FAEB_NEUCR
ID FAEB_NEUCR Reviewed; 292 AA.
AC Q9HGR3; Q7RVZ0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Feruloyl esterase B;
DE EC=3.1.1.73;
DE AltName: Full=Ferulic acid esterase;
DE Short=FAE;
DE Flags: Precursor;
GN Name=fae-1; ORFNames=B22K18.040, NCU09491;
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 [MRNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12435269; DOI=10.1042/bj20020917;
RA Crepin V.F., Faulds C.B., Connerton I.F.;
RT "A non-modular type B feruloyl esterase from Neurospora crassa exhibits
RT concentration-dependent substrate inhibition.";
RL Biochem. J. 370:417-427(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
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).
CC -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes of
CC the feruloyl-arabinose ester bond in arabinoxylans as well as the
CC feruloyl-galactose and feruloyl-arabinose ester bonds in pectin (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family.
CC Feruloyl esterase type B subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ293029; CAC05587.1; -; mRNA.
DR EMBL; BX842597; CAE75726.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA33979.1; -; Genomic_DNA.
DR RefSeq; XP_963215.1; XM_958122.2.
DR AlphaFoldDB; Q9HGR3; -.
DR SMR; Q9HGR3; -.
DR STRING; 5141.EFNCRP00000009285; -.
DR ESTHER; neucr-faeb; Esterase_phb.
DR EnsemblFungi; EAA33979; EAA33979; NCU09491.
DR GeneID; 3879354; -.
DR KEGG; ncr:NCU09491; -.
DR VEuPathDB; FungiDB:NCU09491; -.
DR HOGENOM; CLU_027551_1_1_1; -.
DR InParanoid; Q9HGR3; -.
DR OMA; PRCAMEA; -.
DR BRENDA; 3.1.1.73; 3627.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0030600; F:feruloyl esterase activity; ISS:UniProtKB.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; ISS:UniProtKB.
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; IPR010126; Esterase_phb.
DR Pfam; PF10503; Esterase_PHB; 1.
DR SUPFAM; SSF53474; SSF53474; 2.
DR TIGRFAMs; TIGR01840; esterase_phb; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Serine esterase;
KW Signal; Xylan degradation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..292
FT /note="Feruloyl esterase B"
FT /id="PRO_0000021228"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 37
FT /note="Y -> H (in Ref. 1; CAC05587)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="Y -> C (in Ref. 1; CAC05587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 31084 MW; 9EE5A070F4E42821 CRC64;
MLPRTLLGLA LTAATGLCAS LQQVTNWGSN PTNIRMYTYV PDKLATKPAI IVALHGCGGT
APSWYSGTRL PSYADQYGFI LIYPGTPNMS NCWGVNDPAS LTHGAGGDSL GIVAMVNYTI
AKYNADASRV YVMGTSSGGM MTNVMAATYP EVFEAGAAYS GVAHACFAGA ASATPFSPNQ
TCARGLQHTP EEWGNFVRNS YPGYTGRRPR MQIYHGLADN LVYPRCAMEA LKQWSNVLGV
EFSRNVSGVP SQAYTQIVYG DGSKLVGYMG AGVGHVAPTN EQVMLKFFGL IN
