ID FAEA_ASPFN Reviewed; 281 AA.
AC B8NIB8;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 27-MAR-2024, entry version 62.
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=AFLA_066140;
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 (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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EED49792.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EQ963479; EED49792.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002380173.1; XM_002380132.1.
DR AlphaFoldDB; B8NIB8; -.
DR SMR; B8NIB8; -.
DR STRING; 332952.B8NIB8; -.
DR ESTHER; aspor-q2unw5; Lipase_3.
DR GlyCosmos; B8NIB8; 2 sites, No reported glycans.
DR EnsemblFungi; EED49792; EED49792; AFLA_066140.
DR VEuPathDB; FungiDB:AFLA_008548; -.
DR eggNOG; KOG4569; Eukaryota.
DR OrthoDB; 91669at2759; -.
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:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00519; Lipase_3; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR46640:SF1; LIPASE_3 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46640; TRIACYLGLYCEROL LIPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G06510)-RELATED; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Hydrolase;
KW Polysaccharide degradation; Secreted; Serine esterase; Signal;
KW Xylan degradation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..281
FT /note="Probable feruloyl esterase A"
FT /id="PRO_0000393493"
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; 30222 MW; 0F6C4DF43D07A550 CRC64;
MKNFVSMHAI LLACSAGAGL AAITQGISEG TYSRIVEMAT ISQAAYANLC NIPSTITSAG
KIYNAETDIN GWVLRDDSRQ EIITVFRGTG SDTNLQLDTN YTQAPFDTLP QCSGCAVHGG
YYVGWISVKD QVEGLVQQQA SQYPDYSLVI TGHSLGASMA AITAAQLSAT YNNITVYTFG
EPRTGNQAYA SYVDETFQAT NPDATKFYRV THTNDGIPNL PPTSQGYVHH GTEYWSVEPH
GPQNMYLCLG DEVQCCEAQG GQGVNDAHVT YFGMASGACT W
//
