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O59859

- XYNA_ASPAC

UniProt

O59859 - XYNA_ASPAC

Protein

Endo-1,4-beta-xylanase

Gene

xynIA

Organism
Aspergillus aculeatus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei157 – 1571Proton donorBy similarity
    Active sitei263 – 2631NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

    1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH10. Glycoside Hydrolase Family 10.
    mycoCLAPiXYN10A_ASPAC.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase (EC:3.2.1.8)
    Short name:
    Xylanase
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase
    FIA-xylanase
    Gene namesi
    Name:xynIA
    OrganismiAspergillus aculeatus
    Taxonomic identifieri5053 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    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
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Propeptidei20 – 256Sequence AnalysisPRO_0000007963
    Chaini26 – 327302Endo-1,4-beta-xylanasePRO_0000007964Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei26 – 261Pyrrolidone carboxylic acidBy similarity
    Disulfide bondi281 ↔ 287By similarity

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Structurei

    3D structure databases

    ProteinModelPortaliO59859.
    SMRiO59859. Positions 26-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O59859-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVQIKAAALA VLFASNVLAN PIEPRQASVS IDAKFKAHGK KYLGTIGDQY    50
    TLNKNAKTPA IIKADFGQLT PENSMKWDAT EPNRGQFSFS GSDYLVNFAQ 100
    SNGKLIRGHT LVWHSQLPSW VQSIYDKGTL IQVMQNHIAT VMQRYKGKVY 150
    AWDVVNEIFN EDGSLRQSHF YNVIGEDYVR IAFETARAVD PNAKLYINDY 200
    NLDSASYPKL TGLVNHVKKW VAAGVPIDGI GSQTHLSAGA GAAVSGALNA 250
    LAGAGTKEVA ITELDIAGAS STDYVNVVKA CLNQPKCVGI TVWGVADPDS 300
    WRSSSSPLLF DSNYNPKAAY TAIANAL 327
    Length:327
    Mass (Da):35,331
    Last modified:August 1, 1998 - v1
    Checksum:i4ED731EDB6FF0A74
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB013110 Genomic DNA. Translation: BAA25847.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB013110 Genomic DNA. Translation: BAA25847.1 .

    3D structure databases

    ProteinModelPortali O59859.
    SMRi O59859. Positions 26-327.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH10. Glycoside Hydrolase Family 10.
    mycoCLAPi XYN10A_ASPAC.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Arai M., Kawaguchi T., Sumitani J.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiXYNA_ASPAC
    AccessioniPrimary (citable) accession number: O59859
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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