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Protein

Acetylxylan esterase A

Gene

axeA

Organism
Aspergillus ficuum
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 7.0.1 Publication

Temperature dependencei

Thermal stability decreased at temperatures above 40 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

GO - Biological processi

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

ESTHERiaspnc-axe1. Esterase_phb.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylxylan esterase A (EC:3.1.1.72)
Gene namesi
Name:axeA
Synonyms:aceA
OrganismiAspergillus ficuum
Taxonomic identifieri5058 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 303280Acetylxylan esterase APRO_0000393476Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ96W96.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the axeA family.Curated

Keywords - Domaini

Signal

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.

Q96W96-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSTHLLFLA TTLLTSLFHP IAAHVAKRSG SLQQITDFGD NPTGVGMYIY
60 70 80 90 100
VPNNLASNPG IVVAIHYCTG TGPGYYSNSP YATLSEQYGF IVIYPSSPYS
110 120 130 140 150
GGCWDVSSQA TLTHNGGGNS NSIANMVTWT ISEYGADSKK VYVTGSSSGA
160 170 180 190 200
MMTNVMAATY PELFAAGTVY SGVSAGCFYS DTNQVDGWNS TCAQGDVITT
210 220 230 240 250
PEHWASIAEA MYPGYSGSRP KMQIYHGSVD TTLYPQNYYE TCKQWAGVFG
260 270 280 290 300
YDYSAPESTE ANTPQTNYET TIWGDNLQGI FATGVGHTVP IHGDKDMEWF

GFA
Length:303
Mass (Da):32,591
Last modified:December 1, 2001 - v1
Checksum:i281C57BD9D3996A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF331757 Genomic DNA. Translation: AAK60128.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF331757 Genomic DNA. Translation: AAK60128.1.

3D structure databases

ProteinModelPortaliQ96W96.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiaspnc-axe1. Esterase_phb.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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

  1. "Cloning the gene encoding acetyl xylan esterase from Aspergillus ficuum and its expression in Pichia pastoris."
    Chung H.-J., Park S.-M., Kim H.-R., Yang M.-S., Kim D.-H.
    Enzyme Microb. Technol. 31:384-391(2002)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiAXE1_ASPFI
AccessioniPrimary (citable) accession number: Q96W96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: December 1, 2001
Last modified: December 9, 2015
This is version 51 of the entry and version 1 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

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.