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Protein

Feruloyl esterase C

Gene

faeC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 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. Active against paranitrophenyl-acetate, methyl ferulate and wheat arabinoxylan.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 6.1.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius.1 Publication

GO - Molecular functioni

  • feruloyl esterase activity Source: UniProtKB

GO - Biological processi

  • xylan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Protein family/group databases

ESTHERiemeni-faec. Esterase_phb.
mycoCLAPiFAE1C_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Feruloyl esterase C (EC:3.1.1.73)
Alternative name(s):
Ferulic acid esterase C
Short name:
FAEC
Gene namesi
Name:faeC
ORF Names:AN5267
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome V
  • UP000005890 Componenti: Partially assembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AN5267.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 270249Feruloyl esterase CPRO_0000394942Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ5B2G3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the faeC family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171266.
InParanoidiQ5B2G3.
OMAiSSGCGKQ.
OrthoDBiEOG7CCC2C.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5B2G3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRAVLLPTL LAFGAFTPVH GANSPGCGKQ PTLTNGVNQI NGREYVLKIP
60 70 80 90 100
DGYDPSKPHH LIFGLHWRGG NMYNVVNGDS IQPWYGLEAR AQGSAIFVAP
110 120 130 140 150
NGLNAGWANT NGEDVAFIDA IMEQVEDDLC VDQASRFATG FSWGGGMSYA
160 170 180 190 200
LACARAAEFR AVSVLSGGLI SGCDGGNDPI AYLGIHGIND PVLPLDGGVT
210 220 230 240 250
LANTFVSNNG CQPTDIGQPA SGSGGSVRTD FSGCSHPVSF IAYDGGHDGA
260 270
PLGVGSSLAP DATWEFFMAA
Length:270
Mass (Da):27,977
Last modified:April 26, 2005 - v1
Checksum:i89D4972DDDFC8C97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000093 Genomic DNA. Translation: EAA62427.1.
BN001305 Genomic DNA. Translation: CBF82209.1.
RefSeqiXP_662871.1. XM_657779.1.

Genome annotation databases

EnsemblFungiiCADANIAT00003838; CADANIAP00003838; CADANIAG00003838.
EAA62427; EAA62427; AN5267.2.
GeneIDi2871558.
KEGGiani:AN5267.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000093 Genomic DNA. Translation: EAA62427.1.
BN001305 Genomic DNA. Translation: CBF82209.1.
RefSeqiXP_662871.1. XM_657779.1.

3D structure databases

ProteinModelPortaliQ5B2G3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiemeni-faec. Esterase_phb.
mycoCLAPiFAE1C_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00003838; CADANIAP00003838; CADANIAG00003838.
EAA62427; EAA62427; AN5267.2.
GeneIDi2871558.
KEGGiani:AN5267.2.

Organism-specific databases

EuPathDBiFungiDB:AN5267.

Phylogenomic databases

HOGENOMiHOG000171266.
InParanoidiQ5B2G3.
OMAiSSGCGKQ.
OrthoDBiEOG7CCC2C.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiFAEC_EMENI
AccessioniPrimary (citable) accession number: Q5B2G3
Secondary accession number(s): C8VH20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: April 13, 2016
This is version 49 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

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.