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A2QT85

- ABNA_ASPNC

UniProt

A2QT85 - ABNA_ASPNC

Protein

Probable arabinan endo-1,5-alpha-L-arabinosidase A

Gene

abnA

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 45 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan By similarity.By similarity

    Catalytic activityi

    Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.

    Pathwayi

    GO - Molecular functioni

    1. arabinan endo-1,5-alpha-L-arabinosidase activity Source: ASPGD

    GO - Biological processi

    1. arabinan catabolic process Source: UniProtKB-UniPathway
    2. hemicellulose catabolic process Source: ASPGD
    3. xylan catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    UniPathwayiUPA00667.

    Protein family/group databases

    CAZyiGH43. Glycoside Hydrolase Family 43.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable arabinan endo-1,5-alpha-L-arabinosidase A (EC:3.2.1.99)
    Alternative name(s):
    Endo-1,5-alpha-L-arabinanase A
    Short name:
    ABN A
    Gene namesi
    Name:abnA
    ORF Names:An09g01190
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 1L

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: ASPGD

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 321302Probable arabinan endo-1,5-alpha-L-arabinosidase APRO_5000220397Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00007516.

    Structurei

    3D structure databases

    ProteinModelPortaliA2QT85.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 43 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000292006.
    KOiK06113.
    OrthoDBiEOG761C4Q.

    Family and domain databases

    Gene3Di2.115.10.20. 1 hit.
    InterProiIPR006710. Glyco_hydro_43.
    IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
    IPR023296. Glyco_hydro_beta-prop.
    [Graphical view]
    PANTHERiPTHR22925. PTHR22925. 1 hit.
    PfamiPF04616. Glyco_hydro_43. 1 hit.
    [Graphical view]
    PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
    SUPFAMiSSF75005. SSF75005. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    A2QT85-1 [UniParc]FASTAAdd to Basket

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    MYRLLSVASV PLLASLVHGY ADPGACSGVC TTHDPGLIRR ESDGTYFLFS    50
    TGNKISYVSA SSIEGPWTSV GSMLPDGSSI DLDGNDDLWA PDVSYVDGLY 100
    YVYYAVSTFG SQDSAIGLAT SETMEYGSWT DHGSTGIASS SAKIYNAIDP 150
    NLIYADGTYY INFGSFWDDI YQVPMKSTPT AAASSSYNLA YDPSGTHAEE 200
    GSYMFQYGDY YYLFYSAGIC CGYDTSMPAS GEEYHIKVCR STSPTGDFVD 250
    SDGTACTDGG GTMVLESHGE VYGPGGQGVY DDPNLGPVLY YHYMNTTIGY 300
    ADSDAQFGWN TIDFSSGWPV V 321
    Length:321
    Mass (Da):34,483
    Last modified:March 6, 2007 - v1
    Checksum:i8D176BE3D62B15F0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270193 Genomic DNA. Translation: CAK49041.1.
    RefSeqiXP_001393437.1. XM_001393400.2.

    Genome annotation databases

    EnsemblFungiiCADANGAT00007653; CADANGAP00007516; CADANGAG00007653.
    GeneIDi4983650.
    KEGGiang:ANI_1_118084.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270193 Genomic DNA. Translation: CAK49041.1 .
    RefSeqi XP_001393437.1. XM_001393400.2.

    3D structure databases

    ProteinModelPortali A2QT85.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00007516.

    Protein family/group databases

    CAZyi GH43. Glycoside Hydrolase Family 43.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00007653 ; CADANGAP00007516 ; CADANGAG00007653 .
    GeneIDi 4983650.
    KEGGi ang:ANI_1_118084.

    Phylogenomic databases

    HOGENOMi HOG000292006.
    KOi K06113.
    OrthoDBi EOG761C4Q.

    Enzyme and pathway databases

    UniPathwayi UPA00667 .

    Family and domain databases

    Gene3Di 2.115.10.20. 1 hit.
    InterProi IPR006710. Glyco_hydro_43.
    IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
    IPR023296. Glyco_hydro_beta-prop.
    [Graphical view ]
    PANTHERi PTHR22925. PTHR22925. 1 hit.
    Pfami PF04616. Glyco_hydro_43. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
    SUPFAMi SSF75005. SSF75005. 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 nameiABNA_ASPNC
    AccessioniPrimary (citable) accession number: A2QT85
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 45 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