FAEA_ASPTU
ID FAEA_ASPTU Reviewed; 280 AA.
AC O42815;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Feruloyl esterase A;
DE EC=3.1.1.73;
DE AltName: Full=Ferulic acid esterase A;
DE Flags: Precursor;
GN Name=faeA;
OS Aspergillus tubingensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5068;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=NW756;
RX PubMed=9406381; DOI=10.1128/aem.63.12.4638-4644.1997;
RA de Vries R.P., Michelsen B., Poulsen C.H., Kroon P.A.,
RA van den Heuvel R.H.H., Faulds C.B., Williamson G.,
RA van den Hombergh J.P.T.W., Visser J.;
RT "The faeA genes from Aspergillus niger and Aspergillus tubingensis encode
RT ferulic acid esterases involved in degradation of complex cell wall
RT polysaccharides.";
RL Appl. Environ. Microbiol. 63:4638-4644(1997).
CC -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-
CC galactose ester bond in pectin. {ECO:0000269|PubMed:9406381}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9406381}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FaeA family.
CC {ECO:0000305}.
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DR EMBL; Y09331; CAA70511.1; -; Genomic_DNA.
DR AlphaFoldDB; O42815; -.
DR SMR; O42815; -.
DR ESTHER; asptu-FAEA; Lipase_3.
DR KEGG; ag:CAA70511; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_51570; -.
DR BRENDA; 3.1.1.73; 538.
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 3: Inferred from homology;
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..280
FT /note="Feruloyl esterase A"
FT /id="PRO_0000021227"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT ACT_SITE 267
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 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..278
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT DISULFID 112..115
FT /evidence="ECO:0000250|UniProtKB:O42807"
FT DISULFID 247..254
FT /evidence="ECO:0000250|UniProtKB:O42807"
SQ SEQUENCE 280 AA; 30451 MW; 3601EF04C6E72713 CRC64;
MKQFSAKYAI AVVVTAGHAL AASTQGISED LYSRLVEMAT ISQAAYADLC NIPSTIIKGE
KIYNSQTDIN GWILRDDSSK EIITVFRGTG SDTNLQLDTN YTLTPFDTLP QCNSCEVHGG
YYIGWISVQD QVESLVQQQV SQFPDYALTV TGHSLGASLA ALTAAQLSAT YDNIRLYTFG
EPRSNQAFAS YMNDAFQASS PDTTQYFRVT HANDGIPNLP PADEGYAHGV VEYWSVDPYS
AQNTFVCTGD EVQCCEAQGG QGVNNAHTTY FGMTSGHCTW
