FAEA_ASPNG
ID FAEA_ASPNG Reviewed; 281 AA.
AC O42807; B8XRG2; D2K873; Q96W70;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Feruloyl esterase A;
DE EC=3.1.1.73;
DE AltName: Full=Cinnamoyl esterase;
DE AltName: Full=FAE-III;
DE AltName: Full=Ferulic acid esterase A;
DE Flags: Precursor;
GN Name=faeA;
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 22-107 AND 134-179,
RP MASS SPECTROMETRY, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=9406381; DOI=10.1128/aem.63.12.4638-4644.1997;
RA de Vries R.P., Michelsen B., Poulsen C.H., Kroon P.A.,
RA van den Heuvel R.H.H., Faulds C.B., Williamson G.,
RA van den Hombergh J.P.T.W., Visser J.;
RT "The faeA genes from Aspergillus niger and Aspergillus tubingensis encode
RT ferulic acid esterases involved in degradation of complex cell wall
RT polysaccharides.";
RL Appl. Environ. Microbiol. 63:4638-4644(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12702357; DOI=10.1111/j.1567-1364.2001.tb00023.x;
RA Juge N., Williamson G., Puigserver A., Cummings N.J., Connerton I.F.,
RA Faulds C.B.;
RT "High-level production of recombinant Aspergillus niger cinnamoyl esterase
RT (FAEA) in the methylotrophic yeast Pichia pastoris.";
RL FEMS Yeast Res. 1:127-132(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CIB423.1;
RA Zhang S., Pei X., Wu Z.;
RT "Cloning and directed evolution of feruloyl esterase from Aspergillus
RT niger.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hu X.S., Li X.L.;
RT "Molecular docking of feruloyl esterase A and ferulic acid substrate using
RT computer modeling.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX DOI=10.1099/00221287-140-4-779;
RA Faulds C.B., Williamson G.;
RT "Purification and characterisation of a ferulic acid esterase (FAE-III)
RT from Aspergillus niger: specificity for the phenolic moiety and binding to
RT microcrystalline cellulose.";
RL Microbiology 140:779-787(1994).
RN [6]
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).
RN [7]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=9649839; DOI=10.1042/bst026s164;
RA Aliwan F.O., Williamson G.;
RT "Identification of active site residues in a ferulic acid esterase (FAE-
RT III) from Aspergillus niger.";
RL Biochem. Soc. Trans. 26:S164-S164(1998).
RN [8]
RP INDUCTION.
RX PubMed=10584009; DOI=10.1128/aem.65.12.5500-5503.1999;
RA de Vries R.P., Visser J.;
RT "Regulation of the feruloyl esterase (faeA) gene from Aspergillus niger.";
RL Appl. Environ. Microbiol. 65:5500-5503(1999).
RN [9]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 9089 / N402;
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 22-281 IN COMPLEX WITH FERULIC
RP ACID.
RX PubMed=15103133; DOI=10.1107/s0907444904004937;
RA McAuley K.E., Svendsen A., Patkar S.A., Wilson K.S.;
RT "Structure of a feruloyl esterase from Aspergillus niger.";
RL Acta Crystallogr. D 60:878-887(2004).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-281, DISULFIDE BONDS, FUNCTION,
RP AND MUTAGENESIS OF SER-154.
RX PubMed=15081808; DOI=10.1016/j.jmb.2004.03.003;
RA Hermoso J.A., Sanz-Aparicio J., Molina R., Juge N., Gonzalez R.,
RA Faulds C.B.;
RT "The crystal structure of feruloyl esterase A from Aspergillus niger
RT suggests evolutive functional convergence in feruloyl esterase family.";
RL J. Mol. Biol. 338:495-506(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 22-281 OF MUTANT SER-154 IN
RP COMPLEX WITH SUBSTRATE, AND MUTAGENESIS OF TYR-101 AND TRP-281.
RX PubMed=16128806; DOI=10.1111/j.1742-4658.2005.04849.x;
RA Faulds C.B., Molina R., Gonzalez R., Husband F., Juge N., Sanz-Aparicio J.,
RA Hermoso J.A.;
RT "Probing the determinants of substrate specificity of a feruloyl esterase,
RT AnFaeA, from Aspergillus niger.";
RL FEBS J. 272:4362-4371(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 22-281, GLYCOSYLATION, FUNCTION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17027758; DOI=10.1016/j.febslet.2006.09.039;
RA Benoit I., Asther M., Sulzenbacher G., Record E., Marmuse L., Parsiegla G.,
RA Gimbert I., Asther M., Bignon C.;
RT "Respective importance of protein folding and glycosylation in the thermal
RT stability of recombinant feruloyl esterase A.";
RL FEBS Lett. 580:5815-5821(2006).
CC -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-
CC galactose ester bond in pectin. Binds to cellulose.
CC {ECO:0000269|PubMed:11931668, ECO:0000269|PubMed:15081808,
CC ECO:0000269|PubMed:17027758, ECO:0000269|PubMed:7805053,
CC ECO:0000269|PubMed:9406381, ECO:0000269|PubMed:9649839,
CC ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73;
CC -!- ACTIVITY REGULATION: Inhibited by the specific serine esterase
CC inhibitor diisopropylfluorophosphate. {ECO:0000269|PubMed:9649839}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.31 mM for methyl ferulate {ECO:0000269|PubMed:17027758};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:17027758};
CC Temperature dependence:
CC Optimum temperature is 55-60 degrees Celsius.
CC {ECO:0000269|PubMed:17027758};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9406381,
CC ECO:0000269|Ref.5}.
