ID   FAEA_ASPTN              Reviewed;         281 AA.
AC   Q0CBM7;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=ATEG_08907;
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 (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; CH476606; EAU31039.1; -; Genomic_DNA.
DR   RefSeq; XP_001217493.1; XM_001217492.1.
DR   AlphaFoldDB; Q0CBM7; -.
DR   SMR; Q0CBM7; -.
DR   STRING; 341663.Q0CBM7; -.
DR   ESTHER; asptn-faea; Lipase_3.
DR   PRIDE; Q0CBM7; -.
DR   EnsemblFungi; EAU31039; EAU31039; ATEG_08907.
DR   GeneID; 4323090; -.
DR   VEuPathDB; FungiDB:ATEG_08907; -.
DR   eggNOG; KOG4569; Eukaryota.
DR   HOGENOM; CLU_032957_1_1_1; -.
DR   OMA; HHATEYW; -.
DR   OrthoDB; 612344at2759; -.
DR   BRENDA; 3.1.1.73; 536.
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:0006629; P:lipid metabolic process; IEA:InterPro.
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; IPR002921; Fungal_lipase-like.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 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_0000393495"
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   CARBOHYD        173
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;  30294 MW;  E554B76F61A4D312 CRC64;
     MKQFSAKFAL ALSAAAGQAL AASTQGISED LYNRLVEMAT ISQAAYANMC NIPSTITVGE
     KIYNAQTDIN GWVLRDDSTK EIITVFRGTG SDTNLQLDTN YTLTPFSTFS ECSGCEVHGG
     YFIGWSSVQD QVMSLVKEQA DQYPDYTLTV TGHSLGASMA TLAAAQLSGT YDNITLYTFG
     EPRSGNEAFA SYMNDKFTAT SADTTKYFRV THSNDGIPNL PPAEQGYVHG GVEYWSVDPY
     SAQNTYVCTG DEVQCCEAQG GQGVNDAHTT YFGMTSGACT W