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Database: UniProt
Entry: A0A094EAY4_9PEZI
LinkDB: A0A094EAY4_9PEZI
Original site: A0A094EAY4_9PEZI 
ID   A0A094EAY4_9PEZI        Unreviewed;       322 AA.
AC   A0A094EAY4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=feruloyl esterase {ECO:0000256|ARBA:ARBA00013091};
DE            EC=3.1.1.73 {ECO:0000256|ARBA:ARBA00013091};
GN   ORFNames=V496_00780 {ECO:0000313|EMBL:KFY68825.1};
OS   Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY68825.1, ECO:0000313|Proteomes:UP000029302};
RN   [1] {ECO:0000313|EMBL:KFY68825.1, ECO:0000313|Proteomes:UP000029302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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   -!- 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:KFY68825.1}.
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DR   EMBL; JPJY01000115; KFY68825.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094EAY4; -.
DR   STRING; 1420909.A0A094EAY4; -.
DR   HOGENOM; CLU_027551_3_0_1; -.
DR   OrthoDB; 1940566at2759; -.
DR   Proteomes; UP000029302; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030600; F:feruloyl esterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR010126; Esterase_phb.
DR   InterPro; IPR043595; FaeB/C/D.
DR   PANTHER; PTHR38050; -; 1.
DR   PANTHER; PTHR38050:SF2; FERULOYL ESTERASE; 1.
DR   Pfam; PF10503; Esterase_PHB; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW   Serine esterase {ECO:0000256|ARBA:ARBA00022487};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..322
FT                   /note="feruloyl esterase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5032291982"
SQ   SEQUENCE   322 AA;  35034 MW;  089BCFBC3AF955A5 CRC64;
     MIFARPLAGA ALLLLGAESV GAAVMRSRAG AGCGIVQDFK GDTKTGESIK SDEILRTYDV
     YLPPNYDENK PTPLIISYHG ANGNSTKQRA LDRFDNHTWN PEHIVVWPNG YKGFWEGPSY
     ADPKISDKKF TSALITQLRA DFCVDDTRIY AAGKSNGGGF TGTLACSAEA GKNFAAIAAC
     AGAFYTDVVE DADDKCEPSR SPFPILEFHG SIDKTIPYFP KENGSGGPLP QIPDWLDTWG
     QRNGCPKDYK PAVSQLNGDE TVQETLYRCN DAAVVTGYYI EGMDHSWPST TENSDNIKHG
     DGPVSIDATP MILEFFRGIR KP
//
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