BD-FAE

Family: BD-FAE

Block: H

Parent Family: No family

Comment

Extracted from Hormone sensitive lipases. BD-FAE: The function of many members may differ from the one of the representavive used to describe the family in the PFAM database. (from PFAM): This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilisation loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates. In PFAM database it includes family Tannase_Bact and family Est9X which are separate families in ESTHER. Feruloyl esterases are distributed in different sub-classes type-A B C,D and E and fall respectively in the following families. Type-A in Lipase_3, Type-B in Esterase_phb (PHB depolymerase), Type-C in Tannase, Type-D in FaeC, Type-E in A85-Feruloyl-Esterase, Type-F in BD-FAE. This family also contains Sphingobium fuliginis meta-fission product hydrolase and Non-reducing polyketide synthase Lecanoric acid synthase thioesterase domain farther related to similar thioesterase domain.