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A2Q7E0

- ABFA_ASPNC

UniProt

A2Q7E0 - ABFA_ASPNC

Protein

Probable alpha-L-arabinofuranosidase A

Gene

abfA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (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

    GO - Biological processi

    1. arabinan catabolic process Source: UniProtKB-UniPathway
    2. arabinose metabolic process Source: UniProtKB
    3. hemicellulose catabolic process Source: ASPGD
    4. L-arabinose metabolic process Source: ASPGD

    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 A (EC:3.2.1.55)
    Short name:
    ABF A
    Short name:
    Arabinosidase A
    Gene namesi
    Name:abfA
    ORF Names:An01g00330
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 2R

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 628603Probable alpha-L-arabinofuranosidase APRO_5000219287Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi610 – 6101N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00000030.

    Structurei

    3D structure databases

    ProteinModelPortaliA2Q7E0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 51 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000115340.
    KOiK01209.
    OrthoDBiEOG725DS5.

    Family and domain databases

    InterProiIPR010720. Alpha-L-AF_C.
    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.

    A2Q7E0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVAFSALSGV SAVSLLLSLV QNAHGISLKV STQGGNSSSP ILYGFMFEDI    50
    NHSGDGGIYG QMLQNPGLQG TAPNLTAWAA VGDATIAIDG DSPLTSAIPS 100
    TIKLNIADDA TGAVGLTNEG YWGIPVDGSE FHSSFWIKGD YSGDITVRLV 150
    GNYTGTEYGS TTITHTSTAD NFTQASVKFP TTKAPDGNVL YELTVDGSVA 200
    AGSSLNFGYL TLFGETYKSR ENGLKPQLAN VLDDMKGSFL RFPGGNNLEG 250
    NSAENRWKWN ETIGDLWDRP GREGTWTYYN TDGLGLHEYF YWCEDLGLVP 300
    VLGVWDGFAL ESGGNTPLTG DALTPYIDDV LNELEYILGD TSTTYGAWRA 350
    ANGQEEPWNL TMVEIGNEDM LGGGCESYAE RFTAFYDAIH AAYPDLILIA 400
    STSEADCLPE SMPEGSWVDY HDYSTPDGLV GQFNYFDNLN RSVPYFIGEY 450
    SRWEIDWPNM KGSVAEAVFM IGFERNSDVV KMAAYAPLLQ LINSTQWTPD 500
    LIGYTQSPGD IFLSTSYYVQ EMFSRNRGDT IKEVTSDSDF GPLYWVASSA 550
    GDSYYMKLAN YGSETQDLTV SIPGTSTGKL TVLADSDPDA YNSDTQTLVT 600
    PSESTVQASN GTFTFSLPAW AVAVLAAN 628
    Length:628
    Mass (Da):67,948
    Last modified:March 6, 2007 - v1
    Checksum:iD2961CCBB4195041
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM269950 Genomic DNA. Translation: CAK43424.1.
    RefSeqiXP_001388482.1. XM_001388445.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00000033; CADANGAP00000030; CADANGAG00000033.
    GeneIDi4978177.
    KEGGiang:ANI_1_42014.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM269950 Genomic DNA. Translation: CAK43424.1 .
    RefSeqi XP_001388482.1. XM_001388445.1.

    3D structure databases

    ProteinModelPortali A2Q7E0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00000030.

    Protein family/group databases

    CAZyi GH51. Glycoside Hydrolase Family 51.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00000033 ; CADANGAP00000030 ; CADANGAG00000033 .
    GeneIDi 4978177.
    KEGGi ang:ANI_1_42014.

    Phylogenomic databases

    HOGENOMi HOG000115340.
    KOi K01209.
    OrthoDBi EOG725DS5.

    Enzyme and pathway databases

    UniPathwayi UPA00667 .

    Family and domain databases

    InterProi IPR010720. Alpha-L-AF_C.
    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 nameiABFA_ASPNC
    AccessioniPrimary (citable) accession number: A2Q7E0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 42 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