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O43097

- XYNA_THELA

UniProt

O43097 - XYNA_THELA

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Protein

Endo-1,4-beta-xylanase

Gene

XYNA

Organism
Thermomyces lanuginosus (Humicola lanuginosa)
Status
Reviewed - 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

    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei117 – 1171Nucleophile
    Active sitei209 – 2091Proton donor

    GO - Molecular functioni

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

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-UniPathway
    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. 6317.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Add
    BLAST
    Chaini32 – 225194Endo-1,4-beta-xylanasePRO_0000008012Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321Pyrrolidone carboxylic acid
    Disulfide bondi141 ↔ 185

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Expressioni

    Inductioni

    By xylan.1 Publication

    Structurei

    Secondary structure

    1
    225
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 415Combined sources
    Beta strandi44 – 507Combined sources
    Beta strandi52 – 543Combined sources
    Beta strandi56 – 605Combined sources
    Beta strandi65 – 706Combined sources
    Beta strandi72 – 8413Combined sources
    Beta strandi90 – 11223Combined sources
    Turni113 – 1153Combined sources
    Beta strandi116 – 12712Combined sources
    Turni129 – 1324Combined sources
    Beta strandi134 – 1418Combined sources
    Beta strandi144 – 15815Combined sources
    Beta strandi161 – 17414Combined sources
    Beta strandi177 – 1826Combined sources
    Helixi183 – 19210Combined sources
    Beta strandi199 – 21214Combined sources
    Beta strandi214 – 22310Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YNAX-ray1.55A33-225[»]
    ProteinModelPortaliO43097.
    SMRiO43097. Positions 32-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43097.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    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.

    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1301S → P in ACY69861. 1 PublicationCurated
    Sequence conflicti177 – 1771T → A in ACY69861. 1 PublicationCurated

    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
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YNA X-ray 1.55 A 33-225 [» ]
    ProteinModelPortali O43097.
    SMRi O43097. Positions 32-225.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.
    mycoCLAPi XYN11A_THELA.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .
    BRENDAi 3.2.1.8. 6317.

    Miscellaneous databases

    EvolutionaryTracei O43097.

    Family and domain databases

    Gene3Di 2.60.120.180. 1 hit.
    InterProi IPR013320. ConA-like_dom.
    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. "Cloning and characterization of the gene for the thermostable xylanase XynA from Thermomyces lanuginosus."
      Schlacher A., Holzmann K., Hayn M., Steiner W., Schwab H.
      J. Biotechnol. 49:211-218(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 5826 / Tsiklinsky.
    2. "Expression and characterization of the xylanase gene xynA from Thermomyces lanuginosus in Pichia pastoris."
      Guo R., Zhao N.
      Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-225.
    3. "Thermomyces lanuginosus SS-8 endo-beta-1,4-D-xylanase precursor."
      Shrivastava S., Deepalakshmi P.D., Shukla P., Mukhopadhyay K.
      Submitted (JUL-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 81-89; 154-172 AND 193-225, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, MASS SPECTROMETRY.
      Strain: SS-8.
    4. "Thermophilic xylanase from Thermomyces lanuginosus: high-resolution X-ray structure and modeling studies."
      Gruber K., Klintschar G., Hayn M., Schlacher A., Steiner W., Kratky C.
      Biochemistry 37:13475-13485(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
      Strain: DSM 5826 / Tsiklinsky.

    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 26, 2014
    This is version 85 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

    External Data

    Dasty 3