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P40943

- XYN1_GEOSE

UniProt

P40943 - XYN1_GEOSE

Protein

Endo-1,4-beta-xylanase

Gene
N/A
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei187 – 1871Proton donorBy similarity
    Active sitei293 – 2931NucleophilePROSITE-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

    CAZyiGH10. Glycoside Hydrolase Family 10.

    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
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    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
    Signal peptidei1 – 28281 PublicationAdd
    BLAST
    Chaini29 – 407379Endo-1,4-beta-xylanasePRO_0000007968Add
    BLAST

    Expressioni

    Inductioni

    By xylose.

    Structurei

    Secondary structure

    1
    407
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni34 – 363
    Helixi42 – 443
    Helixi48 – 525
    Turni53 – 553
    Beta strandi57 – 626
    Helixi64 – 685
    Helixi70 – 7910
    Beta strandi81 – 877
    Helixi91 – 944
    Helixi104 – 11512
    Beta strandi119 – 1235
    Beta strandi128 – 1303
    Helixi133 – 1364
    Beta strandi141 – 1433
    Helixi144 – 1463
    Helixi150 – 17526
    Turni176 – 1783
    Beta strandi181 – 1877
    Beta strandi193 – 1953
    Helixi199 – 2046
    Helixi207 – 22014
    Beta strandi224 – 2318
    Helixi238 – 25114
    Beta strandi258 – 2614
    Beta strandi267 – 2704
    Helixi272 – 28413
    Beta strandi288 – 2969
    Beta strandi306 – 3083
    Helixi309 – 3113
    Helixi314 – 33320
    Helixi335 – 3373
    Beta strandi338 – 34710
    Helixi352 – 3565
    Beta strandi359 – 3613
    Beta strandi376 – 3794
    Beta strandi388 – 3903
    Beta strandi394 – 3963
    Helixi398 – 4047

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HIZX-ray2.40A29-407[»]
    1R85X-ray1.45A29-407[»]
    1R86X-ray1.80A29-407[»]
    1R87X-ray1.67A29-407[»]
    3MMDX-ray1.70A29-407[»]
    ProteinModelPortaliP40943.
    SMRiP40943. Positions 33-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40943.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P40943-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRNVVRKPLT IGLALTLLLP MGMTATSAKN ADSYAKKPHI SALNAPQLDQ    50
    RYKNEFTIGA AVEPYQLQNE KDVQMLKRHF NSIVAENVMK PISIQPEEGK 100
    FNFEQADRIV KFAKANGMDI RFHTLVWHSQ VPQWFFLDKE GKPMVNETDP 150
    VKREQNKQLL LKRLETHIKT IVERYKDDIK YWDVVNEVVG DDGKLRNSPW 200
    YQIAGIDYIK VAFQAARKYG GDNIKLYMND YNTEVEPKRT ALYNLVKQLK 250
    EEGVPIDGIG HQSHIQIGWP SEAEIEKTIN MFAALGLDNQ ITELDVSMYG 300
    WPPRAYPTYD AIPKQKFLDQ AARYDRLFKL YEKLSDKISN VTFWGIADNH 350
    TWLDSRADVY YDANGNVVVD PNAPYAKVEK GKGKDAPFVF GPDYKVKPAY 400
    WAIIDHK 407
    Length:407
    Mass (Da):46,763
    Last modified:February 1, 1995 - v1
    Checksum:iAD385C90B252B82A
    GO

    Sequence cautioni

    The sequence ABI49951.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ868502 Genomic DNA. Translation: ABI49951.1. Different initiation.
    PIRiI40570.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ868502 Genomic DNA. Translation: ABI49951.1 . Different initiation.
    PIRi I40570.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HIZ X-ray 2.40 A 29-407 [» ]
    1R85 X-ray 1.45 A 29-407 [» ]
    1R86 X-ray 1.80 A 29-407 [» ]
    1R87 X-ray 1.67 A 29-407 [» ]
    3MMD X-ray 1.70 A 29-407 [» ]
    ProteinModelPortali P40943.
    SMRi P40943. Positions 33-407.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    Miscellaneous databases

    EvolutionaryTracei P40943.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and DNA sequence of the gene coding for Bacillus stearothermophilus T-6 xylanase."
      Gat O., Lapidot A., Alchanati I., Regueros C., Shoham Y.
      Appl. Environ. Microbiol. 60:1889-1896(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: T-6 / NCIMB 40221.
    2. "Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6."
      Khasin A., Alchanati I., Shoham Y.
      Appl. Environ. Microbiol. 59:1725-1730(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-73.
      Strain: T-6.

    Entry informationi

    Entry nameiXYN1_GEOSE
    AccessioniPrimary (citable) accession number: P40943
    Secondary accession number(s): Q09LX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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