ID   FAEC2_ASPCL             Reviewed;         272 AA.
AC   A1CC33;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Probable feruloyl esterase C;
DE            EC=3.1.1.73;
DE   AltName: Full=Ferulic acid esterase C-2;
DE   Flags: Precursor;
GN   Name=faeC-2; ORFNames=ACLA_017480;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027049; EAW13301.1; -; Genomic_DNA.
DR   RefSeq; XP_001274727.1; XM_001274726.1.
DR   AlphaFoldDB; A1CC33; -.
DR   SMR; A1CC33; -.
DR   STRING; 344612.A1CC33; -.
DR   ESTHER; aspcl-faec2; FaeC.
DR   EnsemblFungi; EAW13301; EAW13301; ACLA_017480.
DR   GeneID; 4706641; -.
DR   KEGG; act:ACLA_017480; -.
DR   VEuPathDB; FungiDB:ACLA_017480; -.
DR   eggNOG; ENOG502SMEI; Eukaryota.
DR   HOGENOM; CLU_027551_2_0_1; -.
DR   OrthoDB; 1257904at2759; -.
DR   Proteomes; UP000006701; 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; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..272
FT                   /note="Probable feruloyl esterase C"
FT                   /id="PRO_0000394936"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   272 AA;  28967 MW;  DAA59F5ACF27B923 CRC64;
     MVHSILLYTF LALSVFLSPV FAEARSPGCG KLPNLSNGVH KINGREYTLK VPSNYDKNKA
     YHLVFGLHWR GGNMGAVVKG EGVQPWYGLE KRAHGSAIFV APNGKSAGWA NTGGQDIAFL
     DAIIKEVESN YCVDQSSRFA TGFSWGGGMS YALACSRAKQ FKAVSVLSGG LISGCSGGND
     PIAYLAIHGI KDNVLPFNGG ISLANRFVKN NRCHQSEIHT PKSGSRSSVR TDFRGCSKPV
     SFIAYDGGHD AAPLGVGSSL APDATWKFFM AA