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Q5AUX2 (AXHA2_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alpha-L-arabinofuranosidase axhA-2
EC=3.2.1.55
Alternative name(s):
Arabinoxylan arabinofuranohydrolase axhA-2
Gene names
Name:axhA-2
ORF Names:AN7908
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha-L-arabinofuranosidase 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. Releases L-arabinose from arabinoxylan By similarity. Ref.3

Catalytic activity

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 62 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.4. Ref.3

Temperature dependence:

Optimum temperature is 47 degrees Celsius.

Ontologies

Keywords
   Biological processXylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-arabinose metabolic process

Inferred from electronic annotation. Source: InterPro

arabinose metabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

pectin catabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

xylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-N-arabinofuranosidase activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 325303Alpha-L-arabinofuranosidase axhA-2
PRO_0000393537

Amino acid modifications

Glycosylation831N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5AUX2 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: CD0DC28566CB8064

FASTA32535,560
        10         20         30         40         50         60 
MRNLSTWPTF AALLWSAPRV LAQCGLPSTY SWTSTGPLAE PKDGWASLKD FTAVPYNGQY 

        70         80         90        100        110        120 
LVYATYHDTG TSWGSMNFGL FSNWSDMATA SQNAMTQSTV APTLFYFEPK DVWILAYQWG 

       130        140        150        160        170        180 
PTAFSYLTSS DPTDANGWSS PQPLFSGSIS DSDTGVIDQT VIGDSTTMYL FFAGDNGRIY 

       190        200        210        220        230        240 
RASMPIDQFP GDFGTESEII LSDERNNLFE AVQVYTVSGQ SKDTYLMIVE AIGAQGRYFR 

       250        260        270        280        290        300 
SFTADSLGGS WTPQAATESA PFAGKANSGA TWTDDISHGD LVRSTPDQTM SIDPCNLQLL 

       310        320 
YQGRDPSLNP GYDLLPYRPG LLTLK

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000135 Genomic DNA. Translation: EAA59562.1.
BN001302 Genomic DNA. Translation: CBF73503.1.
RefSeqXP_681177.1. XM_676085.1.

3D structure databases

ProteinModelPortalQ5AUX2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00003927; CADANIAP00003927; CADANIAG00003927.
GeneID2869048.
KEGGani:AN7908.2.

Phylogenomic databases

eggNOGNOG81570.
HOGENOMHOG000164911.
OMADSTTMYL.
OrthoDBEOG4XH383.

Family and domain databases

InterProIPR005193. GH62_arabinosidase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamPF03664. Glyco_hydro_62. 1 hit.
[Graphical view]
SUPFAMSSF75005. Glyco_hydro_43_beta-prop. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAXHA2_EMENI
AccessionPrimary (citable) accession number: Q5AUX2
Secondary accession number(s): C8V4U9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 26, 2005
Last modified: March 6, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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