FAEA_ASPAW
ID FAEA_ASPAW Reviewed; 281 AA.
AC Q9P979;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Feruloyl esterase A;
DE EC=3.1.1.73;
DE AltName: Full=Ferulic acid esterase A;
DE Short=FAEA;
DE AltName: Full=Feruloylesterase;
DE Flags: Precursor;
GN Name=faeA {ECO:0000303|PubMed:15716038};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-92; THR-93; ASP-98
RP AND TYR-101.
RC STRAIN=ATCC 38854 / NBRC 4033;
RX PubMed=15716038; DOI=10.1016/j.bbagen.2004.12.016;
RA Koseki T., Takahashi K., Fushinobu S., Iefuji H., Iwano K., Hashizume K.,
RA Matsuzawa H.;
RT "Mutational analysis of a feruloyl esterase from Aspergillus awamori
RT involved in substrate discrimination and pH dependence.";
RL Biochim. Biophys. Acta 1722:200-208(2005).
CC -!- FUNCTION: Involved in the degradation of plant cell walls. Hydrolyzes
CC the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-
CC galactose ester bond in pectin. Active against methyl ferulate, methyl
CC sinapate, methyl caffeate, and alpha-naphthyl esters with chains
CC containing 2 to 8 carbons (C2-C8). Inactive against alpha-naphthyl
CC esters with longer chains (C10 or more). {ECO:0000269|PubMed:15716038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73; Evidence={ECO:0000269|PubMed:15716038};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 mM for alpha-naphthylbutyrate {ECO:0000269|PubMed:15716038};
CC KM=0.079 mM for alpha-naphthylcaprylate
CC {ECO:0000269|PubMed:15716038};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:15716038};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O42807}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FaeA family.
CC {ECO:0000305}.
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DR EMBL; AB032760; BAA92937.3; -; Genomic_DNA.
DR AlphaFoldDB; Q9P979; -.
DR SMR; Q9P979; -.
DR CLAE; FAE1A_ASPAW; -.
DR ESTHER; aspaw-FERA; Lipase_3.
DR BRENDA; 3.1.1.73; 494.
DR SABIO-RK; Q9P979; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0030600; F:feruloyl esterase activity; ISS:UniProtKB.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Hydrolase;
KW Polysaccharide degradation; Secreted; Serine esterase; Signal;
KW Xylan degradation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..281
FT /note="Feruloyl esterase A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021225"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 50..279
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT DISULFID 112..115
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT DISULFID 248..255
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT MUTAGEN 92
FT /note="D->I: Active against longer alpha-naphthyl esters
FT than wild-type (C10, C12 and C16). Km value for the C8
FT alpha-naphthyl ester is decreased by 1.6-fold compared to
FT wild-type. Decreased activity on arabinoxylan."
FT /evidence="ECO:0000269|PubMed:15716038"
FT MUTAGEN 93
FT /note="T->R: Km value for the C4 alpha-naphthyl ester is
FT increased by 1.9-fold compared to wild-type. Km value for
FT the C8 alpha-naphthyl ester is decreased by 4.6-fold
FT compared to wild-type. Slightly decreased activity on
FT arabinoxylan."
FT /evidence="ECO:0000269|PubMed:15716038"
FT MUTAGEN 98
FT /note="D->I: Increased optimum pH. Km value for the C4
FT alpha-naphthyl ester is decreased. Has higher activity on
FT short chain alpha-naphthyl esters than wild-type, but no
FT activity on substrates containing 6 or more carbon atoms.
FT No activity on arabinoxylan, methyl ferulate, methyl
FT sinapate or methyl caffeate."
FT /evidence="ECO:0000269|PubMed:15716038"
FT MUTAGEN 98
FT /note="D->N: Increased optimum pH. Km value for the C4
FT alpha-naphthyl ester is decreased. Has higher activity on
FT short chain alpha-naphthyl esters than wild-type, but no
FT activity on substrates containing 6 or more carbon atoms.
FT Decreased activity on arabinoxylan."
FT /evidence="ECO:0000269|PubMed:15716038"
FT MUTAGEN 101
FT /note="Y->F: Increased optimum pH. Active against longer
FT alpha-naphthyl esters than wild-type (C10, C12 and C16). Km
FT value for the C4 alpha-naphthyl ester is increased by 1.9-
FT fold compared to wild-type. Km value for the C8 alpha-
FT naphthyl ester is decreased by 1.9-fold compared to wild-
FT type. Decreased activity on arabinoxylan, methyl ferulate,
FT methyl sinapate or methyl caffeate."
FT /evidence="ECO:0000269|PubMed:15716038"
SQ SEQUENCE 281 AA; 30401 MW; C344247FD0A341FF CRC64;
MKQFSAKHAL AVVVTAGHAL AASTQGISED LYTRLVEMAT ISQAAYADLC NIPSTIIKGE
KIYNSQTDIN GWILRDDSSK EIITVFRGTG SDTNLQLDTN YTLTPFDTLP QCNGCEVHGG
YYIGWVSVQD QVESLVKQQV SQYPDYALTV TGHSLGASLA ALTAAQLSAT YDNIRLYTFG
EPRSGNQAFA SYMNDAFQAS SPDTTQYFRV THANDGIPNL PPVEQGYAHG GVEYWSVDPY
SAQNTFVCTG DEVQCCEAQG GQGVNNAHTT YFGMTSGACT W
