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A2QQ94

- ABFC_ASPNC

UniProt

A2QQ94 - ABFC_ASPNC

Protein

Probable alpha-L-arabinofuranosidase C

Gene

abfC

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    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 By similarity.By similarity

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

    1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. arabinan catabolic process Source: UniProtKB-UniPathway
    2. L-arabinose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA00667.

    Protein family/group databases

    CAZyiGH51. Glycoside Hydrolase Family 51.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable alpha-L-arabinofuranosidase C (EC:3.2.1.55)
    Short name:
    ABF C
    Short name:
    Arabinosidase C
    Gene namesi
    Name:abfC
    ORF Names:An08g01710
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 8R

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 505Probable alpha-L-arabinofuranosidase CPRO_0000394614
    Signal peptidei1 – ?Sequence Analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00006368.

    Structurei

    3D structure databases

    ProteinModelPortaliA2QQ94.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 51 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3534.
    HOGENOMiHOG000236895.
    KOiK01209.
    OrthoDBiEOG71P2KW.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR010720. Alpha-L-AF_C.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF06964. Alpha-L-AF_C. 1 hit.
    [Graphical view]
    SMARTiSM00813. Alpha-L-AF_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    A2QQ94-1 [UniParc]FASTAAdd to Basket

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    MTTFTKLSDQ DAPSISIHPA RRLSKINPNI YAGFTEHMGR CIYGGIYDPG    50
    NSLSDENGFR KDVLEALKEL NIPVVRYPGG NFMATYHWID GVGPKEKRPA 100
    RPELAWLGTE TNQFGTDEFL KWCEVLGTEP YFCLNFGTGT LDEALAWVEY 150
    CNGTKDTYYA NLRRKNGREE PYNVKYWALG NETWGPWQVE QMTKEAYAHK 200
    AYQWAKALKL LDPSLILILC GQDGTASWDY YTLKQCLLPA HSPLSTSTVP 250
    LIDMHSIHLY TSSPSHLPNV TAPLAAERAI EITSSLIDLA RIENGVPPDQ 300
    HRPTICFDEW NVWDPIRAEG SKGAEESYTL SDALAVAVFL NVFVRKSKDL 350
    GMACIAQSVN VISPLMTSKD GITKQTTYWP LYLFSKYMRG WTISVHLSCA 400
    SYEGETSPKW VRGVKDTPWL DVSATLGEDG YVNVAVVNIH EEKDIRSSID 450
    GPSGTVSVFT VTGERVQACN MNGKEEVAVT ESTWEAREQF VFPKHSLTLL 500
    RWKLA 505
    Length:505
    Mass (Da):56,636
    Last modified:March 6, 2007 - v1
    Checksum:i3ACDD463A8BB24AE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270160 Genomic DNA. Translation: CAK39851.1.
    RefSeqiXP_001392290.1. XM_001392253.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00006491; CADANGAP00006368; CADANGAG00006491.
    GeneIDi4982486.
    KEGGiang:ANI_1_1698074.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270160 Genomic DNA. Translation: CAK39851.1 .
    RefSeqi XP_001392290.1. XM_001392253.1.

    3D structure databases

    ProteinModelPortali A2QQ94.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00006368.

    Protein family/group databases

    CAZyi GH51. Glycoside Hydrolase Family 51.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00006491 ; CADANGAP00006368 ; CADANGAG00006491 .
    GeneIDi 4982486.
    KEGGi ang:ANI_1_1698074.

    Phylogenomic databases

    eggNOGi COG3534.
    HOGENOMi HOG000236895.
    KOi K01209.
    OrthoDBi EOG71P2KW.

    Enzyme and pathway databases

    UniPathwayi UPA00667 .

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR010720. Alpha-L-AF_C.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF06964. Alpha-L-AF_C. 1 hit.
    [Graphical view ]
    SMARTi SM00813. Alpha-L-AF_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
      Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
      , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
      Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CBS 513.88 / FGSC A1513.

    Entry informationi

    Entry nameiABFC_ASPNC
    AccessioniPrimary (citable) accession number: A2QQ94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 44 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3