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Protein

Feruloyl esterase A

Gene

faeA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Active against methyl ferulate, methyl sinapate, methyl caffeate, and alpha-naphthyl esters with chains containing 2 to 8 carbons (C2-C8). Inactive against alpha-naphthyl esters with longer chains (C10 or more).1 Publication

Catalytic activityi

Feruloyl-polysaccharide + H2O = ferulate + polysaccharide.1 Publication

Kineticsi

  1. KM=0.33 mM for alpha-naphthylbutyrate1 Publication
  2. KM=0.079 mM for alpha-naphthylcaprylate1 Publication

    pH dependencei

    Optimum pH is 5.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei98 – 981SubstrateBy similarity
    Binding sitei101 – 1011SubstrateBy similarity
    Active sitei154 – 1541NucleophileBy similarity
    Active sitei215 – 2151Charge relay systemBy similarity
    Active sitei268 – 2681Charge relay systemBy similarity
    Binding sitei268 – 2681SubstrateBy similarity

    GO - Molecular functioni

    • feruloyl esterase activity Source: UniProtKB

    GO - Biological processi

    • 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

    BRENDAi3.1.1.73. 494.
    SABIO-RKQ9P979.

    Protein family/group databases

    ESTHERiaspaw-FERA. Lipase_3.
    mycoCLAPiFAE1A_ASPAW.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Feruloyl esterase A (EC:3.1.1.73)
    Alternative name(s):
    Ferulic acid esterase A
    Short name:
    FAEA
    Feruloylesterase
    Gene namesi
    Name:faeA1 Publication
    OrganismiAspergillus awamori (Black koji mold)
    Taxonomic identifieri105351 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    • Secreted By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi92 – 921D → I: Active against longer alpha-naphthyl esters than wild-type (C10, C12 and C16). Km value for the C8 alpha-naphthyl ester is decreased by 1.6-fold compared to wild-type. Decreased activity on arabinoxylan. 1 Publication
    Mutagenesisi93 – 931T → R: Km value for the C4 alpha-naphthyl ester is increased by 1.9-fold compared to wild-type. Km value for the C8 alpha-naphthyl ester is decreased by 4.6-fold compared to wild-type. Slightly decreased activity on arabinoxylan. 1 Publication
    Mutagenesisi98 – 981D → I: Increased optimum pH. Km value for the C4 alpha-naphthyl ester is decreased. Has higher activity on short chain alpha-naphthyl esters than wild-type, but no activity on substrates containing 6 or more carbon atoms. No activity on arabinoxylan, methyl ferulate, methyl sinapate or methyl caffeate. 1 Publication
    Mutagenesisi98 – 981D → N: Increased optimum pH. Km value for the C4 alpha-naphthyl ester is decreased. Has higher activity on short chain alpha-naphthyl esters than wild-type, but no activity on substrates containing 6 or more carbon atoms. Decreased activity on arabinoxylan. 1 Publication
    Mutagenesisi101 – 1011Y → F: Increased optimum pH. Active against longer alpha-naphthyl esters than wild-type (C10, C12 and C16). Km value for the C4 alpha-naphthyl ester is increased by 1.9-fold compared to wild-type. Km value for the C8 alpha-naphthyl ester is decreased by 1.9-fold compared to wild-type. Decreased activity on arabinoxylan, methyl ferulate, methyl sinapate or methyl caffeate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence analysisAdd
    BLAST
    Chaini22 – 281260Feruloyl esterase ASequence analysisPRO_0000021225Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi50 ↔ 279By similarity
    Glycosylationi100 – 1001N-linked (GlcNAc...)Curated
    Disulfide bondi112 ↔ 115By similarity
    Disulfide bondi248 ↔ 255By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. FaeA family.Curated

    Keywords - Domaini

    Signal

    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.

    Q9P979-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKQFSAKHAL AVVVTAGHAL AASTQGISED LYTRLVEMAT ISQAAYADLC
    60 70 80 90 100
    NIPSTIIKGE KIYNSQTDIN GWILRDDSSK EIITVFRGTG SDTNLQLDTN
    110 120 130 140 150
    YTLTPFDTLP QCNGCEVHGG YYIGWVSVQD QVESLVKQQV SQYPDYALTV
    160 170 180 190 200
    TGHSLGASLA ALTAAQLSAT YDNIRLYTFG EPRSGNQAFA SYMNDAFQAS
    210 220 230 240 250
    SPDTTQYFRV THANDGIPNL PPVEQGYAHG GVEYWSVDPY SAQNTFVCTG
    260 270 280
    DEVQCCEAQG GQGVNNAHTT YFGMTSGACT W
    Length:281
    Mass (Da):30,401
    Last modified:September 22, 2009 - v3
    Checksum:iC344247FD0A341FF
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB032760 Genomic DNA. Translation: BAA92937.3.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB032760 Genomic DNA. Translation: BAA92937.3.

    3D structure databases

    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    ESTHERiaspaw-FERA. Lipase_3.
    mycoCLAPiFAE1A_ASPAW.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.1.1.73. 494.
    SABIO-RKQ9P979.

    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...

    Entry informationi

    Entry nameiFAEA_ASPAW
    AccessioniPrimary (citable) accession number: Q9P979
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: September 22, 2009
    Last modified: April 13, 2016
    This is version 65 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. 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.