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Protein

Endo-1,4-beta-xylanase

Gene

XYNA

Organism
Thermomyces lanuginosus (Humicola lanuginosa)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Kineticsi

    1. Vmax=2223.3 µmol/min/mg enzyme1 Publication

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius. Thermostable.1 Publication

    Pathwayi: xylan degradation

    This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
    View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei117Nucleophile1
    Active sitei209Proton donor1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionGlycosidase, Hydrolase
    Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BRENDAi3.2.1.8 2711
    UniPathwayi
    UPA00114

    Protein family/group databases

    CAZyiGH11 Glycoside Hydrolase Family 11
    mycoCLAPiXYN11A_THELA

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase (EC:3.2.1.8)
    Short name:
    Xylanase
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase
    Gene namesi
    Name:XYNA
    OrganismiThermomyces lanuginosus (Humicola lanuginosa)
    Taxonomic identifieri5541 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeThermomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 31Add BLAST31
    ChainiPRO_000000801232 – 225Endo-1,4-beta-xylanaseAdd BLAST194

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei32Pyrrolidone carboxylic acidBy similarity1
    Disulfide bondi141 ↔ 185

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Expressioni

    Inductioni

    By xylan.1 Publication

    Structurei

    Secondary structure

    1225
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliO43097
    SMRiO43097
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43097

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini32 – 222GH11PROSITE-ProRule annotationAdd BLAST191

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.180, 1 hit
    InterProiView protein in InterPro
    IPR013320 ConA-like_dom_sf
    IPR013319 GH11/12
    IPR018208 GH11_AS_1
    IPR033119 GH11_AS_2
    IPR033123 GH11_dom
    IPR001137 Glyco_hydro_11
    PfamiView protein in Pfam
    PF00457 Glyco_hydro_11, 1 hit
    PRINTSiPR00911 GLHYDRLASE11
    SUPFAMiSSF49899 SSF49899, 1 hit
    PROSITEiView protein in PROSITE
    PS00776 GH11_1, 1 hit
    PS00777 GH11_2, 1 hit
    PS51761 GH11_3, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O43097-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MVGFTPVALA ALAATGALAF PAGNATELEK RQTTPNSEGW HDGYYYSWWS
    60 70 80 90 100
    DGGAQATYTN LEGGTYEISW GDGGNLVGGK GWNPGLNARA IHFEGVYQPN
    110 120 130 140 150
    GNSYLAVYGW TRNPLVEYYI VENFGTYDPS SGATDLGTVE CDGSIYRLGK
    160 170 180 190 200
    TTRVNAPSID GTQTFDQYWS VRQDKRTSGT VQTGCHFDAW ARAGLNVNGD
    210 220
    HYYQIVATEG YFSSGYARIT VADVG
    Length:225
    Mass (Da):24,356
    Last modified:June 1, 1998 - v1
    Checksum:iFAA79A914C5C676C
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti130S → P in ACY69861 (Ref. 2) Curated1
    Sequence conflicti177T → A in ACY69861 (Ref. 2) Curated1

    Mass spectrometryi

    Molecular mass is 21300 Da from positions 32 - 225. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U35436 Genomic DNA Translation: AAB94633.1
    GU166389 Genomic DNA Translation: ACY69861.1

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U35436 Genomic DNA Translation: AAB94633.1
    GU166389 Genomic DNA Translation: ACY69861.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1YNAX-ray1.55A33-225[»]
    ProteinModelPortaliO43097
    SMRiO43097
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH11 Glycoside Hydrolase Family 11
    mycoCLAPiXYN11A_THELA

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayi
    UPA00114

    BRENDAi3.2.1.8 2711

    Miscellaneous databases

    EvolutionaryTraceiO43097

    Family and domain databases

    Gene3Di2.60.120.180, 1 hit
    InterProiView protein in InterPro
    IPR013320 ConA-like_dom_sf
    IPR013319 GH11/12
    IPR018208 GH11_AS_1
    IPR033119 GH11_AS_2
    IPR033123 GH11_dom
    IPR001137 Glyco_hydro_11
    PfamiView protein in Pfam
    PF00457 Glyco_hydro_11, 1 hit
    PRINTSiPR00911 GLHYDRLASE11
    SUPFAMiSSF49899 SSF49899, 1 hit
    PROSITEiView protein in PROSITE
    PS00776 GH11_1, 1 hit
    PS00777 GH11_2, 1 hit
    PS51761 GH11_3, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiXYNA_THELA
    AccessioniPrimary (citable) accession number: O43097
    Secondary accession number(s): D1MH26
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 1, 1998
    Last modified: November 22, 2017
    This is version 96 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

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

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