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Q9HFS9 (ABNA_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arabinan endo-1,5-alpha-L-arabinosidase A

EC=3.2.1.99
Alternative name(s):
Endo-1,5-alpha-L-arabinanase A
Short name=ABN A
Gene names
Name:abnA
Synonyms:ara1
OrganismAspergillus aculeatus
Taxonomic identifier5053 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan By similarity. Ref.1

Catalytic activity

Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.

Pathway

Glycan metabolism; L-arabinan degradation.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 43 family.

Biophysicochemical properties

Kinetic parameters:

KM=66 mM for AZCL-debranched arabinan Ref.1

pH dependence:

Optimum pH is 5.5. Stable between pH 5.5 and 6.5.

Temperature dependence:

Optimum temperature is 50 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processarabinan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

xylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionarabinan endo-1,5-alpha-L-arabinosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 321302Arabinan endo-1,5-alpha-L-arabinosidase A
PRO_5000058634

Amino acid modifications

Glycosylation1921N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9HFS9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: FAE9D565631613F1

FASTA32134,097
        10         20         30         40         50         60 
MYSLLTALSV PLLAGLAHGY ANPGSCSGSC NVHDPALIVR ESDGKYFRFS TGNEISYASA 

        70         80         90        100        110        120 
SSINGPWTAI GSVVPAGSKI DLSGNTDLWA PDLSYVDGTY YCLYSVSTFG SQDSAIGVAS 

       130        140        150        160        170        180 
STTMELNTWT DHGSVGVASS SSKNYNAIDG NLLVDGSSYY LQFGSFWGDI YQVKMASPLK 

       190        200        210        220        230        240 
TAGSASYNIA YNATGTHSEE GSYLFKYGSY YYLFFSSGTC CGYDTSRPAQ GEEYKIMVCR 

       250        260        270        280        290        300 
STSATGGFVD KNGNACTESG GTIVLASHGT VYGPGGQGVY DDPTYGPVLY YHYVDTTIGY 

       310        320 
ADDQKLFGWN TIDFSSGWPV V 

« Hide

References

[1]"Functional cloning of an endo-arabinanase from Aspergillus aculeatus and its heterologous expression in A. oryzae and tobacco."
Skjoet M., Kauppinen S., Kofod L.V., Fuglsang C.C., Pauly M., Dalboege H., Andersen L.N.
Mol. Genet. Genomics 265:913-921(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-38, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: CBS 101.43.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF300878 mRNA. Translation: AAG27441.1.

3D structure databases

ProteinModelPortalQ9HFS9.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH43. Glycoside Hydrolase Family 43.
mycoCLAPABN43A_ASPAC.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00667.

Family and domain databases

Gene3D2.115.10.20. 1 hit.
InterProIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERPTHR22925. PTHR22925. 1 hit.
PfamPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMSSF75005. SSF75005. 1 hit.
ProtoNetSearch...

Entry information

Entry nameABNA_ASPAC
AccessionPrimary (citable) accession number: Q9HFS9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 1, 2001
Last modified: November 13, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries