ID FAEA_ASPNC Reviewed; 281 AA.
AC A2QSY5;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Probable feruloyl esterase A;
DE EC=3.1.1.73;
DE AltName: Full=Ferulic acid esterase A;
DE Flags: Precursor;
GN Name=faeA; ORFNames=An09g00120;
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FaeA family.
CC {ECO:0000305}.
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DR EMBL; AM270190; CAK45846.1; -; Genomic_DNA.
DR RefSeq; XP_001393337.1; XM_001393300.2.
DR AlphaFoldDB; A2QSY5; -.
DR SMR; A2QSY5; -.
DR ESTHER; aspni-FAEA; Lipase_3.
DR GlyCosmos; A2QSY5; 1 site, No reported glycans.
DR EnsemblFungi; CAK45846; CAK45846; An09g00120.
DR GeneID; 4983573; -.
DR KEGG; ang:An09g00120; -.
DR VEuPathDB; FungiDB:An09g00120; -.
DR HOGENOM; CLU_032957_1_1_1; -.
DR OrthoDB; 91669at2759; -.
DR Proteomes; UP000006706; Chromosome 1L.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030600; F:feruloyl esterase activity; IDA:AspGD.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:AspGD.
DR GO; GO:0044347; P:cell wall polysaccharide catabolic process; IDA:AspGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IDA:AspGD.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00519; Lipase_3; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR46640:SF1; LIPASE_3 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46640; TRIACYLGLYCEROL LIPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G06510)-RELATED; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Serine esterase;
KW Signal; Xylan degradation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..281
FT /note="Probable feruloyl esterase A"
FT /id="PRO_5000220371"
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:0000255"
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"
SQ SEQUENCE 281 AA; 30550 MW; 9F5623A33211BBF3 CRC64;
MKQFSAKYAL ILLATAGQAL AASTQGISED LYNRLVEMAT ISQAAYADLC NIPSTIIKGE
KIYNAQTDIN GWILRDDTSK EIITVFRGTG SDTNLQLDTN YTLTPFDTLP QCNDCEVHGG
YYIGWISVQD QVESLVKQQA SQYPDYALTV TGHSLGASMA ALTAAQLSAT YDNVRLYTFG
EPRSGNQAFA SYMNDAFQVS SPETTQYFRV THSNDGIPNL PPAEQGYAHG GVEYWSVDPY
SAQNTFVCTG DEVQCCEAQG GQGVNDAHTT YFGMTSGACT W
//
