ID   FAED_NEUCR              Reviewed;         290 AA.
AC   Q7RWX8;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Feruloyl esterase D {ECO:0000303|PubMed:14595525};
DE            EC=3.1.1.73 {ECO:0000269|PubMed:14595525};
DE   AltName: Full=Ferulic acid esterase D;
DE            Short=FAE;
DE   Flags: Precursor;
GN   Name=faeD-3.544 {ECO:0000303|PubMed:14595525}; ORFNames=NCU08785;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=14595525; DOI=10.1007/s00253-003-1466-5;
RA   Crepin V.F., Faulds C.B., Connerton I.F.;
RT   "Identification of a type-D feruloyl esterase from Neurospora crassa.";
RL   Appl. Microbiol. Biotechnol. 63:567-570(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 ferulate (MFA), sinapate (MSA),
CC       caffeate (MCA) and p-coumarate (MpCA) (PubMed:14595525).
CC       {ECO:0000250|UniProtKB:O42807, ECO:0000269|PubMed:14595525}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC         EC=3.1.1.73; Evidence={ECO:0000269|PubMed:14595525};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O42807}.
CC   -!- SIMILARITY: Belongs to the serine esterase family. {ECO:0000305}.
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DR   EMBL; CM002238; EAA26992.1; -; Genomic_DNA.
DR   RefSeq; XP_956228.1; XM_951135.1.
DR   AlphaFoldDB; Q7RWX8; -.
DR   STRING; 5141.EFNCRP00000004770; -.
DR   ESTHER; neucr-FAED; FaeC.
DR   EnsemblFungi; EAA26992; EAA26992; NCU08785.
DR   GeneID; 3872386; -.
DR   KEGG; ncr:NCU08785; -.
DR   VEuPathDB; FungiDB:NCU08785; -.
DR   HOGENOM; CLU_027551_2_0_1; -.
DR   InParanoid; Q7RWX8; -.
DR   OMA; YAQHGTS; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR043595; FaeB/C/D.
DR   PANTHER; PTHR38050; PTHR38050; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Serine esterase; Signal; Xylan degradation.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..290
FT                   /note="Feruloyl esterase D"
FT                   /id="PRO_0000433995"
FT   REGION          260..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   290 AA;  31146 MW;  CCB003568FDCCE27 CRC64;
     MAGLHSRLTT FLLLLLSALP AIAAAAPSSG CGKGPTLRNG QTVTTNINGK SRRYTVRLPD
     NYNQNNPYRL IFLWHPLGSS MQKIIQGEDP NRGGVLPYYG LPPLDTSKSA IYVVPDGLNA
     GWANQNGEDV SFFDNILQTV SDGLCIDTNL VFSTGFSYGG GMSFSLACSR ANKVRAVAVI
     SGAQLSGCAG GNDPVAYYAQ HGTSDGVLNV AMGRQLRDRF VRNNGCQPAN GEVQPGSGGR
     STRVEYQGCQ QGKDVVWVVH GGDHNPSQRD PGQNDPFAPR NTWEFFSRFN