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Protein

Acetylxylan esterase A

Gene

axeA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.1 Publication

Catalytic activityi

Deacetylation of xylans and xylo-oligosaccharides.

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

Optimum temperature is 49 degrees Celsius.1 Publication

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei147 – 1471Charge relay systemBy similarity

GO - Molecular functioni

  • acetylxylan esterase activity Source: UniProtKB

GO - Biological processi

  • cellulose catabolic process Source: UniProtKB-KW
  • xylan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

ESTHERiemeni-axe1. Esterase_phb.
mycoCLAPiAXE1A_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylxylan esterase A (EC:3.1.1.72)
Gene namesi
Name:axeA
Synonyms:aceA
ORF Names:AN6093
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome I
  • UP000005890 Componenti: Partially assembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AN6093.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 304285Acetylxylan esterase APRO_0000393482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5B037.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the axeA family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171266.
InParanoidiQ5B037.
KOiK05972.
OrthoDBiEOG7KDFN9.

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.

Q5B037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLQYLLSI LLYAYSCTAL MLDRRDPTPG QLSQVTDFGD NPTNVGFYIY
60 70 80 90 100
VPQNLASNPA IIVAIHYCTG TAQAYYSGTP YAQYAETYGF IVIYPESPYS
110 120 130 140 150
GTCWDVSSQS TLTHNGGGNS NSIANMVDWT INQYNADASR VYVTGTSSGA
160 170 180 190 200
MMTNVMAATY PNLFAAGIAY AGVPAGCFYS EANVEDQWNS TCAQGQSIST
210 220 230 240 250
PEHWAQIAQA MYSGYEGSRP KMQIYHGSAD ATLYPQNYYE TCKQWAGVFG
260 270 280 290 300
YNYDSPQEVQ NDTPVAGWAK TIWGENLQGI LADGVGHNIQ IQGEEDLKWF

GFTS
Length:304
Mass (Da):33,302
Last modified:April 20, 2010 - v2
Checksum:i6573784DF0261190
GO

Sequence cautioni

The sequence CBF70198.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA58068.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490499 mRNA. Translation: ABF50875.1.
AACD01000104 Genomic DNA. Translation: EAA58068.1. Sequence problems.
BN001301 Genomic DNA. Translation: CBF70198.1. Sequence problems.
RefSeqiXP_663697.1. XM_658605.1.

Genome annotation databases

EnsemblFungiiCADANIAT00006921; CADANIAP00006921; CADANIAG00006921.
EAA58068; EAA58068; AN6093.2.
GeneIDi2870922.
KEGGiani:AN6093.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490499 mRNA. Translation: ABF50875.1.
AACD01000104 Genomic DNA. Translation: EAA58068.1. Sequence problems.
BN001301 Genomic DNA. Translation: CBF70198.1. Sequence problems.
RefSeqiXP_663697.1. XM_658605.1.

3D structure databases

ProteinModelPortaliQ5B037.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiemeni-axe1. Esterase_phb.
mycoCLAPiAXE1A_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00006921; CADANIAP00006921; CADANIAG00006921.
EAA58068; EAA58068; AN6093.2.
GeneIDi2870922.
KEGGiani:AN6093.2.

Organism-specific databases

EuPathDBiFungiDB:AN6093.

Phylogenomic databases

HOGENOMiHOG000171266.
InParanoidiQ5B037.
KOiK05972.
OrthoDBiEOG7KDFN9.

Enzyme and pathway databases

UniPathwayiUPA00114.

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...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "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.

Entry informationi

Entry nameiAXE1_EMENI
AccessioniPrimary (citable) accession number: Q5B037
Secondary accession number(s): C8V2L3, Q1HFS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: April 13, 2016
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

The C-terminal carbohydrate-binding module (CBM) extension found in some acetylxylan esterases from other species is absent.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.