(from Interpro) This is a family of type-C feruloyl esterases. Feruloyl esterases catalyze the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugar, which is usually arabinose in 'natural' substrates. FaeC from Aspergillus oryzae and Emericella nidulans have been shown to display hydrolytic activity towards arabinoxylan and methyl ferulate, among other substrates. Many proteins in the family have a Cellulose Binding Motif (CBM) or a Ricin_B_lectin motif shuffled either at N-terminus or C-terminus of the core alpha/beta hydrolase sequence. These have been excluded in the sequences used in alignment and BLAST base. Other less frequent extensions include IPR013784 Carb-bd-like_fold; IPR026444 Secre_tail; IPR008969 CarboxyPept-like_regulatory. 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
Interpro : IPR034429 Feruloyl esterase C FaeC , IPR043595 Feruloyl esterase B\/C\/D
PIRSF : No PIRSF
Pdoc : No Pdoc
Pfam : No Pfam
Prints : No Print
EC Number : No EC Number
Structures (2)
Genes Proteins in FaeC family (726)
Fragments of genes in FaeC family (57)
Structures in FaeC family (2)Substrates in FaeC family (13)
No Inhibitor
Title : Identification and characterization of an acetyl xylan esterase from Aspergillus oryzae - Kato_2021_J.Biosci.Bioeng__ |
Author(s) : Kato T , Shiono Y , Koseki T |
Ref : J Biosci Bioeng , : , 2021 |
Abstract : Kato_2021_J.Biosci.Bioeng__ |
ESTHER : Kato_2021_J.Biosci.Bioeng__ |
PubMedSearch : Kato_2021_J.Biosci.Bioeng__ |
PubMedID: 34376338 |
Gene_locus related to this paper: aspfu-faec , aspor-faec |
Title : Characterization of a feruloyl esterase from Aspergillus terreus facilitates the division of fungal enzymes from Carbohydrate Esterase family 1 of the carbohydrate-active enzymes (CAZy) database - Makela_2018_Microb.Biotechnol_11_869 |
Author(s) : Makela MR , Dilokpimol A , Koskela SM , Kuuskeri J , de Vries RP , Hilden K |
Ref : Microb Biotechnol , 11 :869 , 2018 |
Abstract : Makela_2018_Microb.Biotechnol_11_869 |
ESTHER : Makela_2018_Microb.Biotechnol_11_869 |
PubMedSearch : Makela_2018_Microb.Biotechnol_11_869 |
PubMedID: 29697197 |
Gene_locus related to this paper: asptn-q0ci40 |
Title : Characterization of two distinct feruloyl esterases, AoFaeB and AoFaeC, from Aspergillus oryzae - Koseki_2009_Appl.Microbiol.Biotechnol_83_689 |
Author(s) : Koseki T , Hori A , Seki S , Murayama T , Shiono Y |
Ref : Applied Microbiology & Biotechnology , 83 :689 , 2009 |
Abstract : Koseki_2009_Appl.Microbiol.Biotechnol_83_689 |
ESTHER : Koseki_2009_Appl.Microbiol.Biotechnol_83_689 |
PubMedSearch : Koseki_2009_Appl.Microbiol.Biotechnol_83_689 |
PubMedID: 19242690 |
Gene_locus related to this paper: aspor-q2umx6 , aspor-q2up89 |
Title : Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls - Bauer_2006_Proc.Natl.Acad.Sci.U.S.A_103_11417 |
Author(s) : Bauer S , Vasu P , Persson S , Mort AJ , Somerville CR |
Ref : Proc Natl Acad Sci U S A , 103 :11417 , 2006 |
Abstract : Bauer_2006_Proc.Natl.Acad.Sci.U.S.A_103_11417 |
ESTHER : Bauer_2006_Proc.Natl.Acad.Sci.U.S.A_103_11417 |
PubMedSearch : Bauer_2006_Proc.Natl.Acad.Sci.U.S.A_103_11417 |
PubMedID: 16844780 |
Gene_locus related to this paper: emeni-axe1 , emeni-CUTI3 , emeni-faec |
Title : Identification of a type-D feruloyl esterase from Neurospora crassa - Crepin_2004_Appl.Microbiol.Biotechnol_63_567 |
Author(s) : Crepin VF , Faulds CB , Connerton IF |
Ref : Applied Microbiology & Biotechnology , 63 :567 , 2004 |
Abstract : Crepin_2004_Appl.Microbiol.Biotechnol_63_567 |
ESTHER : Crepin_2004_Appl.Microbiol.Biotechnol_63_567 |
PubMedSearch : Crepin_2004_Appl.Microbiol.Biotechnol_63_567 |
PubMedID: 14595525 |
Gene_locus related to this paper: neucr-FAED |