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C5J411

- XYNC_ASPNG

UniProt

C5J411 - XYNC_ASPNG

Protein

Probable endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 24 (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.

    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

    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable endo-1,4-beta-xylanase C (EC:3.2.1.8)
    Short name:
    Xylanase C
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase C
    Gene namesi
    Name:xlnC
    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 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 327308Probable endo-1,4-beta-xylanase CPRO_0000393190Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi281 ↔ 287By similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    Expressed in presence of xylan and repressed by glucose.

    Structurei

    3D structure databases

    ProteinModelPortaliC5J411.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3693.

    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.

    C5J411-1 [UniParc]FASTAAdd to Basket

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    MVQIKVAALA MLFASQVLSE PIDPRQASVS IDTKFKAHGK KYLGNIGDQY    50
    TLTKNSKTPA IIKADFGALT PENSMKWDAT EPSRGQFSFS GSDYLVNFAQ 100
    SNNKLIRGHT LVWHSQLPSW VQSITDKNTL IEVMKNHITT VMQHYKGKIY 150
    AWDVVNEIFN EDGSLRDSVF YKVIGEDYVR IAFETARAAD PNAKLYINDY 200
    NLDSASYSKL TGMVSHVKKW IAAGIPIDGI GSQTHLSAGG GAGISGALNA 250
    LAGAGTKEIA VTELDIAGAS STDYVEVVEA CLNQPKCIGI TVWGVADPDS 300
    WRSSSTPLLF DSNYNPKPAY DAIANAL 327
    Length:327
    Mass (Da):35,476
    Last modified:March 23, 2010 - v2
    Checksum:i90B2F71FFCA70A65
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 133MLF → KLI in ACR83565. 1 PublicationCurated
    Sequence conflicti23 – 231D → E in ACR83565. 1 PublicationCurated
    Sequence conflicti77 – 771W → R in ACR83565. 1 PublicationCurated
    Sequence conflicti123 – 1231S → A in ACR83565. 1 PublicationCurated
    Sequence conflicti132 – 1321E → G in ACR83565. 1 PublicationCurated
    Sequence conflicti208 – 2081S → P in ACR83565. 1 PublicationCurated
    Sequence conflicti268 – 2681G → D in ACR83565. 1 PublicationCurated
    Sequence conflicti283 – 2831N → D in ACR83565. 1 PublicationCurated
    Sequence conflicti321 – 3233DAI → FAV in ACR83565. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ986225 mRNA. Translation: ACR83565.1.
    EU848304 mRNA. Translation: ACJ26381.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ986225 mRNA. Translation: ACR83565.1 .
    EU848304 mRNA. Translation: ACJ26381.1 .

    3D structure databases

    ProteinModelPortali C5J411.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG3693.

    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. "Gene cloning, sequencing, expression and characterization of a xylanase A gene from Aspergillus niger DMS1957."
      Nguyen S.L.T., Quyen D.T.
      Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: DMS1957.
    2. Huang J.Z., Xu Y., Tian B.Y., Huang Q.G.
      Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: IME-216.

    Entry informationi

    Entry nameiXYNC_ASPNG
    AccessioniPrimary (citable) accession number: C5J411
    Secondary accession number(s): C6F1T1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 2010
    Last sequence update: March 23, 2010
    Last modified: October 1, 2014
    This is version 24 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