ID   FAEA_ASPOR              Reviewed;         281 AA.
AC   Q2UNW5;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=AO090001000207;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007154; BAE56750.1; -; Genomic_DNA.
DR   RefSeq; XP_001818752.1; XM_001818700.1.
DR   AlphaFoldDB; Q2UNW5; -.
DR   SMR; Q2UNW5; -.
DR   STRING; 510516.Q2UNW5; -.
DR   ESTHER; aspor-q2unw5; Lipase_3.
DR   EnsemblFungi; BAE56750; BAE56750; AO090001000207.
DR   GeneID; 5990723; -.
DR   KEGG; aor:AO090001000207; -.
DR   VEuPathDB; FungiDB:AO090001000207; -.
DR   HOGENOM; CLU_032957_1_1_1; -.
DR   OMA; HHATEYW; -.
DR   BRENDA; 3.1.1.73; 522.
DR   Proteomes; UP000006564; Chromosome 2.
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_0000393494"
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;  30246 MW;  B1C961A0FF378716 CRC64;
     MKNFFSMHAI LLACSAGAGL AAITQGISEG TYSRIVEMAT ISQAAYANLC NIPPAITSAG
     KIYNAETDIN GWVLRDDSRQ EIITVFRGTG SDTNLQLDTN YTQAPFDTLP QCSGCAVHGG
     YYVGWVSVKD QVEGLIHQQA SQYPDYSLVV TGHSLGASMA AITAAQLSAT YNNITVYTFG
     EPRTGNQAYA SYVDETFQAT NPDATKFYRV THTNDGIPNL PPTSQGYVHH GTEYWSVEPH
     GPQNMYLCLG DEVQCCEAQG GQGVNDAHVT YFGMASGACT W