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Family Report for: BD-FAE


Family BD-FAE
Block H
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

PF20434 (BD-FAE)
no EC number

Peptide in
Nucleotide in
Alignment with Multalin
|Text only/graphic display
Seed alignment with MAFFT
|No colour/coloured with Mview
Alignment with MAFFT
|No colour/coloured with Mview
|Graphical display, obtained with the dnd file produced by Clustalw

4 more
    Title: Polysaccharide utilization loci-driven enzyme discovery reveals BD-FAE: a bifunctional feruloyl and acetyl xylan esterase active on complex natural xylans
    Hameleers L, Penttinen L, Ikonen M, Jaillot L, Faure R, Terrapon N, Deuss PJ, Hakulinen N, Master ER, Jurak E
    Ref: Biotechnol Biofuels, 14:127, 2021 : PubMed


    Title: A Lactobacillus plantarum Esterase Active on a Broad Range of Phenolic Esters
    Esteban-Torres M, Landete JM, Reveron I, Santamaria L, de Las Rivas B, Munoz R
    Ref: Applied Environmental Microbiology, 81:3235, 2015 : PubMed


    Title: The Structure of a Novel Thermophilic Esterase from the Planctomycetes Species, Reveals an Open Active Site Due to a Minimal 'Cap' Domain
    Sayer C, Szabo Z, Isupov MN, Ingham C, Littlechild JA
    Ref: Front Microbiol, 6:1294, 2015 : PubMed


Other Papers

No structure scheme yet for this family

Structures in BD-FAE family (27)

Genes Proteins in BD-FAE family (782)

Fragments of genes in BD-FAE family (89)

Substrates of some enzymes in the BD-FAE family (6)

No Inhibitor

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page

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