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P40942

- CEXY_CLOSR

UniProt

P40942 - CEXY_CLOSR

Protein

Thermostable celloxylanase

Gene

xynB

Organism
Clostridium stercorarium
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Active toward xylan, carboxymethylcellulose, P-nitrophenyl-beta-D-xylopyranoside and P-nitrophenyl-beta-D-cellobioside.

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
    Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

    pH dependencei

    Optimum pH is 7.0.

    Temperature dependencei

    Optimum temperature is 80 degrees Celsius.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei185 – 1851Proton donorBy similarity
    Active sitei293 – 2931NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW
    2. xylan catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH10. Glycoside Hydrolase Family 10.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thermostable celloxylanase (EC:3.2.1.4, EC:3.2.1.8)
    Gene namesi
    Name:xynB
    OrganismiClostridium stercorarium
    Taxonomic identifieri1510 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 387387Thermostable celloxylanasePRO_0000184061Add
    BLAST

    Structurei

    Secondary structure

    1
    387
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi47 – 504
    Turni51 – 544
    Beta strandi57 – 615
    Helixi63 – 653
    Helixi68 – 7710
    Beta strandi79 – 857
    Helixi89 – 924
    Helixi102 – 11312
    Beta strandi117 – 12812
    Helixi131 – 1344
    Beta strandi139 – 1413
    Helixi142 – 1443
    Helixi148 – 17326
    Turni174 – 1763
    Beta strandi179 – 1846
    Helixi192 – 1943
    Helixi199 – 2046
    Helixi207 – 22014
    Beta strandi222 – 23110
    Helixi236 – 25116
    Beta strandi258 – 2614
    Beta strandi264 – 2685
    Helixi272 – 28312
    Turni284 – 2863
    Beta strandi288 – 29912
    Helixi313 – 33119
    Helixi332 – 3365
    Beta strandi337 – 3437
    Helixi351 – 3533
    Beta strandi355 – 3595
    Beta strandi364 – 3663
    Helixi374 – 3807

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DEPX-ray1.80A/B41-387[»]
    ProteinModelPortaliP40942.
    SMRiP40942. Positions 43-382.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40942.

    Family & Domainsi

    Sequence similaritiesi

    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.

    P40942-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKFLNKKWS LILTMGGIFL MATLSLIFAT GKKAFNDQTS AEDIPSLAEA    50
    FRDYFPIGAA IEPGYTTGQI AELYKKHVNM LVAENAMKPA SLQPTEGNFQ 100
    WADADRIVQF AKENGMELRF HTLVWHNQTP TGFSLDKEGK PMVEETDPQK 150
    REENRKLLLQ RLENYIRAVV LRYKDDIKSW DVVNEVIEPN DPGGMRNSPW 200
    YQITGTEYIE VAFRATREAG GSDIKLYIND YNTDDPVKRD ILYELVKNLL 250
    EKGVPIDGVG HQTHIDIYNP PVERIIESIK KFAGLGLDNI ITELDMSIYS 300
    WNDRSDYGDS IPDYILTLQA KRYQELFDAL KENKDIVSAV VFWGISDKYS 350
    WLNGFPVKRT NAPLLFDRNF MPKPAFWAIV DPSRLRE 387
    Length:387
    Mass (Da):44,378
    Last modified:February 1, 1995 - v1
    Checksum:iC7221BD5E32C8E48
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12504 Genomic DNA. Translation: BAA02069.1.
    PIRiJC2484.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12504 Genomic DNA. Translation: BAA02069.1 .
    PIRi JC2484.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DEP X-ray 1.80 A/B 41-387 [» ]
    ProteinModelPortali P40942.
    SMRi P40942. Positions 43-382.
    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 P40942.

    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. "Nucleotide sequence of the Clostridium stercorarium xynB gene encoding an extremely thermostable xylanase, and characterization of the translated product."
      Fukumura M., Sakka K., Shimada K., Ohmiya K.
      Biosci. Biotechnol. Biochem. 59:40-46(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: F-9.

    Entry informationi

    Entry nameiCEXY_CLOSR
    AccessioniPrimary (citable) accession number: P40942
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 72 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

    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