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Q60037

- XYNA_THEMA

UniProt

Q60037 - XYNA_THEMA

Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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 6.2.

    Temperature dependencei

    Optimum temperature is 90 degrees Celsius. Thermostable.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei502 – 5021Proton donorBy similarity
    Active sitei608 – 6081NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16897.
    BRENDAi3.2.1.8. 6331.

    Protein family/group databases

    CAZyiCBM22. Carbohydrate-Binding Module Family 22.
    CBM9. Carbohydrate-Binding Module Family 9.
    GH10. 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
    Ordered Locus Names:TM_0061
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 10591029Endo-1,4-beta-xylanase APRO_0000007986Add
    BLAST

    Proteomic databases

    PRIDEiQ60037.

    Interactioni

    Protein-protein interaction databases

    STRINGi243274.TM0061.

    Structurei

    Secondary structure

    1
    1059
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi872 – 8776
    Beta strandi882 – 8854
    Helixi888 – 8925
    Beta strandi895 – 8973
    Beta strandi900 – 9045
    Turni906 – 9083
    Beta strandi911 – 9188
    Beta strandi920 – 93011
    Beta strandi938 – 9403
    Helixi941 – 9433
    Beta strandi944 – 9529
    Beta strandi965 – 9717
    Beta strandi976 – 9783
    Helixi984 – 9863
    Beta strandi987 – 9948
    Beta strandi997 – 10059
    Beta strandi1015 – 102612
    Beta strandi1032 – 10398
    Beta strandi1041 – 10433
    Turni1045 – 10473
    Helixi1049 – 10513
    Beta strandi1052 – 10587

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I82X-ray1.90A871-1059[»]
    1I8AX-ray1.90A871-1059[»]
    1I8UX-ray1.90A871-1059[»]
    ProteinModelPortaliQ60037.
    SMRiQ60037. Positions 871-1059.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60037.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini700 – 870171CBM-cenC 1Add
    BLAST
    Domaini871 – 1059189CBM-cenC 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 199153A-1Add
    BLAST
    Regioni200 – 354155A-2Add
    BLAST
    Regioni355 – 691337B, catalyticAdd
    BLAST

    Domaini

    The C-terminal CBM-CenC domains mediate the binding of XynA to microcrystalline cellulose. CBM-CenC 2 alone can also promote cellulose binding.

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG3693.
    KOiK01181.
    OMAiQNPTLEF.
    OrthoDBiEOG6B363F.

    Family and domain databases

    Gene3Di2.60.120.260. 2 hits.
    2.60.40.1190. 2 hits.
    3.20.20.80. 1 hit.
    InterProiIPR010502. Carb-bd_dom_fam9.
    IPR003305. CenC_carb-bd.
    IPR008979. Galactose-bd-like.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02018. CBM_4_9. 2 hits.
    PF06452. DUF1083. 2 hits.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 2 hits.
    SSF51445. 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.

