catalytic formylglycine to hydrolyze various sulfate ester substrates; Belongs to the family 1 of sulfatases (S1: formylglycine-dependent sulfatases), subfamily 22; Signal peptide of lipoprotein cleaved between the residues 17 and 18; Possibly localized in the outer membrane and/or in the cytoplasmic membranes; Family membership.

This enzyme is a modular protein consisting of a N-terminal module belonging to the family 6 of the carbohydrate esterases (CE6; 26-342), a central alpha-galactosidase domain belonging to family 27 of the glycoside hydrolases (GH27; 343-733) and a C-terminal domain of unknown function (734-866). Carbohydrate esterases catalyze the de-O or de-N-acetylation of substituted saccharides. The catalytic machinery is a Ser-His-Asp triad. Alpha-galactosidase catalyzes the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharide [...]

This conserved protein belongs to the (Trans)glycosidase superfamily, which is included in the TIM beta/alpha-barrel fold. This protein is distantly related to the glycoside hydrolases from the family GH36; Localized in the cytoplasm; Family membership.

This conserved protein belongs to the (Trans)glycosidase superfamily, which is included in the TIM beta/alpha-barrel fold. Distantly related to the glycoside hydrolases 36 (GH36); Localized in the cytoplasm; Family membership.

Iduronate-2-sulfatase, family S1-7; Iduronate-2-sulfatase, called also chondroitinsulfatase is involved in the glycosaminoglycan degradation. It hydrolyzes the 2-sulfate groups from non-reducing-terminal iduronic acid residues in dermatan sulfate, heparan sulfate and heparin; Belongs to the family 1 of sulfatases (S1: formylglycine-dependent sulfatases), subfamily 7; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; High confidence in function and specificity.

Alpha-L-fucosidase, family GH29; Modular protein that consists of an N-terminal alpha-L-fucosidase module belonging to the family 29 of glycoside hydrolases (GH29), responsible for hydrolyzing of alpha-1,6-linked fucose joined to an alpha-L-fucoside and a C-terminal domain that could be involved in the binding to specific ligands such as carbohydrate or lipids substrates; Signal peptide cleaved between the residue 27 and 28; Localized in the periplasmic space; High confidence in function and specificity.

Protein that consists of a GDSL-like Lipase/Acylhydrolase domain; Seems to have an uncleavable N-terminal signal sequence; Possibly localized in the cytoplasmic membrane; Family membership.

Sulfatase, family S1-17; The family 1 of sulfatases is composed of enzymes that require the posttranslational oxidation of a conserved cysteine (or serine) to a catalytic formylglycine to hydrolyze various sulfate ester substrates; Belongs to the family 1 of sulfatases (S1: formylglycine-dependent sulfatases), subfamily 17; Contains a N-terminal transmembrane helix; Seems localized in the cytoplasmic membrane; Family membership.

Beta-helix fold protein; Protein that likely adopts a right handed parallel beta-helix fold; Contains a C-terminal PDZ domain responsible of protein-protein interaction by binding either the carboxyl-terminal sequences of proteins or internal peptide sequences suggesting that it could be a signaling protein; Prokaryotic lipoprotein signal peptide cleaved between 19 and 20; Localized in the outer membrane; Conserved hypothetical protein.