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Feruloyl esterase A (EC 3.1.1.73) (Cinnamoyl esterase) (FAE-III) (Ferulic acid esterase A)

 FAEA_ASPNG              Reviewed;         281 AA.
O42807; B8XRG2; D2K873; Q96W70;
24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 99.
RecName: Full=Feruloyl esterase A;
EC=3.1.1.73;
AltName: Full=Cinnamoyl esterase;
AltName: Full=FAE-III;
AltName: Full=Ferulic acid esterase A;
Flags: Precursor;
Name=faeA;
Aspergillus niger.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=5061;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-107 AND
134-179, MASS SPECTROMETRY, FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
PubMed=9406381;
de Vries R.P., Michelsen B., Poulsen C.H., Kroon P.A.,
van den Heuvel R.H.H., Faulds C.B., Williamson G.,
van den Hombergh J.P.T.W., Visser J.;
"The faeA genes from Aspergillus niger and Aspergillus tubingensis
encode ferulic acid esterases involved in degradation of complex cell
wall polysaccharides.";
Appl. Environ. Microbiol. 63:4638-4644(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12702357; DOI=10.1111/j.1567-1364.2001.tb00023.x;
Juge N., Williamson G., Puigserver A., Cummings N.J., Connerton I.F.,
Faulds C.B.;
"High-level production of recombinant Aspergillus niger cinnamoyl
esterase (FAEA) in the methylotrophic yeast Pichia pastoris.";
FEMS Yeast Res. 1:127-132(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CIB423.1;
Zhang S., Pei X., Wu Z.;
"Cloning and directed evolution of feruloyl esterase from Aspergillus
niger.";
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Hu X.S., Li X.L.;
"Molecular docking of feruloyl esterase A and ferulic acid substrate
using computer modeling.";
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
DOI=10.1099/00221287-140-4-779;
Faulds C.B., Williamson G.;
"Purification and characterisation of a ferulic acid esterase (FAE-
III) from Aspergillus niger: specificity for the phenolic moiety and
binding to microcrystalline cellulose.";
Microbiology 140:779-787(1994).
[6]
FUNCTION.
PubMed=7805053; DOI=10.1016/0008-6215(94)00177-4;
Ralet M.C., Faulds C.B., Williamson G., Thibault J.F.;
"Degradation of feruloylated oligosaccharides from sugar-beet pulp and
wheat bran by ferulic acid esterases from Aspergillus niger.";
Carbohydr. Res. 263:257-269(1994).
[7]
FUNCTION, AND ENZYME REGULATION.
PubMed=9649839; DOI=10.1042/bst026s164;
Aliwan F.O., Williamson G.;
"Identification of active site residues in a ferulic acid esterase
(FAE-III) from Aspergillus niger.";
Biochem. Soc. Trans. 26:S164-S164(1998).
[8]
INDUCTION.
PubMed=10584009;
de Vries R.P., Visser J.;
"Regulation of the feruloyl esterase (faeA) gene from Aspergillus
niger.";
Appl. Environ. Microbiol. 65:5500-5503(1999).
[9]
FUNCTION, AND INDUCTION.
STRAIN=ATCC 9089 / N402;
PubMed=11931668; DOI=10.1042/0264-6021:3630377;
de Vries R.P., vanKuyk P.A., Kester H.C., Visser J.;
"The Aspergillus niger faeB gene encodes a second feruloyl esterase
involved in pectin and xylan degradation and is specifically induced
in the presence of aromatic compounds.";
Biochem. J. 363:377-386(2002).
[10]
X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 22-281 IN COMPLEX WITH
FERULIC ACID.
PubMed=15103133; DOI=10.1107/S0907444904004937;
McAuley K.E., Svendsen A., Patkar S.A., Wilson K.S.;
"Structure of a feruloyl esterase from Aspergillus niger.";
Acta Crystallogr. D 60:878-887(2004).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-281, DISULFIDE BONDS,
FUNCTION, AND MUTAGENESIS OF SER-154.
PubMed=15081808; DOI=10.1016/j.jmb.2004.03.003;
Hermoso J.A., Sanz-Aparicio J., Molina R., Juge N., Gonzalez R.,
Faulds C.B.;
"The crystal structure of feruloyl esterase A from Aspergillus niger
suggests evolutive functional convergence in feruloyl esterase
family.";
J. Mol. Biol. 338:495-506(2004).
[12]
X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 22-281 OF MUTANT SER-154 IN
COMPLEX WITH SUBSTRATE, AND MUTAGENESIS OF TYR-101 AND TRP-281.
PubMed=16128806; DOI=10.1111/j.1742-4658.2005.04849.x;
Faulds C.B., Molina R., Gonzalez R., Husband F., Juge N.,
Sanz-Aparicio J., Hermoso J.A.;
"Probing the determinants of substrate specificity of a feruloyl
esterase, AnFaeA, from Aspergillus niger.";
FEBS J. 272:4362-4371(2005).
