ID A0A0F0ICL1_ASPPU Unreviewed; 298 AA.
AC A0A0F0ICL1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=feruloyl esterase {ECO:0000256|ARBA:ARBA00013091};
DE EC=3.1.1.73 {ECO:0000256|ARBA:ARBA00013091};
DE AltName: Full=Ferulic acid esterase A {ECO:0000256|ARBA:ARBA00041313};
GN ORFNames=P875_00010208 {ECO:0000313|EMBL:KJK65509.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK65509.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK65509.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73; Evidence={ECO:0000256|ARBA:ARBA00034075};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FaeA family.
CC {ECO:0000256|ARBA:ARBA00037991}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJK65509.1}.
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DR EMBL; JZEE01000362; KJK65509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0ICL1; -.
DR STRING; 1403190.A0A0F0ICL1; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic 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 InterPro; IPR005592; Mono/diacylglycerol_lipase_N.
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; PF03893; Lipase3_N; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022487};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..298
FT /note="feruloyl esterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002443073"
FT DOMAIN 11..78
FT /note="Mono-/di-acylglycerol lipase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03893"
FT DOMAIN 108..238
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 298 AA; 32073 MW; E1F623AE0300AFB3 CRC64;
MHHLGKVLTT FAACAGLGVA APSSSAQITP REVSPQFLQQ LTLYAQYAAA AYCSSNTNSP
NTKLTCSVGN CPLVEGANTK TLTEFEDNEA FGDVAGFLAV DESNQQIVLS FRGTRSIETW
AANVQLGKED VDELCDGCEV HTGFWKSWES VATATLDSVK KALQAYPGFK LAVTGHSFGA
AVGTLAATVL RNSGSEVSLY TYGSPRVGNE EFADYVSGQG PNFRVTHSND IVPRLPPRLL
GYHQTSPEYW IPSGNNEPVG TADVEMINEA DSDMGNAGQK TQSIEAHKWY TDHIYECK
//
