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P23556

- XYNA_CALSA

UniProt

P23556 - XYNA_CALSA

Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 5.5-6.0.

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei144 – 1441Proton donorBy similarity
    Active sitei252 – 2521NucleophilePROSITE-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 A (EC:3.2.1.8)
    Short name:
    Xylanase A
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase A
    Gene namesi
    Name:xynA
    OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
    Taxonomic identifieri44001 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 342342Endo-1,4-beta-xylanase APRO_0000007984Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP23556.
    SMRiP23556. Positions 16-341.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    P23556-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRCLIVCENL EMLNLSLAKT YKDYFKIGAA VTAKDLEGVH RDILLKHFNS    50
    LTPENAMKFE NIHPEEQRYN FEEVARIKEF AIKNDMKLRG HTFVWHNQTP 100
    GWVFLDKNGE EASKELVIER LREHIKTLCE RYKDVVYAWD VVNEAVEDKT 150
    EKLLRESNWR KIIGDDYIKI AFEIAREYAG DAKLFYNDYN NEMPYKLEKT 200
    YKVLKELLER GTPIDGIGIQ AHWNIWDKNL VSNLKKAIEV YASLGLEIHI 250
    TELDISVFEF EDKRTDLFEP TPEMLELQAK VYEDVFAVFR EYKDVITSVT 300
    LWGISDRHTW KDNFPVKGRK DWPLLFDVNG KPKEALYRIL RF 342
    Length:342
    Mass (Da):40,455
    Last modified:November 1, 1991 - v1
    Checksum:iC5380F2AB0CC0271
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34459 Genomic DNA. Translation: AAA23059.1.
    AF005383 Genomic DNA. Translation: AAB87374.1.
    PIRiA37202. A60154.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34459 Genomic DNA. Translation: AAA23059.1 .
    AF005383 Genomic DNA. Translation: AAB87374.1 .
    PIRi A37202. A60154.

    3D structure databases

    ProteinModelPortali P23556.
    SMRi P23556. Positions 16-341.
    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 .

    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, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile 'Caldocellum saccharolyticum'."
      Luethi E., Love D.R., McAnulty J., Wallace C., Caughey P.A., Saul D.J., Bergquist P.L.
      Appl. Environ. Microbiol. 56:1017-1024(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "A cluster of genes involved in xylan degradation cloned from the extreme thermophile Caldicellulosiruptor saccharolyticus."
      Te'O V.S. Jr., Gibbs M.D., Saul D.J., Bergquist P.L.
      Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Xylanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum': overexpression of the gene in Escherichia coli and characterization of the gene product."
      Luethi E., Jasmat N.B., Bergquist P.L.
      Appl. Environ. Microbiol. 56:2677-2683(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiXYNA_CALSA
    AccessioniPrimary (citable) accession number: P23556
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3