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Q5BA89 (ABFA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified September 5, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 alpha-N-arabinofuranosidase A
Short name=ABF A
Short name=Arabinosidase A
EC=3.2.1.55
Gene names
Name:abfA
ORF Names:AN2541
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 length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Alpha-N-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 By similarity.

Catalytic activity

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

Pathway

Glycan metabolism; L-arabinan degradation.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 51 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 565546Probable alpha-N-arabinofuranosidase A
PRO_0000394601

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation4861N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5BA89 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 18B9A9B5206AFBC3

FASTA56562,771
        10         20         30         40         50         60 
MPLSAAIKSS LSVSVRADAK GLVGFANTGY NGITVLKQTY WTSFYMKGEY SGTVLLRLTG 

        70         80         90        100        110        120 
TDSGTVYGSR NLSVKSTGGK WTQYETTFEA NESYVAENEW QLLFDAATAK GHPLHFGLVQ 

       130        140        150        160        170        180 
LFPPTYKNRT NGLRNDIARP IADLKPKFLR FPGGNNIQAD RPGDWHYPNT DALGLDEYLW 

       190        200        210        220        230        240 
WCEDMDMVPV LSVWDGKSYG GIVSGEELQP YLDDIKDELE VTLPLTLLSH PLRAYLTPNT 

       250        260        270        280        290        300 
NEQYLLGPPS TPFGALRARN GHPDPWPIQY IEIGNEDDYS GGCDTYPDRL VQIYDTIHAS 

       310        320        330        340        350        360 
YPNLTLIANN MDENCLPEIP LPGLWHDYHY YRSADDLVAM FNYWDNHDRG DRVLVGEYGC 

       370        380        390        400        410        420 
RNDSNPDGVF WSFMQGSCAE AVHMIGLERN SDVVMMAAYA PLLQHFGYTQ WSVCTPSASL 

       430        440        450        460        470        480 
AYLGIHPADR GEEQPTLFGF ESRPNSLTLS TSYYVNRMFS TNQGSTVHKV HSTAGFGPLY 

       490        500        510        520        530        540 
WVATSNETAY QVKLANYGAA NQTVNIRVPG VGRGVLEMIS GPKDASNLPG DIKIVPVSRN 

       550        560 
IRAGKEGYTV HMPPWGVAVL VVVFK

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000043 Genomic DNA. Translation: EAA64646.1.
BN001307 Genomic DNA. Translation: CBF87061.1.
RefSeqXP_660145.1. XM_655053.1.

3D structure databases

ProteinModelPortalQ5BA89.
ModBaseSearch...

Protein family/group databases

CAZyGH51. Glycoside Hydrolase Family 51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00009271; CADANIAP00009271; CADANIAG00009271.
GeneID2875725.
KEGGani:AN2541.2.

Phylogenomic databases

eggNOGCOG3534.
HOGENOMHOG000115340.
KOK01209.
OMAYPNTDAL.
OrthoDBEOG4Z0FDW.

Enzyme and pathway databases

UniPathwayUPA00667.

Family and domain databases

InterProIPR010720. Alpha-L-AF_C.
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. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameABFA_EMENI
AccessionPrimary (citable) accession number: Q5BA89
Secondary accession number(s): C8VPS5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: September 5, 2012
This is version 49 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents