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Protein

Feruloyl esterase B

Gene

fae-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in degradation of plant cell walls. Hydrolyzes of the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin (By similarity).By similarity

Catalytic activityi

Feruloyl-polysaccharide + H2O = ferulate + polysaccharide.

GO - Molecular functioni

  • feruloyl esterase activity Source: UniProtKB

GO - Biological processi

  • cell wall macromolecule catabolic process Source: UniProtKB
  • xylan catabolic process Source: UniProtKB-KW
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. 3627.

Protein family/group databases

ESTHERineucr-faeb. Esterase_phb.

Names & Taxonomyi

Protein namesi
Recommended name:
Feruloyl esterase B (EC:3.1.1.73)
Alternative name(s):
Ferulic acid esterase
Short name:
FAE
Gene namesi
Name:fae-1
ORF Names:B22K18.040, NCU09491
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
Proteomesi
  • UP000001805 Componenti: Chromosome 6, Linkage Group II

Organism-specific databases

EuPathDBiFungiDB:NCU09491.

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 – 18Sequence analysisAdd BLAST18
ChainiPRO_000002122819 – 292Feruloyl esterase BAdd BLAST274

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi88N-linked (GlcNAc...)Sequence analysis1
Glycosylationi117N-linked (GlcNAc...)Sequence analysis1
Glycosylationi179N-linked (GlcNAc...)Sequence analysis1
Glycosylationi245N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ9HGR3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the feruloyl esterase type B family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171266.
InParanoidiQ9HGR3.
OMAiHACFAGA.
OrthoDBiEOG092C3RN6.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR010126. Esterase_phb.
[Graphical view]
PfamiPF10503. Esterase_phd. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
TIGRFAMsiTIGR01840. esterase_phb. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9HGR3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPRTLLGLA LTAATGLCAS LQQVTNWGSN PTNIRMYTYV PDKLATKPAI
60 70 80 90 100
IVALHGCGGT APSWYSGTRL PSYADQYGFI LIYPGTPNMS NCWGVNDPAS
110 120 130 140 150
LTHGAGGDSL GIVAMVNYTI AKYNADASRV YVMGTSSGGM MTNVMAATYP
160 170 180 190 200
EVFEAGAAYS GVAHACFAGA ASATPFSPNQ TCARGLQHTP EEWGNFVRNS
210 220 230 240 250
YPGYTGRRPR MQIYHGLADN LVYPRCAMEA LKQWSNVLGV EFSRNVSGVP
260 270 280 290
SQAYTQIVYG DGSKLVGYMG AGVGHVAPTN EQVMLKFFGL IN
Length:292
Mass (Da):31,084
Last modified:June 7, 2005 - v2
Checksum:i9EE5A070F4E42821
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37Y → H in CAC05587 (PubMed:12435269).Curated1
Sequence conflicti214Y → C in CAC05587 (PubMed:12435269).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293029 mRNA. Translation: CAC05587.1.
BX842597 Genomic DNA. Translation: CAE75726.1.
CM002237 Genomic DNA. Translation: EAA33979.1.
RefSeqiXP_963215.1. XM_958122.2.

Genome annotation databases

EnsemblFungiiEAA33979; EAA33979; NCU09491.
GeneIDi3879354.
KEGGincr:NCU09491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293029 mRNA. Translation: CAC05587.1.
BX842597 Genomic DNA. Translation: CAE75726.1.
CM002237 Genomic DNA. Translation: EAA33979.1.
RefSeqiXP_963215.1. XM_958122.2.

3D structure databases

ProteinModelPortaliQ9HGR3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERineucr-faeb. Esterase_phb.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAA33979; EAA33979; NCU09491.
GeneIDi3879354.
KEGGincr:NCU09491.

Organism-specific databases

EuPathDBiFungiDB:NCU09491.

Phylogenomic databases

HOGENOMiHOG000171266.
InParanoidiQ9HGR3.
OMAiHACFAGA.
OrthoDBiEOG092C3RN6.

Enzyme and pathway databases

BRENDAi3.1.1.73. 3627.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR010126. Esterase_phb.
[Graphical view]
PfamiPF10503. Esterase_phd. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
TIGRFAMsiTIGR01840. esterase_phb. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFAEB_NEUCR
AccessioniPrimary (citable) accession number: Q9HGR3
Secondary accession number(s): Q7RVZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.