[13]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 22-281, GLYCOSYLATION,
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17027758; DOI=10.1016/j.febslet.2006.09.039;
Benoit I., Asther M., Sulzenbacher G., Record E., Marmuse L.,
Parsiegla G., Gimbert I., Asther M., Bignon C.;
"Respective importance of protein folding and glycosylation in the
thermal stability of recombinant feruloyl esterase A.";
FEBS Lett. 580:5815-5821(2006).
-!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes
the feruloyl-arabinose ester bond in arabinoxylans, and the
feruloyl-galactose ester bond in pectin. Binds to cellulose.
{ECO:0000269|PubMed:11931668, ECO:0000269|PubMed:15081808,
ECO:0000269|PubMed:17027758, ECO:0000269|PubMed:7805053,
ECO:0000269|PubMed:9406381, ECO:0000269|PubMed:9649839,
ECO:0000269|Ref.5}.
-!- CATALYTIC ACTIVITY: Feruloyl-polysaccharide + H(2)O = ferulate +
polysaccharide.
-!- ENZYME REGULATION: Inhibited by the specific serine esterase
inhibitor diisopropylfluorophosphate.
{ECO:0000269|PubMed:9649839}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.31 mM for methyl ferulate {ECO:0000269|PubMed:17027758};
pH dependence:
Optimum pH is 5.0. {ECO:0000269|PubMed:17027758};
Temperature dependence:
Optimum temperature is 55-60 degrees Celsius.
{ECO:0000269|PubMed:17027758};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9406381,
ECO:0000269|Ref.5}.
-!- INDUCTION: By xylose and arabinose, probably via the xylanolytic
transcriptional activator XlnR. By ferulic acid, vanillic acid and
other aromatic residues with the following substituants on the
aromatic ring: a methoxy group at C-3, a hydroxy group at C-4 and
an unsubstituted C-5. Repressed by simple sugars, probably via the
carbon catabolite repressor protein CreA.
{ECO:0000269|PubMed:10584009, ECO:0000269|PubMed:11931668}.
-!- PTM: Glycosylated. {ECO:0000305|PubMed:17027758}.
-!- MASS SPECTROMETRY: Mass=29738; Mass_error=50; Method=MALDI;
Range=22-281; Evidence={ECO:0000269|PubMed:9406381};
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. FaeA family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y09330; CAA70510.1; -; Genomic_DNA.
EMBL; AF361950; AAK60631.1; -; mRNA.
EMBL; FJ430154; ACJ64498.1; -; mRNA.
EMBL; GU188042; ACZ95366.1; -; mRNA.
PDB; 1USW; X-ray; 2.50 A; A=22-281.
PDB; 1UWC; X-ray; 1.08 A; A/B=22-281.
PDB; 1UZA; X-ray; 1.50 A; A/B=22-281.
PDB; 2BJH; X-ray; 2.54 A; A/B/C=22-281.
PDB; 2HL6; X-ray; 1.55 A; A/B=22-281.
PDB; 2IX9; X-ray; 1.70 A; A/B=22-281.
PDBsum; 1USW; -.
PDBsum; 1UWC; -.
PDBsum; 1UZA; -.
PDBsum; 2BJH; -.
PDBsum; 2HL6; -.
PDBsum; 2IX9; -.
ProteinModelPortal; O42807; -.
SMR; O42807; -.
ESTHER; aspni-FAEA; Lipase_3.
mycoCLAP; FAEA_ASPNG; -.
iPTMnet; O42807; -.
PaxDb; O42807; -.
eggNOG; KOG4569; Eukaryota.
eggNOG; COG3675; LUCA.
BioCyc; MetaCyc:MONOMER-16832; -.
BRENDA; 3.1.1.73; 518.
EvolutionaryTrace; O42807; -.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0030248; F:cellulose binding; IDA:UniProtKB.
GO; GO:0030600; F:feruloyl esterase activity; IDA:UniProtKB.
GO; GO:0016998; P:cell wall macromolecule catabolic process; IDA:UniProtKB.
GO; GO:0030245; P:cellulose catabolic process; IDA:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002921; Fungal_lipase-like.
Pfam; PF01764; Lipase_3; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00120; LIPASE_SER; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Polysaccharide degradation;
Secreted; Serine esterase; Signal; Xylan degradation.
SIGNAL 1 21 {ECO:0000269|PubMed:9406381}.
CHAIN 22 281 Feruloyl esterase A.
/FTId=PRO_0000021226.
ACT_SITE 154 154 Nucleophile.
{ECO:0000269|PubMed:15081808}.
