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Q5AU81

- AFCA_EMENI

UniProt

Q5AU81 - AFCA_EMENI

Protein

Alpha-fucosidase A

Gene

afcA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

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

    GO - Molecular functioni

    1. alpha-L-fucosidase activity Source: UniProtKB

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW
    2. xyloglucan metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18214.

    Protein family/group databases

    CAZyiGH95. Glycoside Hydrolase Family 95.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-fucosidase A (EC:3.2.1.51)
    Alternative name(s):
    Alpha-L-fucoside fucohydrolase A
    Gene namesi
    Name:afcA
    ORF Names:AN8149
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome II

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 809790Alpha-fucosidase APRO_0000394704Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi614 – 6141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi642 – 6421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi681 – 6811N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ5AU81.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 95 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG04067.
    HOGENOMiHOG000235039.
    OMAiSVDFSWD.
    OrthoDBiEOG77HDP8.

    Family and domain databases

    Gene3Di2.70.98.50. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR016518. Alpha-L-fucosidase.
    IPR027414. GH_fam_N_dom.
    [Graphical view]
    PfamiPF14498. Glyco_hyd_65N_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF007663. UCP007663. 1 hit.
    SUPFAMiSSF48208. SSF48208. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5AU81-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKTTLFLAV TFATSNAQGR ALRSSSPATY GTTDGSDYIL KTGYLIGNGK    50
    LGVIPFGPPD TEKLNLNVDS LWSGGPFEVE NYTGGNPSSP IYDALPGIRE 100
    RIFENGTGGM EELLGSGNHY GSSRVLGNIT IALDGVEAYS KYKRTLDLSD 150
    GVHRTSFTIA NRTTAALKSS IFCSYPDQVC VYHLESASDA RLPKVTISIE 200
    NLLVNQSLLQ TSCESEAKRA VLRHSGVTQA GPPEGMKYAA VAEVVNPRSS 250
    VTTCLGEGAL QISSRKKQLT IIIGAATNYD QKAGNAKSGW SFKNAKDPAS 300
    IVDGIASAAG WKGYQRLLDR HVKDYKKLMG DFSLELPDTT DSASKDTSEL 350
    IEKYSYASAT GNPYLENLLL DYARHLLVSS SRPNSLPANL QGRWTESLTP 400
    SWSADYHANI NLQMNYWLAD QTGLGETQHA LWNYMADTWV PRGTETARLL 450
    YNASGWVVHN EINIFGFTAM KEDAGWANYP AAAAWMMQHV WDNFDYTHDT 500
    AWLVSQGYAL LKGIASFWLS SLQEDKFFND GSLVVNPCNS PETGPTTFGC 550
    THYQQLIHQV FETVLAAQEY IHESDTKFVD SVASALERLD TGLHLSSWGG 600
    LKEWKLPDSY GYDNMSTHRH LSHLAGWYPG YSISSFAHGY RNKTIQDAVK 650
    ETLTARGMGN AADANAGWAK VWRAACWARL NDSSMAYDEL RYAIDENFVG 700
    NGLSMYWGAS PPFQIDANFG FAGAVLSMLV VDLPTPRSDP GQRTVVLGPA 750
    IPSAWGGGRA KGLRLRGGAK VDFGWDKRGV VNWVNIVKRG KGTSRVKLVN 800
    KEGDILAEM 809
    Length:809
    Mass (Da):88,536
    Last modified:April 26, 2005 - v1
    Checksum:iFDF201647A4BF899
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490516 mRNA. Translation: ABF50892.1.
    AACD01000141 Genomic DNA. Translation: EAA59171.1.
    BN001302 Genomic DNA. Translation: CBF73981.1.
    RefSeqiXP_681418.1. XM_676326.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00004184; CADANIAP00004184; CADANIAG00004184.
    GeneIDi2869274.
    KEGGiani:AN8149.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490516 mRNA. Translation: ABF50892.1 .
    AACD01000141 Genomic DNA. Translation: EAA59171.1 .
    BN001302 Genomic DNA. Translation: CBF73981.1 .
    RefSeqi XP_681418.1. XM_676326.1.

    3D structure databases

    ProteinModelPortali Q5AU81.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH95. Glycoside Hydrolase Family 95.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00004184 ; CADANIAP00004184 ; CADANIAG00004184 .
    GeneIDi 2869274.
    KEGGi ani:AN8149.2.

    Phylogenomic databases

    eggNOGi NOG04067.
    HOGENOMi HOG000235039.
    OMAi SVDFSWD.
    OrthoDBi EOG77HDP8.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-18214.

    Family and domain databases

    Gene3Di 2.70.98.50. 1 hit.
    InterProi IPR008928. 6-hairpin_glycosidase-like.
    IPR016518. Alpha-L-fucosidase.
    IPR027414. GH_fam_N_dom.
    [Graphical view ]
    Pfami PF14498. Glyco_hyd_65N_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF007663. UCP007663. 1 hit.
    SUPFAMi SSF48208. SSF48208. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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.

    Entry informationi

    Entry nameiAFCA_EMENI
    AccessioniPrimary (citable) accession number: Q5AU81
    Secondary accession number(s): C8V6V7, Q1HFQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 52 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3