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P36917

- XYNA_THESA

UniProt

P36917 - XYNA_THESA

Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Thermoanaerobacterium saccharolyticum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Endo-acting enzyme that randomly cleaves the internal xylosidic linkages of the xylan backbone, yielding xylooligosaccharides of various lengths which are further hydrolyzed to xylose molecules by beta-xylosidase (EC 3.2.1.37). Requires at least three xylose residues for catalytic activity. Does not have activity against xylobiose.

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 5.5.

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei495 – 4951Proton donorBy similarity
    Active sitei537 – 53711 Publication
    Active sitei600 – 6001Nucleophile1 PublicationPROSITE-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-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    UniPathwayiUPA00114.

    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
    OrganismiThermoanaerobacterium saccharolyticum
    Taxonomic identifieri28896 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisThermoanaerobacterium

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi537 – 5371D → N: Loss of activity. 1 Publication
    Mutagenesisi600 – 6001E → Q: Loss of activity. 1 Publication
    Mutagenesisi602 – 6021D → N: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 33331 PublicationAdd
    BLAST
    Chaini34 – 11571124Endo-1,4-beta-xylanase APRO_0000007980Add
    BLAST

    Expressioni

    Inductioni

    By xylan and xylose.

    Structurei

    3D structure databases

    ProteinModelPortaliP36917.
    SMRiP36917. Positions 859-1043.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 189152CBM-cenC 1Add
    BLAST
    Domaini195 – 343149CBM-cenC 2Add
    BLAST
    Domaini1051 – 111464SLH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1115 – 115743SLH 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni413 – 649237CatalyticSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 2 SLH (S-layer homology) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    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.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR001119. S-layer_homology_dom.
    [Graphical view]
    PfamiPF02018. CBM_4_9. 2 hits.
    PF06452. DUF1083. 2 hits.
    PF00331. Glyco_hydro_10. 1 hit.
    PF00395. SLH. 2 hits.
    [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.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    PS51272. SLH. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P36917-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMKNNVDRIV SIVTALIMIF GASLFSPPIR VFADDTNINL VSNGDFESGT     50
    IDGWIKQGNP TLAVTTEQAI GQYSMKVTGR TQTYEGPAYS FLGKMQKGES 100
    YSVSLKVRLV SGQNSSNPLI TVTMFREDDN GKHYDTIVWQ KQVSEDSWTT 150
    VSGTYTLDYI GTLKTLYMYV ESPDPTLEYY IDDVVVTTQN PIQVGNVIAN 200
    ETFENGNTSG WIGTGSSVVK AVYGVAHSGD YSLLTTGRTA NWNGPSYDLT 250
    GKIVPGQQYN VDFWVKFVNG NDTEQIKATV KATSDKDNYI QVNDFANVNK 300
    GEWTEIKGSF TLPVADYSGI SIYVESQNPT LEFYIDDFSV IGEISNNQIT 350
    IQNDIPDLYS VFKDYFPIGV AVDPSRLNDA DPHAQLTAKH FNMLVAENAM 400
    KPESLQPTEG NFTFDNADKI VDYAIAHNMK MRGHTLLWHN QVPDWFFQDP 450
    SDPSKSASRD LLLQRLKTHI TTVLDHFKTK YGSQNPIIGW DVVNEVLDDN 500
    GNLRNSKWLQ IIGPDYIEKA FEYAHEADPS MKLFINDYNI ENNGVKTQAM 550
    YDLVKKLKSE GVPIDGIGMQ MHININSNID NIKASIEKLA SLGVEIQVTE 600
    LDMNMNGNIS NEALLKQARL YKQLFDLFKA EKQYITAVVF WGVSDDVTWL 650
    SKPNAPLLFD SKLQAKPAFW AVVDPSKAIP DIQSAKALEG SPTIGANVDS 700
    SWKLVKPLYV NTYVEGTVGA TATVKSMWDT KNLYLLVQVS DNTPSNNDGI 750
    EIFVDKNDDK STSYETDDER YTIKRDGTGS SDITKYVTSN ADGYVAQLAI 800
    PIEDISPAVN DKIGFDIRIN DDKGNGKIDA ITVWNDYTNS QNTNTSYFGD 850
    IVLSKSAQIA TAIYGTPVID GKVDDIWNNV EPISTNTWIL GSNGATATQK 900
    MMWDDKYLYV LADVTDSNLN KSSINPYEQD SVEVFVDQNN DKTTYYENDD 950
    GQYRVNYDNE QSFGGSTNSN GFKSATSLTQ SGYIVEEAIP WTSITPSNGT 1000
    IIGFDLQVNN ADENGKRTGI VTWCDPSGNS WQDTSGFGNL LLTGKPSGAL 1050
    KKGVTFDDIK NSWAKDAIEV LASRHIVEGM TDTQYEPNKT VTRAEFTAMI 1100
    LRLLNIKEEQ YSGEFSDVNS GDWYANAIEA AYKAGIIEGD GKNARPNDSI 1150
    TREEMTQ 1157
    Length:1,157
    Mass (Da):128,380
    Last modified:June 1, 1994 - v1
    Checksum:i51FA6004497EC58B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97882 Genomic DNA. Translation: AAA21812.1. Sequence problems.
    PIRiA48490.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97882 Genomic DNA. Translation: AAA21812.1 . Sequence problems.
    PIRi A48490.

    3D structure databases

    ProteinModelPortali P36917.
    SMRi P36917. Positions 859-1043.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    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.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR001119. S-layer_homology_dom.
    [Graphical view ]
    Pfami PF02018. CBM_4_9. 2 hits.
    PF06452. DUF1083. 2 hits.
    PF00331. Glyco_hydro_10. 1 hit.
    PF00395. SLH. 2 hits.
    [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.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    PS51272. SLH. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene cloning, sequencing, and biochemical characterization of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI."
      Lee Y.-E., Lowe S.E., Zeikus J.G.
      Appl. Environ. Microbiol. 59:3134-3137(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-41.
      Strain: ATCC 49915 / DSM 7060 / B6A-RI.
    2. "Characterization of the active site and thermostability regions of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI."
      Lee Y.-E., Lowe S.E., Henrissat B., Zeikus J.G.
      J. Bacteriol. 175:5890-5898(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, MUTAGENESIS.

    Entry informationi

    Entry nameiXYNA_THESA
    AccessioniPrimary (citable) accession number: P36917
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 93 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3