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Q5BDV3 (ABFC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:
Alpha-L-arabinofuranosidase C

Short name=ABF C
Short name=Arabinosidase C
EC=3.2.1.55
Gene names
Name:abfC
ORF Names:AN1277
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides. Ref.1

Catalytic activity

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

Pathway

Glycan metabolism; L-arabinan degradation.

Subcellular location

Secreted Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 51 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide 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

arabinan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

arabinose metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

pectin catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-L-arabinofuranosidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ? Potential
Chain? – 504Alpha-L-arabinofuranosidase CPRO_0000394616

Amino acid modifications

Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1521N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5BDV3 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 0E79FD944F10970D

FASTA50456,554
        10         20         30         40         50         60 
MTTFTKLSEQ EAPGISIHPD RRISKINPNI YAGFAEHMGR CIYGGIYDPG NPLSDENGFR 

        70         80         90        100        110        120 
KDVLEALKEL KVPVIRYPGG NFTATYHWID GVGPRDQRPA RPELAWLGTE TNQFGTDEFL 

       130        140        150        160        170        180 
KWCEVLGTEP YLCLNMGTGT LDEALAWVDY CNGTRDTYYA NLRRKNGREE PYNVKYWALG 

       190        200        210        220        230        240 
NEVWGPWQVE QSTKEEYAHK AYQWAKALKL LDPSIELILC GKEGPTSWDY YTLKQTMLPV 

       250        260        270        280        290        300 
HSPLSTSAVP LIDMHSIHLY TAHSSHLPNV TAPLAAERAI EITSSLIDLA RVENGVPPEQ 

       310        320        330        340        350        360 
RRPTICFDEW NVWDPIRAEG SKGAEESYNL SDALAVGVWL NVFVRKSKDV GMACIAQSVN 

       370        380        390        400        410        420 
VISPLMTTKD GIVKQTTWWP LYLFSNYMRG WTISAHISVS AYEGETHPKW VRGVKDTPWL 

       430        440        450        460        470        480 
DVSATLGEDG YVNVVVINIH EEKGIEAKLD GPSGEVTVFT VTGDNPAVTN MKGKEEVGLV 

       490        500 
ETKWDAQGPY VFPKHSLTLL RWKA 

« Hide

References

« Hide 'large scale' references
[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.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"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.
[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. 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ490471 mRNA. Translation: ABF50847.1.
AACD01000017 Genomic DNA. Translation: EAA65870.1.
BN001308 Genomic DNA. Translation: CBF87808.1.
RefSeqXP_658881.1. XM_653789.1.

3D structure databases

ProteinModelPortalQ5BDV3.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH51. Glycoside Hydrolase Family 51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00001344; CADANIAP00001344; CADANIAG00001344.
GeneID2877053.
KEGGani:AN1277.2.

Phylogenomic databases

eggNOGCOG3534.
HOGENOMHOG000236895.
KOK01209.
OMADEFIAWC.
OrthoDBEOG71P2KW.

Enzyme and pathway databases

UniPathwayUPA00667.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR010720. Alpha-L-AF_C.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameABFC_EMENI
AccessionPrimary (citable) accession number: Q5BDV3
Secondary accession number(s): C8VSG2, Q1HFV3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: May 14, 2014
This is version 58 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