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Q12550

- XYN4_ASPNG

UniProt

Q12550 - XYN4_ASPNG

Protein

Endo-1,4-beta-xylanase 4

Gene

XYN4

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 2 (23 Mar 2010)
      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 4.0.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    Pathwayi

    Sites

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

    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.
    mycoCLAPiXYN11D_ASPNG.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase 4 (EC:3.2.1.8)
    Short name:
    Xylanase 4
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase 4
    Gene namesi
    Name:XYN4
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [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 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 211195Endo-1,4-beta-xylanase 4PRO_0000393171Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi86 – 927Poly-Ser

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG05353.

    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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q12550-1 [UniParc]FASTAAdd to Basket

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    MKVTAAFAGL LVTAFAPPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA    50
    GTFSMYWEDG VSSDFVVGLG WTTGSSNAIT YSAEYSASGS SSYLAVYGWV 100
    NLSQAEYYIV EDYGDYNPCS SATSLGTEYS DGSTYQVCTD TRTNEPSITG 150
    TSTFTQYFSV RESTRTSGTV TVAIHFNFWA QHGFGNSDFN YQVMAVEAWS 200
    GACSASVTIS S 211
    Length:211
    Mass (Da):22,669
    Last modified:March 23, 2010 - v2
    Checksum:iB27B7D7F692979EE
    GO

    Sequence cautioni

    The sequence AAA99066.1 differs from that shown. Reason: Frameshift at positions 102 and 178.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39785 mRNA. Translation: AAA99066.1. Frameshift.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39785 mRNA. Translation: AAA99066.1 . Frameshift.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.
    mycoCLAPi XYN11D_ASPNG.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG05353.

    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of two beta-xylanase-encoding genes from Aspergillus niger and their expression in Saccharomyces cerevisiae."
      Luttig M., Pretorius I.S., van Zyl W.H.
      Biotechnol. Lett. 19:411-415(1997)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 90196 / Alo MP-22.

    Entry informationi

    Entry nameiXYN4_ASPNG
    AccessioniPrimary (citable) accession number: Q12550
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 2010
    Last sequence update: March 23, 2010
    Last modified: October 1, 2014
    This is version 54 of the entry and version 2 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