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Glycosyl hydrolase 2 galactose-binding domain-like
malectin domain-containing carbohydrate-binding protein
Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan [1]. [1]. 18524852. Malectin: a novel carbohydrate-binding protein of the. endoplasmic reticulum and a candidate player in the early steps. of protein N-glycosylation.. Schallus T, Jaeckh C, Feher K, Palma AS, Liu Y, Simpson JC,. Mackeen M, Stier G, Gibson TJ, Feizi T, Pieler T, Muhle-Goll C;. Mol Biol Cell. 2008;19:3404-3414. (from Pfam)
glycoside hydrolase family 2 TIM barrel-domain containing protein
This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. [1]. 8008071. Three-dimensional structure of beta-galactosidase from E. coli.. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW;. Nature. 1994;369:761-766. (from Pfam)
sugar-binding domain-containing protein
This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction. [1]. 8008071. Three-dimensional structure of beta-galactosidase from E. coli.. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW;. Nature. 1994;369:761-766. (from Pfam)
Glycosyl hydrolases family 2
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