Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
    Binding sitei98Substrate1 Publication1
    Binding sitei101Substrate1 Publication1
    Active sitei154Nucleophile1 Publication1
    Active sitei215Charge relay system1 Publication1
    Active sitei268Charge relay system1 Publication1
    Binding sitei268Substrate1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi101Y → V or S: Decreases feruloyl esterase activity. 1 Publication1
    Mutagenesisi154S → A: Impairs catalytic activity. 1 Publication1
    Mutagenesisi281W → V or S: Decreases feruloyl esterase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 211 PublicationAdd BLAST21
    ChainiPRO_000002122622 – 281Feruloyl esterase AAdd BLAST260

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi50 ↔ 2791 Publication
    Glycosylationi100N-linked (GlcNAc...)1 Publication1
    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

    1281
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi23 – 25Combined sources3
    Helixi29 – 44Combined sources16
    Turni45 – 51Combined sources7
    Beta strandi56 – 64Combined sources9
    Turni65 – 68Combined sources4
    Beta strandi69 – 76Combined sources8
    Turni77 – 80Combined sources4
    Beta strandi81 – 86Combined sources6
    Helixi92 – 98Combined sources7
    Beta strandi103 – 105Combined sources3
    Beta strandi116 – 118Combined sources3
    Helixi119 – 142Combined sources24
    Beta strandi146 – 153Combined sources8
    Helixi155 – 168Combined sources14
    Beta strandi172 – 180Combined sources9
    Helixi187 – 196Combined sources10
    Turni197 – 200Combined sources4
    Turni202 – 204Combined sources3
    Beta strandi206 – 212Combined sources7
    Helixi217 – 219Combined sources3
    Helixi223 – 225Combined sources3
    Beta strandi231 – 236Combined sources6
    Helixi242 – 244Combined sources3
    Beta strandi245 – 248Combined sources4
    Beta strandi250 – 252Combined sources3
    Helixi255 – 259Combined sources5
    Helixi266 – 269Combined sources4
    Beta strandi274 – 277Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti13L → S in ACJ64498 (Ref. 3) Curated1
    Sequence conflicti23S → F in ACZ95366 (Ref. 4) Curated1
    Sequence conflicti44A → P in ACZ95366 (Ref. 4) Curated1
    Sequence conflicti56I → T in ACJ64498 (Ref. 3) Curated1
    Sequence conflicti107D → E in ACJ64498 (Ref. 3) Curated1
    Sequence conflicti113N → S in ACJ64498 (Ref. 3) Curated1
    Sequence conflicti128V → I in ACJ64498 (Ref. 3) Curated1
    Sequence conflicti142Q → K in ACZ95366 (Ref. 4) Curated1
    Sequence conflicti150V → M in ACJ64498 (Ref. 3) Curated1
    Sequence conflicti159M → L AA sequence (PubMed:9406381).Curated1
    Sequence conflicti174V → I AA sequence (PubMed:9406381).Curated1
    Sequence conflicti205T → I in ACZ95366 (Ref. 4) Curated1
    Sequence conflicti208F → S in ACJ64498 (Ref. 3) Curated1
    Sequence conflicti224D → E in AAK60631 (PubMed:12702357).Curated1
    Sequence conflicti224D → E in ACJ64498 (Ref. 3) Curated1
    Sequence conflicti224D → E in ACZ95366 (Ref. 4) Curated1
    Sequence conflicti225E → Q in AAK60631 (PubMed:12702357).Curated1
    Sequence conflicti225E → Q in ACJ64498 (Ref. 3) Curated1
    Sequence conflicti264V → A in ACJ64498 (Ref. 3) Curated1

    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
    PDB 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.
    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...

    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: November 2, 2016
    This is version 95 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.