ID   FAEC_ASPNC              Reviewed;         270 AA.
AC   A2QYU7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable feruloyl esterase C;
DE            EC=3.1.1.73;
DE   AltName: Full=Ferulic acid esterase C;
DE   Flags: Precursor;
GN   Name=faeC; ORFNames=An12g02550;
OS   Aspergillus niger (strain 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=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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. Active against paranitrophenyl-acetate,
CC       methyl ferulate and wheat arabinoxylan (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 faeC family. {ECO:0000305}.
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DR   EMBL; AM270264; CAK41096.1; -; Genomic_DNA.
DR   RefSeq; XP_001395336.1; XM_001395299.1.
DR   AlphaFoldDB; A2QYU7; -.
DR   SMR; A2QYU7; -.
DR   ESTHER; aspnc-faec; FaeC.
DR   PaxDb; A2QYU7; -.
DR   EnsemblFungi; CAK41096; CAK41096; An12g02550.
DR   GeneID; 4985606; -.
DR   KEGG; ang:ANI_1_342104; -.
DR   VEuPathDB; FungiDB:An12g02550; -.
DR   HOGENOM; CLU_027551_2_0_1; -.
DR   Proteomes; UP000006706; Chromosome 3L.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030600; F:feruloyl esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR043595; FaeB/C/D.
DR   InterPro; IPR034429; FaeC.
DR   PANTHER; PTHR38050; PTHR38050; 1.
DR   PANTHER; PTHR38050:SF1; PTHR38050:SF1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Serine esterase; Signal; Xylan degradation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..270
FT                   /note="Probable feruloyl esterase C"
FT                   /id="PRO_5000220706"
SQ   SEQUENCE   270 AA;  28588 MW;  EE8A6D6D0ADFA61C CRC64;
     MTRSIFIHTL LALSALTSVH GANSPGCGKN PTLANGVHQI NGREYTLKIP DDYDANNPYH
     LIFGLHWRGG NMDNVVSGDS IQPWYGLESR AQGSAIFIAP NGLNAGWANT NGEDVAFIDA
     IMEQVESDLC VDQSSRFATG FSWGGGMSYS LACSRAKEFR AVSVLSGGVI SGCDGGNDPI
     AYLGIHGIND PVLPFDGGVE LAERFVGNNG CQPASIEKPQ SGSNGWKRTD FYGCSKPVSF
     IAYDGGHDGA PLGVQSSLAP DATWEFFMAA