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P55329

- XYNA_ASPNG

UniProt

P55329 - XYNA_ASPNG

Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (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.

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 3.0.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei106 – 1061Nucleophile
    Active sitei197 – 1971Proton donor

    GO - Molecular functioni

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

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BRENDAi3.2.1.8. 518.
    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH11. Glycoside Hydrolase Family 11.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase A (EC:3.2.1.8)
    Short name:
    Xylanase A
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase A
    Endo-1,4-beta-xylanase I
    Short name:
    Xylanase I
    Gene namesi
    Name:xynA
    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

    Pathology & Biotechi

    Protein family/group databases

    Allergomei980. Asp n Hemicellulase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Add
    BLAST
    Chaini28 – 211184Endo-1,4-beta-xylanase APRO_0000007992Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi119 ↔ 138

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 386
    Helixi39 – 413
    Beta strandi42 – 476
    Turni48 – 514
    Beta strandi52 – 6312
    Beta strandi65 – 739
    Beta strandi79 – 868
    Beta strandi90 – 10011
    Turni101 – 1044
    Beta strandi105 – 11511
    Beta strandi120 – 13011
    Beta strandi133 – 14513
    Beta strandi150 – 16314
    Beta strandi166 – 1705
    Helixi172 – 1798
    Helixi180 – 1823
    Beta strandi187 – 20923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T6GX-ray1.80C/D28-211[»]
    1UKRX-ray2.40A/B/C/D28-211[»]
    2QZ2X-ray2.80A28-211[»]
    ProteinModelPortaliP55329.
    SMRiP55329. Positions 29-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55329.

    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.

    P55329-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVTAAFAGL LVTAFAAPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA    50
    GTFSMYWEDG VSSDFVVGLG WTTGSSKAIT YSAEYSASGS SSYLAVYGWV 100
    NYPQAEYYIV EDYGDYNPCS SATSLGTVYS DGSTYQVCTD TRTNEPSITG 150
    TSTFTQYFSV RESTRTSGTV TVANHFNFWA QHGFGNSDFN YQVMAVEAWS 200
    GAGSASVTIS S 211
    Length:211
    Mass (Da):22,642
    Last modified:October 1, 1996 - v1
    Checksum:i82BEBEE12ED79303
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    A19535 Unassigned DNA. Translation: CAA01470.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    A19535 Unassigned DNA. Translation: CAA01470.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T6G X-ray 1.80 C/D 28-211 [» ]
    1UKR X-ray 2.40 A/B/C/D 28-211 [» ]
    2QZ2 X-ray 2.80 A 28-211 [» ]
    ProteinModelPortali P55329.
    SMRi P55329. Positions 29-210.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 980. Asp n Hemicellulase.
    CAZyi GH11. Glycoside Hydrolase Family 11.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .
    BRENDAi 3.2.1.8. 518.

    Miscellaneous databases

    EvolutionaryTracei P55329.

    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus niger: molecular basis for its low pH optimum."
      Krengel U., Dijkstra B.W.
      J. Mol. Biol. 263:70-78(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiXYNA_ASPNG
    AccessioniPrimary (citable) accession number: P55329
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 82 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

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3