ID   FAEC_ASPFN              Reviewed;         270 AA.
AC   B8N7Z6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=AFLA_105900;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963475; EED53215.1; -; Genomic_DNA.
DR   RefSeq; XP_002376461.1; XM_002376420.1.
DR   AlphaFoldDB; B8N7Z6; -.
DR   SMR; B8N7Z6; -.
DR   STRING; 332952.B8N7Z6; -.
DR   ESTHER; aspfn-faec; FaeC.
DR   EnsemblFungi; EED53215; EED53215; AFLA_105900.
DR   VEuPathDB; FungiDB:AFLA_105900; -.
DR   eggNOG; ENOG502SMEI; Eukaryota.
DR   HOGENOM; CLU_027551_2_0_1; -.
DR   OMA; SSGCGKQ; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
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   InterPro; IPR003140; PLipase/COase/thioEstase.
DR   PANTHER; PTHR38050; PTHR38050; 1.
DR   PANTHER; PTHR38050:SF1; PTHR38050:SF1; 1.
DR   Pfam; PF02230; Abhydrolase_2; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Hydrolase;
KW   Polysaccharide degradation; Secreted; Serine esterase; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..270
FT                   /note="Probable feruloyl esterase C"
FT                   /id="PRO_0000394938"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   270 AA;  28385 MW;  3930F359FCF20F1A CRC64;
     MIKSIILQAI MVLSTLTSVH GANSSGCGKQ PTLVNGVHKI NDREYILKVP DNYNANKPHH
     LIFGLHWRGG NMNSVVNGES VEPWYGLETR AQGSAILVAP NGRNAGWANT NGEDVALIDA
     IIKQVEDDLC IDQSSRFATG FSWGGGMSYA LACARAKEFR AVSVLSGGVI SGCEGGHDPI
     AYLGIHGISD PVLPFDGGVT LANKFAANNG CQQAYVGKPG LGSHSSVQTD FKGCSRPVSF
     IAYDGGHDAA PLGVGNPLAP DATWKFFMAA