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Protein

Feruloyl esterase A

Gene

faeA

Organism
Aspergillus tubingensis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin.1 Publication

Catalytic activityi

Feruloyl-polysaccharide + H2O = ferulate + polysaccharide.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei98SubstrateBy similarity1
Binding sitei101SubstrateBy similarity1
Active sitei154NucleophileBy similarity1
Active sitei214Charge relay systemBy similarity1
Active sitei267Charge relay systemBy similarity1
Binding sitei267SubstrateBy similarity1

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. 538.

Protein family/group databases

ESTHERiasptu-FAEA. Lipase_3.

Names & Taxonomyi

Protein namesi
Recommended name:
Feruloyl esterase A (EC:3.1.1.73)
Alternative name(s):
Ferulic acid esterase A
Gene namesi
Name:faeA
OrganismiAspergillus tubingensis
Taxonomic identifieri5068 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000002122722 – 280Feruloyl esterase AAdd BLAST259

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 278By similarity
Glycosylationi100N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi112 ↔ 115By similarity
Disulfide bondi247 ↔ 254By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliO42815.
ModBaseiSearch...
MobiDBiSearch...

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.

O42815-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQFSAKYAI AVVVTAGHAL AASTQGISED LYSRLVEMAT ISQAAYADLC
60 70 80 90 100
NIPSTIIKGE KIYNSQTDIN GWILRDDSSK EIITVFRGTG SDTNLQLDTN
110 120 130 140 150
YTLTPFDTLP QCNSCEVHGG YYIGWISVQD QVESLVQQQV SQFPDYALTV
160 170 180 190 200
TGHSLGASLA ALTAAQLSAT YDNIRLYTFG EPRSNQAFAS YMNDAFQASS
210 220 230 240 250
PDTTQYFRVT HANDGIPNLP PADEGYAHGV VEYWSVDPYS AQNTFVCTGD
260 270 280
EVQCCEAQGG QGVNNAHTTY FGMTSGHCTW
Length:280
Mass (Da):30,451
Last modified:June 1, 1998 - v1
Checksum:i3601EF04C6E72713
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09331 Genomic DNA. Translation: CAA70511.1.

Genome annotation databases

KEGGiag:CAA70511.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09331 Genomic DNA. Translation: CAA70511.1.

3D structure databases

ProteinModelPortaliO42815.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiasptu-FAEA. Lipase_3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA70511.

Enzyme and pathway databases

BRENDAi3.1.1.73. 538.

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_ASPTU
AccessioniPrimary (citable) accession number: O42815
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: June 1, 1998
Last modified: October 5, 2016
This is version 64 of the entry and version 1 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.