FAEB_ASPNG
ID FAEB_ASPNG Reviewed; 521 AA.
AC Q8WZI8;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Feruloyl esterase B;
DE EC=3.1.1.73 {ECO:0000269|PubMed:8679110};
DE AltName: Full=Cinnamoyl esterase {ECO:0000303|PubMed:8679110};
DE Short=CinnAE;
DE AltName: Full=FAE-I;
DE AltName: Full=Ferulic acid esterase B;
DE Short=FAEB;
DE Flags: Precursor;
GN Name=faeB;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-36 AND 252-267,
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=11931668; DOI=10.1042/0264-6021:3630377;
RA de Vries R.P., vanKuyk P.A., Kester H.C., Visser J.;
RT "The Aspergillus niger faeB gene encodes a second feruloyl esterase
RT involved in pectin and xylan degradation and is specifically induced in the
RT presence of aromatic compounds.";
RL Biochem. J. 363:377-386(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND
RP GLYCOSYLATION.
RX PubMed=8679110;
RA Kroon P.A., Faulds C.B., Williamson G.;
RT "Purification and characterization of a novel esterase induced by growth of
RT Aspergillus niger on sugar-beet pulp.";
RL Biotechnol. Appl. Biochem. 23:255-262(1996).
RN [3]
RP FUNCTION.
RX PubMed=7805053; DOI=10.1016/0008-6215(94)00177-4;
RA Ralet M.C., Faulds C.B., Williamson G., Thibault J.F.;
RT "Degradation of feruloylated oligosaccharides from sugar-beet pulp and
RT wheat bran by ferulic acid esterases from Aspergillus niger.";
RL Carbohydr. Res. 263:257-269(1994).
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.
CC {ECO:0000269|PubMed:11931668, ECO:0000269|PubMed:7805053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73; Evidence={ECO:0000269|PubMed:8679110};
CC -!- ACTIVITY REGULATION: Inhibited by the specific serine esterase
CC inhibitor AEBSF. {ECO:0000269|PubMed:8679110}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8679110}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11931668}.
CC -!- INDUCTION: By caffeic acid, p-coumaric acid and to a lesser extent by
CC ferulic acid. Repressed by simple sugars, probably via the carbon
CC catabolite repressor protein CreA. {ECO:0000269|PubMed:11931668}.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the tannase family. {ECO:0000305}.
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DR EMBL; AJ309807; CAC83933.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WZI8; -.
DR SMR; Q8WZI8; -.
DR STRING; 5061.CADANGAP00010268; -.
DR CLAE; FAEB_ASPNG; -.
DR ESTHER; aspng-faeb; Tannase.
DR VEuPathDB; FungiDB:An12g10390; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1085850; -.
DR VEuPathDB; FungiDB:ATCC64974_33570; -.
DR VEuPathDB; FungiDB:M747DRAFT_340208; -.
DR eggNOG; ENOG502QPXZ; Eukaryota.
DR BRENDA; 3.1.1.73; 518.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030600; F:feruloyl esterase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IDA:UniProtKB.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011118; Tannase/feruloyl_esterase.
DR PANTHER; PTHR33938; PTHR33938; 1.
DR Pfam; PF07519; Tannase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Polysaccharide degradation; Secreted; Serine esterase; Signal;
KW Xylan degradation.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:11931668"
FT CHAIN 18..521
FT /note="Feruloyl esterase B"
FT /id="PRO_0000033586"
FT ACT_SITE 185
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 397
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 437
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..72
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 61..111
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 184..438
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 253..270
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 279..288
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 498..520
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT CONFLICT 26
FT /note="C -> P (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 57153 MW; F93F81AAC460E5DC CRC64;
MKVASLLSLA LPGAALAATD PFQSRCNEFQ NKIDIANVTV RSVAYVAAGQ NISQAEVASV
CKASVQASVD LCRVTMNIST SDRSHLWAEA WLPRNYTGRF VSTGNGGLAG CVQETDLNFA
ANFGFATVGT NGGHDGDTAK YFLNNSEVLA DFAYRSVHEG TVVGKQLTQL FYDEGYNYSY
YLGCSTGGRQ GYQQVQRFPD DYDGVIAGSA AMNFINLISW GAFLWKATGL ADDPDFISAN
LWSVIHQEIV RQCDLVDGAL DGIIEDPDFC APVIERLICD GTTNGTSCIT GAQAAKVNRA
LSDFYGPDGT VYYPRLNYGG EADSASLYFT GSMYSRTEEW YKYVVYNDTN WNSSQWTLES
AKLALEQNPF NIQAFDPNIT AFRDRGGKLL SYHGTQDPII SSTDSKLYYR RVANALNAAP
SELDEFYRFF QISGMGHCGD GTGASYIGQG YGTYTSKAPQ VNLLRTMVDW VENGKAPEYM
PGNKLNANGS IEYMRKHCRY PKHNIHTGPG NYTDPNSWTC V
