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Q5AU81 (AFCA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-fucosidase A

EC=3.2.1.51
Alternative name(s):
Alpha-L-fucoside fucohydrolase A
Gene names
Name:afcA
ORF Names:AN8149
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 length809 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Alpha-fucosidase involved in degradation of fucosylated xyloglucans. Hydrolyzes alpha-1,2-linked fucose. Active on cotton xyloglucan oligomers but not active on paranitrophenyl-fucoside. Ref.1

Catalytic activity

An alpha-L-fucoside + H2O = L-fucose + an alcohol.

Subcellular location

Secreted Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 95 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

xyloglucan metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-L-fucosidase 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 – 1919 Potential
Chain20 – 809790Alpha-fucosidase A
PRO_0000394704

Amino acid modifications

Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2051N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential
Glycosylation6141N-linked (GlcNAc...) Potential
Glycosylation6421N-linked (GlcNAc...) Potential
Glycosylation6811N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5AU81 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: FDF201647A4BF899

FASTA80988,536
        10         20         30         40         50         60 
MRKTTLFLAV TFATSNAQGR ALRSSSPATY GTTDGSDYIL KTGYLIGNGK LGVIPFGPPD 

        70         80         90        100        110        120 
TEKLNLNVDS LWSGGPFEVE NYTGGNPSSP IYDALPGIRE RIFENGTGGM EELLGSGNHY 

       130        140        150        160        170        180 
GSSRVLGNIT IALDGVEAYS KYKRTLDLSD GVHRTSFTIA NRTTAALKSS IFCSYPDQVC 

       190        200        210        220        230        240 
VYHLESASDA RLPKVTISIE NLLVNQSLLQ TSCESEAKRA VLRHSGVTQA GPPEGMKYAA 

       250        260        270        280        290        300 
VAEVVNPRSS VTTCLGEGAL QISSRKKQLT IIIGAATNYD QKAGNAKSGW SFKNAKDPAS 

       310        320        330        340        350        360 
IVDGIASAAG WKGYQRLLDR HVKDYKKLMG DFSLELPDTT DSASKDTSEL IEKYSYASAT 

       370        380        390        400        410        420 
GNPYLENLLL DYARHLLVSS SRPNSLPANL QGRWTESLTP SWSADYHANI NLQMNYWLAD 

       430        440        450        460        470        480 
QTGLGETQHA LWNYMADTWV PRGTETARLL YNASGWVVHN EINIFGFTAM KEDAGWANYP 

       490        500        510        520        530        540 
AAAAWMMQHV WDNFDYTHDT AWLVSQGYAL LKGIASFWLS SLQEDKFFND GSLVVNPCNS 

       550        560        570        580        590        600 
PETGPTTFGC THYQQLIHQV FETVLAAQEY IHESDTKFVD SVASALERLD TGLHLSSWGG 

       610        620        630        640        650        660 
LKEWKLPDSY GYDNMSTHRH LSHLAGWYPG YSISSFAHGY RNKTIQDAVK ETLTARGMGN 

       670        680        690        700        710        720 
AADANAGWAK VWRAACWARL NDSSMAYDEL RYAIDENFVG NGLSMYWGAS PPFQIDANFG 

       730        740        750        760        770        780 
FAGAVLSMLV VDLPTPRSDP GQRTVVLGPA IPSAWGGGRA KGLRLRGGAK VDFGWDKRGV 

       790        800 
VNWVNIVKRG KGTSRVKLVN KEGDILAEM 

« 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
DQ490516 mRNA. Translation: ABF50892.1.
AACD01000141 Genomic DNA. Translation: EAA59171.1.
BN001302 Genomic DNA. Translation: CBF73981.1.
RefSeqXP_681418.1. XM_676326.1.

3D structure databases

ProteinModelPortalQ5AU81.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH95. Glycoside Hydrolase Family 95.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00004184; CADANIAP00004184; CADANIAG00004184.
GeneID2869274.
KEGGani:AN8149.2.

Phylogenomic databases

eggNOGNOG04067.
HOGENOMHOG000235039.
OMASVDFSWD.
OrthoDBEOG77HDP8.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-18214.

Family and domain databases

Gene3D2.70.98.50. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR016518. Alpha-L-fucosidase.
IPR027414. GH_fam_N_dom.
[Graphical view]
PfamPF14498. Glyco_hyd_65N_2. 1 hit.
[Graphical view]
PIRSFPIRSF007663. UCP007663. 1 hit.
SUPFAMSSF48208. SSF48208. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAFCA_EMENI
AccessionPrimary (citable) accession number: Q5AU81
Secondary accession number(s): C8V6V7, Q1HFQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: April 16, 2014
This is version 51 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries