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Q4WYX7 (ABNA_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 52. 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:
Probable 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
ORF Names:AFUA_3G14620
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
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 – 321302Probable arabinan endo-1,5-alpha-L-arabinosidase A
PRO_0000394620

Sequences

Sequence LengthMass (Da)Tools
Q4WYX7 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 9D9BFFE699F10574

FASTA32134,036
        10         20         30         40         50         60 
MSASVFVVVA SCLAALAHGY ANPGSCLGAC NVHDPALIRR ESDGKYFRFS TGNKISYASS 

        70         80         90        100        110        120 
SSIEGPWTVL GSVLPSGSSI DLPGNDDLWA PDVSLVNGVY HVYYSVSTFG SQSSAIGLAT 

       130        140        150        160        170        180 
SSTMDLNSWT DHGSTGIQSS SSKPYNAIDG NLFKDGGTYY MNFGSFWHDI YQAPMNSAAT 

       190        200        210        220        230        240 
SVASSSYNIA YNPSGTHAVE GAFMYKYGNY YYLFFSAGIC CGYDTSRPAS GEEYKIKVCR 

       250        260        270        280        290        300 
STSATGNFVD ANGVACTNGG GTVVLESHGN VYGPGGQGVF TDPSLGPILY YHYVDTTIGY 

       310        320 
ADSQKLFGWN KIDFSSGWPV V 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000002 Genomic DNA. Translation: EAL92126.1.
RefSeqXP_754164.1. XM_749071.1.

3D structure databases

ProteinModelPortalQ4WYX7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00005003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00005003; CADAFUAP00005003; CADAFUAG00005003.
GeneID3512291.
KEGGafm:AFUA_3G14620.

Phylogenomic databases

eggNOGCOG3507.
HOGENOMHOG000292006.
KOK06113.
OMAGACNVHD.
OrthoDBEOG761C4Q.

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_ASPFU
AccessionPrimary (citable) accession number: Q4WYX7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: January 22, 2014
This is version 52 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