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A2QFV7

- XYNC_ASPNC

UniProt

A2QFV7 - XYNC_ASPNC

Protein

Probable endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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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-1,4-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.

    Protein family/group databases

    CAZyiGH10. Glycoside Hydrolase Family 10.

    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
    Synonyms:xynA
    ORF Names:An03g00940
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 6R

    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_5000219726Add
    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.

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00003040.

    Structurei

    3D structure databases

    ProteinModelPortaliA2QFV7.
    SMRiA2QFV7. Positions 26-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000019847.
    OrthoDBiEOG7GJ6PM.

    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.

    A2QFV7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVQIKVAALA MLFASQVLSE PIEPRQASVS IDTKFKAHGK KYLGNIGDQY    50
    TLTKNSKTPA IIKADFGALT PENSMKWDAT EPSRGQFSFS GSDYLVNFAQ 100
    SNNKLIRGHT LVWHSQLPSW VQSITDKNTL IEVMKNHITT VMQHYKGKIY 150
    AWDVVNEIFN EDGSLRDSVF YKVIGEDYVR IAFETARAAD PNAKLYINDY 200
    NLDSASYPKL TGMVSHVKKW IAAGIPIDGI GSQTHLSAGG GAGISGALNA 250
    LAGAGTKEIA VTELDIAGAS STDYVEVVEA CLNQPKCIGI TVWGVADPDS 300
    WRSSSTPLLF DSNYNPKPAY TAIANAL 327
    Length:327
    Mass (Da):35,486
    Last modified:March 6, 2007 - v1
    Checksum:iB0769C723DD3CA09
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270045 Genomic DNA. Translation: CAK38067.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00003119; CADANGAP00003040; CADANGAG00003119.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270045 Genomic DNA. Translation: CAK38067.1 .

    3D structure databases

    ProteinModelPortali A2QFV7.
    SMRi A2QFV7. Positions 26-327.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00003040.

    Protein family/group databases

    CAZyi GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00003119 ; CADANGAP00003040 ; CADANGAG00003119 .

    Phylogenomic databases

    HOGENOMi HOG000019847.
    OrthoDBi EOG7GJ6PM.

    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. "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 nameiXYNC_ASPNC
    AccessioniPrimary (citable) accession number: A2QFV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 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