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Protein

Feruloyl esterase A

Gene

faeA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

Feruloyl-polysaccharide + H2O = ferulate + polysaccharide.

Enzyme regulationi

Inhibited by the specific serine esterase inhibitor diisopropylfluorophosphate.1 Publication

Kineticsi

  1. KM=0.31 mM for methyl ferulate1 Publication

    pH dependencei

    Optimum pH is 5.0.1 Publication

    Temperature dependencei

    Optimum temperature is 55-60 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei98 – 981Substrate1 Publication
    Binding sitei101 – 1011Substrate1 Publication
    Active sitei154 – 1541Nucleophile1 Publication
    Active sitei215 – 2151Charge relay system1 Publication
    Active sitei268 – 2681Charge relay system1 Publication
    Binding sitei268 – 2681Substrate1 Publication

    GO - Molecular functioni

    • cellulose binding Source: UniProtKB
    • feruloyl esterase activity Source: UniProtKB

    GO - Biological processi

    • cellulose catabolic process Source: UniProtKB
    • cell wall macromolecule catabolic process Source: UniProtKB
    • lipid metabolic process Source: InterPro
    • pectin catabolic process Source: UniProtKB
    • xylan catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16832.
    BRENDAi3.1.1.73. 518.

    Protein family/group databases

    ESTHERiaspni-FAEA. Lipase_3.
    mycoCLAPiFAE1A_ASPNG.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Feruloyl esterase A (EC:3.1.1.73)
    Alternative name(s):
    Cinnamoyl esterase
    FAE-III
    Ferulic acid esterase A
    Gene namesi
    Name:faeA
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011Y → V or S: Decreases feruloyl esterase activity. 1 Publication
    Mutagenesisi154 – 1541S → A: Impairs catalytic activity. 1 Publication
    Mutagenesisi281 – 2811W → V or S: Decreases feruloyl esterase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21211 PublicationAdd
    BLAST
    Chaini22 – 281260Feruloyl esterase APRO_0000021226Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi50 ↔ 2791 Publication
    Glycosylationi100 – 1001N-linked (GlcNAc...)1 Publication
    Disulfide bondi112 ↔ 1151 Publication
    Disulfide bondi248 ↔ 2551 Publication

    Post-translational modificationi

    Glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO42807.

    Expressioni

    Inductioni

    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.2 Publications

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00007416.

    Structurei

    Secondary structure

    1
    281
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 253Combined sources
    Helixi29 – 4416Combined sources
    Turni45 – 517Combined sources
    Beta strandi56 – 649Combined sources
    Turni65 – 684Combined sources
    Beta strandi69 – 768Combined sources
    Turni77 – 804Combined sources
    Beta strandi81 – 866Combined sources
    Helixi92 – 987Combined sources
    Beta strandi103 – 1053Combined sources
    Beta strandi116 – 1183Combined sources
    Helixi119 – 14224Combined sources
    Beta strandi146 – 1538Combined sources
    Helixi155 – 16814Combined sources
    Beta strandi172 – 1809Combined sources
    Helixi187 – 19610Combined sources
    Turni197 – 2004Combined sources
    Turni202 – 2043Combined sources
    Beta strandi206 – 2127Combined sources
    Helixi217 – 2193Combined sources
    Helixi223 – 2253Combined sources
    Beta strandi231 – 2366Combined sources
    Helixi242 – 2443Combined sources
    Beta strandi245 – 2484Combined sources
    Beta strandi250 – 2523Combined sources
    Helixi255 – 2595Combined sources
    Helixi266 – 2694Combined sources
    Beta strandi274 – 2774Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1USWX-ray2.50A22-281[»]
    1UWCX-ray1.08A/B22-281[»]
    1UZAX-ray1.50A/B22-281[»]
    2BJHX-ray2.54A/B/C22-281[»]
    2HL6X-ray1.55A/B22-281[»]
    2IX9X-ray1.70A/B22-281[»]
    ProteinModelPortaliO42807.
    SMRiO42807. Positions 22-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO42807.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. FaeA family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG4569. Eukaryota.
    COG3675. LUCA.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002921. Fungal_lipase-like.
    [Graphical view]
    PfamiPF01764. Lipase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O42807-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKQFSAKYAL ILLATAGQAL AASTQGISED LYNRLVEMAT ISQAAYADLC
    60 70 80 90 100
    NIPSTIIKGE KIYNAQTDIN GWILRDDTSK EIITVFRGTG SDTNLQLDTN
    110 120 130 140 150
    YTLTPFDTLP QCNDCEVHGG YYIGWISVQD QVESLVKQQA SQYPDYALTV
    160 170 180 190 200
    TGHSLGASMA ALTAAQLSAT YDNVRLYTFG EPRSGNQAFA SYMNDAFQVS
    210 220 230 240 250
    SPETTQYFRV THSNDGIPNL PPADEGYAHG GVEYWSVDPY SAQNTFVCTG
    260 270 280
    DEVQCCEAQG GQGVNDAHTT YFGMTSGACT W
    Length:281
    Mass (Da):30,537
    Last modified:June 1, 1998 - v1
    Checksum:i8B4322B72710BBF3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131L → S in ACJ64498 (Ref. 3) Curated
    Sequence conflicti23 – 231S → F in ACZ95366 (Ref. 4) Curated
    Sequence conflicti44 – 441A → P in ACZ95366 (Ref. 4) Curated
    Sequence conflicti56 – 561I → T in ACJ64498 (Ref. 3) Curated
    Sequence conflicti107 – 1071D → E in ACJ64498 (Ref. 3) Curated
    Sequence conflicti113 – 1131N → S in ACJ64498 (Ref. 3) Curated
    Sequence conflicti128 – 1281V → I in ACJ64498 (Ref. 3) Curated
    Sequence conflicti142 – 1421Q → K in ACZ95366 (Ref. 4) Curated
    Sequence conflicti150 – 1501V → M in ACJ64498 (Ref. 3) Curated
    Sequence conflicti159 – 1591M → L AA sequence (PubMed:9406381).Curated
    Sequence conflicti174 – 1741V → I AA sequence (PubMed:9406381).Curated
    Sequence conflicti205 – 2051T → I in ACZ95366 (Ref. 4) Curated
    Sequence conflicti208 – 2081F → S in ACJ64498 (Ref. 3) Curated
    Sequence conflicti224 – 2241D → E in AAK60631 (PubMed:12702357).Curated
    Sequence conflicti224 – 2241D → E in ACJ64498 (Ref. 3) Curated
    Sequence conflicti224 – 2241D → E in ACZ95366 (Ref. 4) Curated
    Sequence conflicti225 – 2251E → Q in AAK60631 (PubMed:12702357).Curated
    Sequence conflicti225 – 2251E → Q in ACJ64498 (Ref. 3) Curated
    Sequence conflicti264 – 2641V → A in ACJ64498 (Ref. 3) Curated