CC -!- INDUCTION: By xylose and arabinose, probably via the xylanolytic
CC transcriptional activator XlnR. By ferulic acid, vanillic acid and
CC other aromatic residues with the following substituants on the aromatic
CC ring: a methoxy group at C-3, a hydroxy group at C-4 and an
CC unsubstituted C-5. Repressed by simple sugars, probably via the carbon
CC catabolite repressor protein CreA. {ECO:0000269|PubMed:10584009,
CC ECO:0000269|PubMed:11931668}.
CC -!- PTM: Glycosylated. {ECO:0000305|PubMed:17027758}.
CC -!- MASS SPECTROMETRY: Mass=29738; Mass_error=50; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9406381};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FaeA family.
CC {ECO:0000305}.
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DR EMBL; Y09330; CAA70510.1; -; Genomic_DNA.
DR EMBL; AF361950; AAK60631.1; -; mRNA.
DR EMBL; FJ430154; ACJ64498.1; -; mRNA.
DR EMBL; GU188042; ACZ95366.1; -; mRNA.
DR PDB; 1USW; X-ray; 2.50 A; A=22-281.
DR PDB; 1UWC; X-ray; 1.08 A; A/B=22-281.
DR PDB; 1UZA; X-ray; 1.50 A; A/B=22-281.
DR PDB; 2BJH; X-ray; 2.54 A; A/B/C=22-281.
DR PDB; 2HL6; X-ray; 1.55 A; A/B=22-281.
DR PDB; 2IX9; X-ray; 1.70 A; A/B=22-281.
DR PDBsum; 1USW; -.
DR PDBsum; 1UWC; -.
DR PDBsum; 1UZA; -.
DR PDBsum; 2BJH; -.
DR PDBsum; 2HL6; -.
DR PDBsum; 2IX9; -.
DR AlphaFoldDB; O42807; -.
DR SMR; O42807; -.
DR STRING; 5061.CADANGAP00007416; -.
DR CLAE; FAEA_ASPNG; -.
DR ESTHER; aspni-FAEA; Lipase_3.
DR iPTMnet; O42807; -.
DR VEuPathDB; FungiDB:An09g00120; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1180590; -.
DR VEuPathDB; FungiDB:ATCC64974_6040; -.
DR VEuPathDB; FungiDB:M747DRAFT_361454; -.
DR eggNOG; KOG4569; Eukaryota.
DR BioCyc; MetaCyc:MON-16832; -.
DR BRENDA; 3.1.1.73; 518.
DR EvolutionaryTrace; O42807; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030248; F:cellulose binding; IDA:UniProtKB.
DR GO; GO:0030600; F:feruloyl esterase activity; IDA:UniProtKB.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IDA:UniProtKB.
DR GO; GO:0030245; P:cellulose catabolic process; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
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; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Polysaccharide degradation;
KW Secreted; Serine esterase; Signal; Xylan degradation.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:9406381"
FT CHAIN 22..281
FT /note="Feruloyl esterase A"
FT /id="PRO_0000021226"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:15081808"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:15103133"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:15103133"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16128806"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16128806"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16128806"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17027758"
FT DISULFID 50..279
FT /evidence="ECO:0000269|PubMed:15081808"
FT DISULFID 112..115
FT /evidence="ECO:0000269|PubMed:15081808"
FT DISULFID 248..255
FT /evidence="ECO:0000269|PubMed:15081808"
FT MUTAGEN 101
FT /note="Y->V,S: Decreases feruloyl esterase activity."
FT /evidence="ECO:0000269|PubMed:16128806"
FT MUTAGEN 154
FT /note="S->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:15081808"
FT MUTAGEN 281
FT /note="W->V,S: Decreases feruloyl esterase activity."
FT /evidence="ECO:0000269|PubMed:16128806"
FT CONFLICT 13
FT /note="L -> S (in Ref. 3; ACJ64498)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="S -> F (in Ref. 4; ACZ95366)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="A -> P (in Ref. 4; ACZ95366)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="I -> T (in Ref. 3; ACJ64498)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="D -> E (in Ref. 3; ACJ64498)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="N -> S (in Ref. 3; ACJ64498)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="V -> I (in Ref. 3; ACJ64498)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="Q -> K (in Ref. 4; ACZ95366)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="V -> M (in Ref. 3; ACJ64498)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="M -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="V -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="T -> I (in Ref. 4; ACZ95366)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="F -> S (in Ref. 3; ACJ64498)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="D -> E (in Ref. 2; AAK60631, 3; ACJ64498 and 4;
FT ACZ95366)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="E -> Q (in Ref. 2; AAK60631 and 3; ACJ64498)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="V -> A (in Ref. 3; ACJ64498)"
FT /evidence="ECO:0000305"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1UWC"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:1UWC"
FT TURN 45..51
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:1UWC"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:1UWC"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1UWC"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1UWC"
FT HELIX 119..142
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:1UWC"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:1UWC"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:1UWC"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:1UWC"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:1UWC"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1UWC"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:1UWC"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1UWC"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:1UWC"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1UWC"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:1USW"
SQ SEQUENCE 281 AA; 30537 MW; 8B4322B72710BBF3 CRC64;
MKQFSAKYAL ILLATAGQAL AASTQGISED LYNRLVEMAT ISQAAYADLC NIPSTIIKGE
KIYNAQTDIN GWILRDDTSK EIITVFRGTG SDTNLQLDTN YTLTPFDTLP QCNDCEVHGG
YYIGWISVQD QVESLVKQQA SQYPDYALTV TGHSLGASMA ALTAAQLSAT YDNVRLYTFG
EPRSGNQAFA SYMNDAFQVS SPETTQYFRV THSNDGIPNL PPADEGYAHG GVEYWSVDPY
SAQNTFVCTG DEVQCCEAQG GQGVNDAHTT YFGMTSGACT W
