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Protein

Endo-1,4-beta-xylanase

Gene

XYNA

Organism
Thermomyces lanuginosus (Humicola lanuginosa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BRENDAi3.2.1.8. 2711.
    UniPathwayiUPA00114.

    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 acid1
    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
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi37 – 41Combined sources5
    Beta strandi44 – 50Combined sources7
    Beta strandi52 – 54Combined sources3
    Beta strandi56 – 60Combined sources5
    Beta strandi65 – 70Combined sources6
    Beta strandi72 – 84Combined sources13
    Beta strandi90 – 112Combined sources23
    Turni113 – 115Combined sources3
    Beta strandi116 – 127Combined sources12
    Turni129 – 132Combined sources4
    Beta strandi134 – 141Combined sources8
    Beta strandi144 – 158Combined sources15
    Beta strandi161 – 174Combined sources14
    Beta strandi177 – 182Combined sources6
    Helixi183 – 192Combined sources10
    Beta strandi199 – 212Combined sources14
    Beta strandi214 – 223Combined sources10

    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...

    Miscellaneous databases

    EvolutionaryTraceiO43097.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    IPR013319. GH11/12.
    IPR018208. GH11_AS_1.
    IPR033119. GH11_AS_2.
    IPR033123. GH11_dom.
    IPR001137. Glyco_hydro_11.
    [Graphical view]
    PfamiPF00457. Glyco_hydro_11. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS00776. GH11_1. 1 hit.
    PS00777. GH11_2. 1 hit.
    PS51761. GH11_3. 1 hit.
    [Graphical view]

    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.

    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

    UniPathwayiUPA00114.
    BRENDAi3.2.1.8. 2711.

    Miscellaneous databases

    EvolutionaryTraceiO43097.

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    IPR013319. GH11/12.
    IPR018208. GH11_AS_1.
    IPR033119. GH11_AS_2.
    IPR033123. GH11_dom.
    IPR001137. Glyco_hydro_11.
    [Graphical view]
    PfamiPF00457. Glyco_hydro_11. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS00776. GH11_1. 1 hit.
    PS00777. GH11_2. 1 hit.
    PS51761. GH11_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiXYNA_THELA
    AccessioniPrimary (citable) accession number: O43097
    Secondary accession number(s): D1MH26
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 1, 1998
    Last modified: November 2, 2016
    This is version 92 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, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.