    Mass spectrometryi

    Molecular mass is 29738±50 Da from positions 22 - 281. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y09330 Genomic DNA. Translation: CAA70510.1.
    AF361950 mRNA. Translation: AAK60631.1.
    FJ430154 mRNA. Translation: ACJ64498.1.
    GU188042 mRNA. Translation: ACZ95366.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y09330 Genomic DNA. Translation: CAA70510.1.
    AF361950 mRNA. Translation: AAK60631.1.
    FJ430154 mRNA. Translation: ACJ64498.1.
    GU188042 mRNA. Translation: ACZ95366.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1USWX-ray2.50A22-281[»]
    1UWCX-ray1.08A/B22-281[»]
    1UZAX-ray1.50A/B22-281[»]
    2BJHX-ray2.54A/B/C22-281[»]
    2HL6X-ray1.55A/B22-281[»]
    2IX9X-ray1.70A/B22-281[»]
    ProteinModelPortaliO42807.
    SMRiO42807. Positions 22-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00007416.

    Protein family/group databases

    ESTHERiaspni-FAEA. Lipase_3.
    mycoCLAPiFAE1A_ASPNG.

    Proteomic databases

    PaxDbiO42807.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiKOG4569. Eukaryota.
    COG3675. LUCA.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16832.
    BRENDAi3.1.1.73. 518.

    Miscellaneous databases

    EvolutionaryTraceiO42807.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002921. Fungal_lipase-like.
    [Graphical view]
    PfamiPF01764. Lipase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides."
      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.
      Appl. Environ. Microbiol. 63:4638-4644(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-107 AND 134-179, MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION.
      Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
    2. "High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris."
      Juge N., Williamson G., Puigserver A., Cummings N.J., Connerton I.F., Faulds C.B.
      FEMS Yeast Res. 1:127-132(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning and directed evolution of feruloyl esterase from Aspergillus niger."
      Zhang S., Pei X., Wu Z.
      Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: CIB423.1.
    4. "Molecular docking of feruloyl esterase A and ferulic acid substrate using computer modeling."
      Hu X.S., Li X.L.
      Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Purification and characterisation of a ferulic acid esterase (FAE-III) from Aspergillus niger: specificity for the phenolic moiety and binding to microcrystalline cellulose."
      Faulds C.B., Williamson G.
      Microbiology 140:779-787(1994)
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
      Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
    6. "Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger."
      Ralet M.C., Faulds C.B., Williamson G., Thibault J.F.
      Carbohydr. Res. 263:257-269(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Identification of active site residues in a ferulic acid esterase (FAE-III) from Aspergillus niger."
      Aliwan F.O., Williamson G.
      Biochem. Soc. Trans. 26:S164-S164(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    8. "Regulation of the feruloyl esterase (faeA) gene from Aspergillus niger."
      de Vries R.P., Visser J.
      Appl. Environ. Microbiol. 65:5500-5503(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "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."
      de Vries R.P., vanKuyk P.A., Kester H.C., Visser J.
      Biochem. J. 363:377-386(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
      Strain: ATCC 9089 / N402.
    10. "Structure of a feruloyl esterase from Aspergillus niger."
      McAuley K.E., Svendsen A., Patkar S.A., Wilson K.S.
      Acta Crystallogr. D 60:878-887(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 22-281 IN COMPLEX WITH FERULIC ACID.
    11. "The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family."
      Hermoso J.A., Sanz-Aparicio J., Molina R., Juge N., Gonzalez R., Faulds C.B.
      J. Mol. Biol. 338:495-506(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-281, DISULFIDE BONDS, FUNCTION, MUTAGENESIS OF SER-154.
    12. "Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger."
      Faulds C.B., Molina R., Gonzalez R., Husband F., Juge N., Sanz-Aparicio J., Hermoso J.A.
      FEBS J. 272:4362-4371(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 22-281 OF MUTANT SER-154 IN COMPLEX WITH SUBSTRATE, MUTAGENESIS OF TYR-101 AND TRP-281.
    13. "Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A."
      Benoit I., Asther M., Sulzenbacher G., Record E., Marmuse L., Parsiegla G., Gimbert I., Asther M., Bignon C.
      FEBS Lett. 580:5815-5821(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 22-281, GLYCOSYLATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiFAEA_ASPNG
    AccessioniPrimary (citable) accession number: O42807
    Secondary accession number(s): B8XRG2, D2K873, Q96W70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2001
    Last sequence update: June 1, 1998
    Last modified: April 13, 2016
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.