ID   FAEA_TALSN              Reviewed;          49 AA.
AC   P0CT85;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Feruloyl esterase A {ECO:0000303|PubMed:15006424};
DE            EC=3.1.1.73 {ECO:0000269|PubMed:15006424};
DE   AltName: Full=Ferulic acid esterase A;
DE            Short=FAE;
DE   Flags: Fragments;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=15006424; DOI=10.1016/j.jbiotec.2003.12.003;
RA   Garcia-Conesa M.T., Crepin V.F., Goldson A.J., Williamson G.,
RA   Cummings N.J., Connerton I.F., Faulds C.B., Kroon P.A.;
RT   "The feruloyl esterase system of Talaromyces stipitatus: production of
RT   three discrete feruloyl esterases, including a novel enzyme, TsFaeC, with a
RT   broad substrate specificity.";
RL   J. Biotechnol. 108:227-241(2004).
CC   -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC       feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-
CC       galactose and feruloyl-arabinose ester bonds in pectin (By similarity).
CC       Active against methyl esters of sinapate (MSA), but not caffeate (MCA)
CC       (PubMed:15006424). {ECO:0000250|UniProtKB:O42807,
CC       ECO:0000269|PubMed:15006424}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC         EC=3.1.1.73; Evidence={ECO:0000269|PubMed:15006424};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O42807}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FaeA family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0CT85; -.
DR   SMR; P0CT85; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030600; F:feruloyl esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Hydrolase;
KW   Polysaccharide degradation; Secreted; Serine esterase; Xylan degradation.
FT   CHAIN           1..>49
FT                   /note="Feruloyl esterase A"
FT                   /id="PRO_0000433996"
FT   NON_CONS        28..29
FT   NON_CONS        39..40
FT   NON_TER         49
SQ   SEQUENCE   49 AA;  5216 MW;  DA38F77428FFEECC CRC64;
     ASTQGISEDL YNRLVEMATI IQAAYADLAI YNAQTDINGA SGNQAFASY