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P55330

- XYNB_ASPNG

UniProt

P55330 - XYNB_ASPNG

Protein

Endo-1,4-beta-xylanase B

Gene

xlnB

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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.

    Enzyme regulationi

    Metal ions, copper, iron and N-bromosuccinimide decrease enzyme activity. Manganese, calcium, L-tryptophan, beta-mercaptoethanol, L-cysteine and dithiodipyridine stimulate the enzyme activity.1 Publication

    pH dependencei

    Optimum pH is 5.0. Retains about 76 percent of its activity after being incubated at pH 2.0 for 30 min at 37 degrees Celsius.2 Publications

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius. Displays about 95 percent of peak activity in the temperature range from 37 to 41 degrees Celsius.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei121 – 1211NucleophilePROSITE-ProRule annotation
    Active sitei212 – 2121Proton 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase B (EC:3.2.1.8)
    Short name:
    Xylanase B
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase B
    Endo-1,4-beta-xylanase G1
    Short name:
    Xylanase G1
    Endo-1,4-beta-xylanase II
    Short name:
    Xylanase II
    Gene namesi
    Name:xlnB
    Synonyms:xyn2, xynB, xynG1
    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 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 3719PRO_0000007993Add
    BLAST
    Chaini38 – 225188Endo-1,4-beta-xylanase BPRO_0000007994Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP55330.
    SMRiP55330. Positions 39-224.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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.
    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.

    P55330-1 [UniParc]FASTAAdd to Basket

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    MLTKNLLLCF AAAKAALAVP HDSVAQRSDA LHMLSERSTP SSTGENNGFY    50
    YSFWTDGGGD VTYTNGDAGA YTVEWSNVGN FVGGKGWNPG SAQDITYSGT 100
    FTPSGNGYLS VYGWTTDPLI EYYIVESYGD YNPGSGGTYK GTVTSDGSVY 150
    DIYTATRTNA ASIQGTATFT QYWSVRQNKR VGGTVTTSNH FNAWAKLGMN 200
    LGTHNYQIVA TEGYQSSGSS SITVQ 225
    Length:225
    Mass (Da):24,057
    Last modified:October 1, 1996 - v1
    Checksum:iC4B8BB007AB2B8FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161A → V in AAM08362. 1 PublicationCurated
    Sequence conflicti16 – 161A → V in AAM95167. 1 PublicationCurated
    Sequence conflicti16 – 161A → V in ABA00146. 1 PublicationCurated
    Sequence conflicti16 – 161A → V in AAS46914. 1 PublicationCurated
    Sequence conflicti16 – 161A → V in ACA51680. 1 PublicationCurated
    Sequence conflicti25 – 262AQ → VE in AAM08362. 1 PublicationCurated
    Sequence conflicti25 – 262AQ → VE in AAM95167. 1 PublicationCurated
    Sequence conflicti25 – 262AQ → VE in ABA00146. 1 PublicationCurated
    Sequence conflicti25 – 262AQ → VE in AAS46914. 1 PublicationCurated
    Sequence conflicti25 – 262AQ → VE in ACA51680. 1 PublicationCurated
    Sequence conflicti33 – 331M → K in AAM08362. 1 PublicationCurated
    Sequence conflicti33 – 331M → K in AAM95167. 1 PublicationCurated
    Sequence conflicti33 – 331M → K in ABA00146. 1 PublicationCurated
    Sequence conflicti33 – 331M → K in AAS46914. 1 PublicationCurated
    Sequence conflicti33 – 331M → K in ACA51680. 1 PublicationCurated
    Sequence conflicti70 – 701A → S in AAM08362. 1 PublicationCurated
    Sequence conflicti70 – 701A → S in AAM95167. 1 PublicationCurated
    Sequence conflicti70 – 701A → S in ABA00146. 1 PublicationCurated
    Sequence conflicti70 – 701A → S in AAS46914. 1 PublicationCurated
    Sequence conflicti70 – 701A → S in ACA51680. 1 PublicationCurated
    Sequence conflicti76 – 761S → P in ACJ26382. 1 PublicationCurated
    Sequence conflicti130 – 1301D → V in ACA24724. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38071 Genomic DNA. Translation: BAA07265.1.
    AF490982 mRNA. Translation: AAM08362.1.
    AY126481 Genomic DNA. Translation: AAM95167.1.
    DQ174549 Genomic DNA. Translation: ABA00146.1.
    AY536639 mRNA. Translation: AAS46914.1.
    EU423881 Genomic DNA. Translation: ACA24724.1.
    EU430370 mRNA. Translation: ACA51680.1.
    EU848305 mRNA. Translation: ACJ26382.1.
    FJ772090 mRNA. Translation: ACN89393.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38071 Genomic DNA. Translation: BAA07265.1 .
    AF490982 mRNA. Translation: AAM08362.1 .
    AY126481 Genomic DNA. Translation: AAM95167.1 .
    DQ174549 Genomic DNA. Translation: ABA00146.1 .
    AY536639 mRNA. Translation: AAS46914.1 .
    EU423881 Genomic DNA. Translation: ACA24724.1 .
    EU430370 mRNA. Translation: ACA51680.1 .
    EU848305 mRNA. Translation: ACJ26382.1 .
    FJ772090 mRNA. Translation: ACN89393.1 .

    3D structure databases

    ProteinModelPortali P55330.
    SMRi P55330. Positions 39-224.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.

    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.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Ito K.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: IFO 4066 / RIB 1061.
    2. Gu S., Sun J., Xu Z., Li W., Zhao H.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "High-level expression of xylanase B of Aspergillus niger in Pichia pastoris."
      Zhu L., Liu W., Dong Z., Yu W.
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Cloning of a gene encoding an acidophilic endo-beta-1,4-xylanase obtained from Aspergillus niger CGMCC1067 and constitutive expression in Pichia pastoris."
      Deng P., Li D., Cao Y., Lu W., Wang C.
      Enzyme Microb. Technol. 39:1096-1102(2006)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    5. "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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: IBT-90.
    6. "Isolation and identification of xynB from Aspergillus niger."
      Su Y., Bai J., Chen G.
      Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Cloning, expression and characterization of the xylanase B from Aspergillus niger F19 in Escherichia coli."
      Cui L., Zhang Z., Zhu M., Wang C.
      Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: F19.
    8. "Gene cloning, sequencing, expression and characterization of a xylanase 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.
    9. "Expression of Xylanase Gene xynB from Aspergillus niger in Escherichia coli and Characterization of Its Recombinant Xylanase."
      Yi X., Qiao D., Cao Y.
      Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: SCTCC 400264.

    Entry informationi

    Entry nameiXYNB_ASPNG
    AccessioniPrimary (citable) accession number: P55330
    Secondary accession number(s): B1A5N7
    , C0LVA6, C6F1T2, Q12557, Q8TG22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 75 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