    Q60037-1 [UniParc]FASTAAdd to Basket

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    MQVRKRRGLL DVSTAVLVGI LAGFLGVVLA ASGVLSFGKE ASSKGDSSLE     50
    TVLALSFEGT TEGVVPFGKD VVLTASQDVA ADGEYSLKVE NRTSPWDGVE 100
    IDLTGKVKSG ADYLLSFQVY QSSDAPQLFN VVARTEDEKG ERYDVILDKV 150
    VVSDHWKEIL VPFSPTFEGT PAKYSLIIVA SKNTNFNFYL DKVQVLAPKE 200
    SGPKVIYETS FENGVGDWQP RGDVNIEASS EVAHSGKSSL FISNRQKGWQ 250
    GAQINLKGIL KTGKTYAFEA WVYQNSGQDQ TIIMTMQRKY SSDASTQYEW 300
    IKSATVPSGQ WVQLSGTYTI PAGVTVEDLT LYFESQNPTL EFYVDDVKIV 350
    DTTSAEIKIE MEPEKEIPAL KEVLKDYFKV GVALPSKVFL NPKDIELITK 400
    HFNSITAENE MKPESLLAGI ENGKLKFRFE TADKYIQFVE ENGMVIRGHT 450
    LVWHNQTPDW FFKDENGNLL SKEAMTERLK EYIHTVVGHF KGKVYAWDVV 500
    NEAVDPNQPD GLRRSTWYQI MGPDYIELAF KFAREADPDA KLFYNDYNTF 550
    EPRKRDIIYN LVKDLKEKGL IDGIGMQCHI SLATDIKQIE EAIKKFSTIP 600
    GIEIHITELD MSVYRDSSSN YPEAPRTALI EQAHKMMQLF EIFKKYSNVI 650
    TNVTFWGLKD DYSWRATRRN DWPLIFDKDH QAKLAYWAIV APEVLPPLPK 700
    ESRISEGEAV VVGMMDDSYL MSKPIEILDE EGNVKATIRA VWKDSTIYIY 750
    GEVQDKTKKP AEDGVAIFIN PNNERTPYLQ PDDTYAVLWT NWKTEVNRED 800
    VQVKKFVGPG FRRYSFEMSI TIPGVEFKKD SYIGFDAAVI DDGKWYSWSD 850
    TTNSQKTNTM NYGTLKLEGI MVATAKYGTP VIDGEIDEIW NTTEEIETKA 900
    VAMGSLDKNA TAKVRVLWDE NYLYVLAIVK DPVLNKDNSN PWEQDSVEIF 950
    IDENNHKTGY YEDDDAQFRV NYMNEQTFGT GGSPARFKTA VKLIEGGYIV 1000
    EAAIKWKTIK PTPNTVIGFN IQVNDANEKG QRVGIISWSD PTNNSWRDPS 1050
    KFGNLRLIK 1059
    Length:1,059
    Mass (Da):119,643
    Last modified:November 1, 1997 - v1
    Checksum:i045936844A2D72E2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46264 Genomic DNA. Translation: CAA86406.1.
    AE000512 Genomic DNA. Translation: AAD35155.1.
    PIRiS61311.
    RefSeqiNP_227877.1. NC_000853.1.
    WP_004082550.1. NC_023151.1.
    YP_007976409.1. NC_021214.1.
    YP_008990963.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD35155; AAD35155; TM_0061.
    GeneIDi896885.
    KEGGitma:TM0061.
    tmi:THEMA_04500.
    tmm:Tmari_0058.
    PATRICi23934962. VBITheMar51294_0059.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46264 Genomic DNA. Translation: CAA86406.1 .
    AE000512 Genomic DNA. Translation: AAD35155.1 .
    PIRi S61311.
    RefSeqi NP_227877.1. NC_000853.1.
    WP_004082550.1. NC_023151.1.
    YP_007976409.1. NC_021214.1.
    YP_008990963.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I82 X-ray 1.90 A 871-1059 [» ]
    1I8A X-ray 1.90 A 871-1059 [» ]
    1I8U X-ray 1.90 A 871-1059 [» ]
    ProteinModelPortali Q60037.
    SMRi Q60037. Positions 871-1059.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM0061.

    Protein family/group databases

    CAZyi CBM22. Carbohydrate-Binding Module Family 22.
    CBM9. Carbohydrate-Binding Module Family 9.
    GH10. Glycoside Hydrolase Family 10.

    Proteomic databases

    PRIDEi Q60037.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD35155 ; AAD35155 ; TM_0061 .
    GeneIDi 896885.
    KEGGi tma:TM0061.
    tmi:THEMA_04500.
    tmm:Tmari_0058.
    PATRICi 23934962. VBITheMar51294_0059.

    Phylogenomic databases

    eggNOGi COG3693.
    KOi K01181.
    OMAi QNPTLEF.
    OrthoDBi EOG6B363F.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16897.
    BRENDAi 3.2.1.8. 6331.

    Miscellaneous databases

    EvolutionaryTracei Q60037.

    Family and domain databases

    Gene3Di 2.60.120.260. 2 hits.
    2.60.40.1190. 2 hits.
    3.20.20.80. 1 hit.
    InterProi IPR010502. Carb-bd_dom_fam9.
    IPR003305. CenC_carb-bd.
    IPR008979. Galactose-bd-like.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02018. CBM_4_9. 2 hits.
    PF06452. DUF1083. 2 hits.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima."
      Winterhalter C., Heinrich P., Candussio A., Wich G., Liebl W.
      Mol. Microbiol. 15:431-444(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

    Entry informationi

    Entry nameiXYNA_THEMA
    AccessioniPrimary (citable) accession number: Q60037
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 114 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, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3