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P35809

- XYNA_SCHCO

UniProt

P35809 - XYNA_SCHCO

Protein

Endo-1,4-beta-xylanase A

Gene

XYNA

Organism
Schizophyllum commune (Split gill fungus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Hydrolyzes xylans into xylobiose and xylose.

    Catalytic activityi

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

    pH dependencei

    Active over a very broad pH range.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei87 – 871Nucleophile1 Publication
    Active sitei184 – 1841Proton donorPROSITE-ProRule annotation

    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_SCHCO.

    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
    Gene namesi
    Name:XYNA
    OrganismiSchizophyllum commune (Split gill fungus)
    Taxonomic identifieri5334 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesSchizophyllaceaeSchizophyllum

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 197197Endo-1,4-beta-xylanase APRO_0000184071Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi111 ↔ 1601 Publication

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliP35809.
    SMRiP35809. Positions 3-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    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.

    P35809-1 [UniParc]FASTAAdd to Basket

    « Hide

    SGTPSSTGTD GGYYYSWWTD GAGDATYQNN GGGSYTLTWS GNNGNLVGGK    50
    GWNPGAASRS ISYSGTYQPN GNSYLSVYGW TRSSLIEYYI VESYGSYDPS 100
    SAASHKGSVT CNGATYDILS TWRYNAPSID GTQTFEQFWS VRNPKKAPGG 150
    SISGTVDVQC HFDAWKGLGM NLGSEHNYQI VATEGYQSSG TATITVT 197
    Length:197
    Mass (Da):20,979
    Last modified:June 1, 1994 - v1
    Checksum:i42C8074E67C1FBE9
    GO

    Sequence databases

    PIRiA44597.

    Cross-referencesi

    Sequence databases

    PIRi A44597.

    3D structure databases

    ProteinModelPortali P35809.
    SMRi P35809. Positions 3-196.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.
    mycoCLAPi XYN11A_SCHCO.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. Yaguchi M., Roy C., Ujiie M., Watson D.C., Wakarchuk W.
      (In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J. (eds.); Xylans and xylanases, pp.149-154, Elsevier, Amsterdam (1992)
      Cited for: PROTEIN SEQUENCE.
      Strain: ATCC 38548 / Delmar / 13 / IHEM 5263.
    2. "Amino acid sequence and thermostability of xylanase A from Schizophyllum commune."
      Oku T., Roy C., Watson D.C., Wakarchuk W., Campbell R., Yaguchi M., Jurasek L., Paice M.G.
      FEBS Lett. 334:296-300(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS.
      Strain: ATCC 38548 / Delmar / 13 / IHEM 5263.
    3. "Identification of a glutamate residue at the active site of xylanase A from Schizophyllum commune."
      Bray M.R., Clarke A.J.
      Eur. J. Biochem. 219:821-827(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, ACTIVE SITE GLU-87.
      Strain: ATCC 38548 / Delmar / 13 / IHEM 5263.

    Entry informationi

    Entry nameiXYNA_SCHCO
    AccessioniPrimary (citable) accession number: P35809
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 76 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

    Direct protein sequencing

    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