ID   FAEC_ASPTN              Reviewed;         270 AA.
AC   Q0CDX2;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=ATEG_08112;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476605; EAU31285.1; -; Genomic_DNA.
DR   RefSeq; XP_001216733.1; XM_001216733.1.
DR   AlphaFoldDB; Q0CDX2; -.
DR   SMR; Q0CDX2; -.
DR   STRING; 341663.Q0CDX2; -.
DR   ESTHER; asptn-faec; FaeC.
DR   EnsemblFungi; EAU31285; EAU31285; ATEG_08112.
DR   GeneID; 4353506; -.
DR   VEuPathDB; FungiDB:ATEG_08112; -.
DR   eggNOG; ENOG502SMEI; Eukaryota.
DR   HOGENOM; CLU_027551_2_0_1; -.
DR   OMA; SSGCGKQ; -.
DR   OrthoDB; 1257904at2759; -.
DR   Proteomes; UP000007963; 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   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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..270
FT                   /note="Probable feruloyl esterase C"
FT                   /id="PRO_0000394941"
SQ   SEQUENCE   270 AA;  27939 MW;  C76601F82BF49ACF CRC64;
     MAILSRLLTT VTLGSLLTSA VAQSSGCGKQ PTLTNGVQNI NGREYILNIP EGYDSSKQYK
     LIFGLHWLGG SMNDVVSGNS IEPWYGLESR AEGSAIFVAP NGLNAGWANN GGEDTALMDA
     IIEAVEADLC IDQSSRFATG FSFGGGMSYA LACARASKFR AVSVLSGGVI SGCDGGNDPI
     AYLGIHGIND PVLPIDGGIE MANKFVQNNG CQSADVGRPN SGSGQSVRTD FQGCSRPVSF
     IAYDGGHEGA PLGVGNPLAP DATWEFFTGA