ACT_SITE 215 215 Charge relay system.
{ECO:0000305|PubMed:15103133}.
ACT_SITE 268 268 Charge relay system.
{ECO:0000305|PubMed:15103133}.
BINDING 98 98 Substrate. {ECO:0000269|PubMed:16128806}.
BINDING 101 101 Substrate. {ECO:0000269|PubMed:16128806}.
BINDING 268 268 Substrate. {ECO:0000269|PubMed:16128806}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17027758}.
DISULFID 50 279 {ECO:0000269|PubMed:15081808}.
DISULFID 112 115 {ECO:0000269|PubMed:15081808}.
DISULFID 248 255 {ECO:0000269|PubMed:15081808}.
MUTAGEN 101 101 Y->V,S: Decreases feruloyl esterase
activity. {ECO:0000269|PubMed:16128806}.
MUTAGEN 154 154 S->A: Impairs catalytic activity.
{ECO:0000269|PubMed:15081808}.
MUTAGEN 281 281 W->V,S: Decreases feruloyl esterase
activity. {ECO:0000269|PubMed:16128806}.
CONFLICT 13 13 L -> S (in Ref. 3; ACJ64498).
{ECO:0000305}.
CONFLICT 23 23 S -> F (in Ref. 4; ACZ95366).
{ECO:0000305}.
CONFLICT 44 44 A -> P (in Ref. 4; ACZ95366).
{ECO:0000305}.
CONFLICT 56 56 I -> T (in Ref. 3; ACJ64498).
{ECO:0000305}.
CONFLICT 107 107 D -> E (in Ref. 3; ACJ64498).
{ECO:0000305}.
CONFLICT 113 113 N -> S (in Ref. 3; ACJ64498).
{ECO:0000305}.
CONFLICT 128 128 V -> I (in Ref. 3; ACJ64498).
{ECO:0000305}.
CONFLICT 142 142 Q -> K (in Ref. 4; ACZ95366).
{ECO:0000305}.
CONFLICT 150 150 V -> M (in Ref. 3; ACJ64498).
{ECO:0000305}.
CONFLICT 159 159 M -> L (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 174 174 V -> I (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 205 205 T -> I (in Ref. 4; ACZ95366).
{ECO:0000305}.
CONFLICT 208 208 F -> S (in Ref. 3; ACJ64498).
{ECO:0000305}.
CONFLICT 224 224 D -> E (in Ref. 2; AAK60631, 3; ACJ64498
and 4; ACZ95366). {ECO:0000305}.
CONFLICT 225 225 E -> Q (in Ref. 2; AAK60631 and 3;
ACJ64498). {ECO:0000305}.
CONFLICT 264 264 V -> A (in Ref. 3; ACJ64498).
{ECO:0000305}.
STRAND 23 25 {ECO:0000244|PDB:1UWC}.
HELIX 29 44 {ECO:0000244|PDB:1UWC}.
TURN 45 51 {ECO:0000244|PDB:1UWC}.
STRAND 56 64 {ECO:0000244|PDB:1UWC}.
TURN 65 68 {ECO:0000244|PDB:1UWC}.
STRAND 69 76 {ECO:0000244|PDB:1UWC}.
TURN 77 80 {ECO:0000244|PDB:1UWC}.
STRAND 81 86 {ECO:0000244|PDB:1UWC}.
HELIX 92 98 {ECO:0000244|PDB:1UWC}.
STRAND 103 105 {ECO:0000244|PDB:1UWC}.
STRAND 116 118 {ECO:0000244|PDB:1UWC}.
HELIX 119 142 {ECO:0000244|PDB:1UWC}.
STRAND 146 153 {ECO:0000244|PDB:1UWC}.
HELIX 155 168 {ECO:0000244|PDB:1UWC}.
STRAND 172 180 {ECO:0000244|PDB:1UWC}.
HELIX 187 196 {ECO:0000244|PDB:1UWC}.
TURN 197 200 {ECO:0000244|PDB:1UWC}.
TURN 202 204 {ECO:0000244|PDB:1UWC}.
STRAND 206 212 {ECO:0000244|PDB:1UWC}.
HELIX 217 219 {ECO:0000244|PDB:1UWC}.
HELIX 223 225 {ECO:0000244|PDB:1UWC}.
STRAND 231 236 {ECO:0000244|PDB:1UWC}.
HELIX 242 244 {ECO:0000244|PDB:1UWC}.
STRAND 245 248 {ECO:0000244|PDB:1UWC}.
STRAND 250 252 {ECO:0000244|PDB:1UWC}.
HELIX 255 259 {ECO:0000244|PDB:1UWC}.
HELIX 266 269 {ECO:0000244|PDB:1UWC}.
STRAND 274 277 {ECO:0000244|PDB:1USW}.
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


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