ID A0A395H6B9_9EURO Unreviewed; 286 AA.
AC A0A395H6B9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=BO80DRAFT_401496 {ECO:0000313|EMBL:RAL03461.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL03461.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAL03461.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL03461.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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}.
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DR EMBL; KZ824427; RAL03461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395H6B9; -.
DR STRING; 1448316.A0A395H6B9; -.
DR VEuPathDB; FungiDB:BO80DRAFT_401496; -.
DR OrthoDB; 2167487at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
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.
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:UP000249402};
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..286
FT /note="feruloyl esterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017388379"
FT DOMAIN 87..220
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 286 AA; 30296 MW; E98960CED1FDE694 CRC64;
MRVAQSSLLG GLALTPLALA VPMLQSRATS DTAEWTELHR AAQLASAAYT GCTGSAFDVT
VTKQINDLVT DTQGFIGYST EKKRITVAMR GSTTMTDIQN DVDTTLVEPT LSGVNFPSGA
KMMHGIYSPW SSVHDDVISE VKSLVEQYPD YSLESTGHSL GGSLTYISYI ALAQNFPGKQ
LISNALAAFP IGNEAFANFG ASQNGTLNRG NNADDGVPNM YIMWPWDFVH YGTEYYSSGT
QATTVKCSGE RDTSCSAGNG QLGVTAGHFS NFGIAMGMAG CSSSLL
//
