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Q6QJ75

- XYN6_ASPNG

UniProt

Q6QJ75 - XYN6_ASPNG

Protein

Endo-1,4-beta-xylanase 6

Gene

XYN6

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.By similarity

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 3.5.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei106 – 1061NucleophilePROSITE-ProRule annotation
    Active sitei197 – 1971Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH11. Glycoside Hydrolase Family 11.
    mycoCLAPiXYN11F_ASPNG.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase 6 (EC:3.2.1.8)
    Short name:
    Xylanase 6
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase 6
    Gene namesi
    Name:XYN6
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    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 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 211195Endo-1,4-beta-xylanase 6PRO_0000393173Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00011453.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6QJ75.
    SMRiQ6QJ75. Positions 29-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    [Graphical view]
    PfamiPF00457. Glyco_hydro_11. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q6QJ75-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVTAAFAGL LVTALAAPAP EPVLVSRSAG INYVQNYNGN LGDFTYDESA    50
    GTFSMYWEDG VSSDFVVGLG WTTGSSNPIT YSADYSASGS SSYLAVYGWD 100
    NYPQAEYYIV EDYGDYNPCS SATSLGTVYS DGSTYQVCTD TRTNEPSITG 150
    TSTFTQYFSV RESTRTSGTV TVANHFNFWA QHGFGNSDFN YQVVAVEAWS 200
    GAGSASVTIS S 211
    Length:211
    Mass (Da):22,561
    Last modified:July 5, 2004 - v1
    Checksum:i973CD0651D5F8C9A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY536638 mRNA. Translation: AAS46913.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY536638 mRNA. Translation: AAS46913.1 .

    3D structure databases

    ProteinModelPortali Q6QJ75.
    SMRi Q6QJ75. Positions 29-210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00011453.

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.
    mycoCLAPi XYN11F_ASPNG.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    Family and domain databases

    Gene3Di 2.60.120.180. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    [Graphical view ]
    Pfami PF00457. Glyco_hydro_11. 1 hit.
    [Graphical view ]
    PRINTSi PR00911. GLHYDRLASE11.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Efficient expression and secretion of two co-produced xylanases from Aspergillus niger in Pichia pastoris directed by their native signal peptides and the Saccharomyces cerevisiae a-mating factor."
      Korona B., Korona D., Bielecki S.
      Enzyme Microb. Technol. 39:683-689(2006)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: IBT-90.

    Entry informationi

    Entry nameiXYN6_ASPNG
    AccessioniPrimary (citable) accession number: Q6QJ75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 2010
    Last sequence update: July 5, 2004
    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

    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