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Q12667

- XYNA_PIRSP

UniProt

Q12667 - XYNA_PIRSP

Protein

Endo-1,4-beta-xylanase A

Gene

XYNA

Organism
Piromyces sp.
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Hydrolyzes 1,4-beta linked polysaccharide backbones of xylans, one of the major hemicellulose components in hardwoods and softwoods. It is more active against xylopentaose than xylotetraose, has trace activity against xylotriose. The major products released from hydrolysis of xylooligosaccharides are xylobiose and xylotriose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei510 – 5101NucleophilePROSITE-ProRule annotation
    Active sitei603 – 6031Proton donorBy similarity

    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

    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH11. Glycoside Hydrolase Family 11.
    mycoCLAPiXYN11A_PIRSP.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase A (EC:3.2.1.8)
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase
    Xylanase A
    Short name:
    XYLA
    Gene namesi
    Name:XYNA
    OrganismiPiromyces sp.
    Taxonomic identifieri45796 [NCBI]
    Taxonomic lineageiEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaePiromyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 625606Endo-1,4-beta-xylanase APRO_0000008017Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ12667.
    SMRiQ12667. Positions 292-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati259 – 268101
    Repeati269 – 278102
    Domaini286 – 32338CBM10 1Add
    BLAST
    Domaini338 – 37033CBM10 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 254235Catalytic 1Add
    BLAST
    Regioni255 – 27925LinkerAdd
    BLAST
    Regioni259 – 278202 X 10 AA tandem repeats of G-Q-G-[LQ]-G-N-G-Q-G-[NQ]Add
    BLAST
    Regioni374 – 40330LinkerAdd
    BLAST
    Regioni404 – 625222Catalytic 2Add
    BLAST

    Domaini

    Consists of an N- and C-terminal catalytic domains linked to a middle reiterated domain. Only the C-terminal catalytic domain is active.

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.60.120.180. 2 hits.
    3.90.1220.10. 2 hits.
    InterProiIPR002883. CBM10/Dockerin_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR009034. Dockerin_dom_fun.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    [Graphical view]
    PfamiPF02013. CBM_10. 2 hits.
    PF00457. Glyco_hydro_11. 2 hits.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49899. SSF49899. 2 hits.
    SSF64571. SSF64571. 2 hits.
    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.

    Q12667-1 [UniParc]FASTAAdd to Basket

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    MKLFQIFPLL LSLTSVTLAA DDFCNATGFQ GQSVVSTGHD VKKIGNIDYE    50
    QWADGGNNSA TFYSDGSFKC NFSNTKDYLC RSGVAFSQAK YPSEIGHIEA 100
    EYRLVKKSAS NVGYSYVGVY GWTLQSGISG VYEYYIVDNW LSQWRPGDWV 150
    GNTKFGDFTI DGGVYTVYKN VNGNLTQYFS LRKSERTCGT IDVTAHFAQW 200
    EKLGLKMPKI TEIKVLAEAG NTGGGCSGSV EIPYAKIYIN GKDQDGKSKG 250
    GSSSGGSNGQ GLGNGQGNGQ GQGNGQGQSA TGSGKCPSTI TSQGYKCCSS 300
    NCDIIYRDQS GDWGVENDEW CGCGSRVPKT TNCPSSIKNQ GYKCCSDSCE 350
    IVLTDSDGDW GIENDEWCGC GIKNTTPTTT TKKSNNSQPT QGQSNNNSST 400
    NTNFCSTSKH SGQSVTETSN KVGSIGGVGY ELWADSGNNS ATFYSDGSFS 450
    CSFRNAKDYL CRSGLSFDST KTYQQLGHMY ADFKLVKQNI QNVDYSYVGI 500
    YGWTRNPLVE FYVVDNWLSQ WRPGDWVGNK KHGDFTIDGA KYTVYENTRT 550
    GPSIDGNTTF KQYFSIRQQA RDCGTIDITA HFEQWEKLGM RMGKMHEAKV 600
    LGEAGSTGSG TSGTADFPYA KVYIK 625
    Length:625
    Mass (Da):68,049
    Last modified:November 1, 1996 - v1
    Checksum:i9DA99B6A17290922
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91858 mRNA. Translation: CAA62969.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91858 mRNA. Translation: CAA62969.1 .

    3D structure databases

    ProteinModelPortali Q12667.
    SMRi Q12667. Positions 292-323.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.
    mycoCLAPi XYN11A_PIRSP.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    Family and domain databases

    Gene3Di 2.60.120.180. 2 hits.
    3.90.1220.10. 2 hits.
    InterProi IPR002883. CBM10/Dockerin_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR009034. Dockerin_dom_fun.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    [Graphical view ]
    Pfami PF02013. CBM_10. 2 hits.
    PF00457. Glyco_hydro_11. 2 hits.
    [Graphical view ]
    PRINTSi PR00911. GLHYDRLASE11.
    SUPFAMi SSF49899. SSF49899. 2 hits.
    SSF64571. SSF64571. 2 hits.
    PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain."
      Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J.
      J. Biol. Chem. 270:29314-29322(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiXYNA_PIRSP
    AccessioniPrimary (citable) accession number: Q12667
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 81 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