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P83513

- XY11A_PSEXY

UniProt

P83513 - XY11A_PSEXY

Protein

Bifunctional xylanase/deacetylase

Gene

xyn11A

Organism
Pseudobutyrivibrio xylanivorans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    Functioni

    Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is also probably able, via its C-terminal domain, to remove acetyl groups from acetylated xylan, and thus it is probably capable of hydrolyzing acetylated xylan.1 Publication

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 5.6. Active from pH 4.0 to 8.0.

    Temperature dependencei

    Optimum temperature is 38 degrees Celsius.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei108 – 1081NucleophilePROSITE-ProRule annotation
    Active sitei198 – 1981Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
    3. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Source: InterPro

    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

    BioCyciMetaCyc:MONOMER-17647.
    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiCBM36. Carbohydrate-Binding Module Family 36.
    GH11. Glycoside Hydrolase Family 11.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional xylanase/deacetylase
    Including the following 2 domains:
    Endo-1,4-beta-xylanase 11A (EC:3.2.1.8)
    Alternative name(s):
    Xylanase XynT
    Xylanase xyn11A
    Acetylated xylan deacetylase (EC:3.5.1.-)
    Gene namesi
    Name:xyn11A
    Synonyms:xynT
    OrganismiPseudobutyrivibrio xylanivorans
    Taxonomic identifieri185007 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesLachnospiraceaePseudobutyrivibrio

    Subcellular locationi

    Secreted 1 PublicationCurated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Biotechnological usei

    Could be used as a feed additive for animals in order to diminish health problems due to undigested plant fiber and enhance proliferation of beneficial microflora.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 14141 PublicationAdd
    BLAST
    Chaini15 – 602588Bifunctional xylanase/deacetylasePRO_0000184070Add
    BLAST

    Post-translational modificationi

    In the later growth phases, seems to undergo a proteolytic cleavage into a 30 kDa protein possessing xylanolytic activity.

    Structurei

    3D structure databases

    ProteinModelPortaliP83513.
    SMRiP83513. Positions 18-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini249 – 366118CBM6PROSITE-ProRule annotationAdd
    BLAST
    Domaini402 – 578177NodB homologyPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 210187EndoglucanaseAdd
    BLAST

    Domaini

    Consists of three domains: two complementary catalytic domains and one substrate-binding module.1 Publication

    Sequence similaritiesi

    Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation
    Contains 1 NodB homology domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    2.60.120.260. 1 hit.
    3.20.20.370. 1 hit.
    InterProiIPR005084. CMB_fam6.
    IPR008985. ConA-like_lec_gl_sf.
    IPR008979. Galactose-bd-like.
    IPR011330. Glyco_hydro/deAcase_b/a-brl.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    IPR002509. Polysac_deacetylase.
    [Graphical view]
    PfamiPF03422. CBM_6. 1 hit.
    PF00457. Glyco_hydro_11. 1 hit.
    PF01522. Polysacc_deac_1. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 1 hit.
    SSF88713. SSF88713. 1 hit.
    PROSITEiPS51175. CBM6. 1 hit.
    PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    PS51677. NODB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P83513-1 [UniParc]FASTAAdd to Basket

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    MSATLLVPSM TVKAADTIYN NKTGNQDGYD YELWKDTGNT SMTLNAGGTF    50
    DCSWSNINNA LFRKGKKFDS TQTYQQIGNI TFDYGCDYRP NGNSYLCVYG 100
    WTVDPLVEYY IVDSWGTWRP PGGTPKGQIQ VDGGTYDVYE TTRYNAPSIQ 150
    GDTTFKQYFS VRTSKRTSGT ISVSEHFKAW ERMGMRCGNF MKPALNIEGY 200
    QSSGSASVYK NNMTIGGSSS SSGNQGGNQG GNTGNENAGN NLVTVADADK 250
    IQCETMTKSG QYTGNISSPF NGVALYANND AVKYTQYFAS GTHDFTLRGC 300
    SNNNKMARVD LKIGGQNKGT FYYGDSYPAE YTIKNVSHGT GNQTIELVVT 350
    ADDGQWDAYL DYFNNSVEPG CSLVPGAVVV LVALGSSSNT GNNSGTNTQN 400
    QKLIALTFDD GPSSTTSQVL DMLEKYNVKA TFFLIGQNVN SNTASIVQRQ 450
    VKMGCELACH SYTHEDMTKM NASQIRNQID WTASAIKNTA GVDVKFFRPP 500
    YISVNNTMYQ NIDLPFIQGS MHNDWESSTS ASQRVNSVLS SAKDGDIILL 550
    HDFQGNSQTV SALPQIIEGL KNQGYTFVTV SELFEMKGVN PNVEYKIWSN 600
    VK 602
    Length:602
    Mass (Da):65,923
    Last modified:May 30, 2006 - v2
    Checksum:iF3D7AE32EF7A3CF0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ543424 Genomic DNA. Translation: CAD65888.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ543424 Genomic DNA. Translation: CAD65888.2 .

    3D structure databases

    ProteinModelPortali P83513.
    SMRi P83513. Positions 18-363.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM36. Carbohydrate-Binding Module Family 36.
    GH11. Glycoside Hydrolase Family 11.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .
    BioCyci MetaCyc:MONOMER-17647.

    Family and domain databases

    Gene3Di 2.60.120.180. 1 hit.
    2.60.120.260. 1 hit.
    3.20.20.370. 1 hit.
    InterProi IPR005084. CMB_fam6.
    IPR008985. ConA-like_lec_gl_sf.
    IPR008979. Galactose-bd-like.
    IPR011330. Glyco_hydro/deAcase_b/a-brl.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    IPR002509. Polysac_deacetylase.
    [Graphical view ]
    Pfami PF03422. CBM_6. 1 hit.
    PF00457. Glyco_hydro_11. 1 hit.
    PF01522. Polysacc_deac_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00911. GLHYDRLASE11.
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 1 hit.
    SSF88713. SSF88713. 1 hit.
    PROSITEi PS51175. CBM6. 1 hit.
    PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    PS51677. NODB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio xylanivorcans Mz5T."
      Cepeljnik T., Rincon M.T., Flint H.J., Marinsek-Logar R.
      Folia Microbiol. (Praha) 51:263-267(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN ORGANIZATION.
      Strain: Mz5T.
    2. "Isolation and characterization of the Pseudobutyrivibrio xylanivorans Mz5T xylanase XynT -- the first family 11 endoxylanase from rumen Butyrivibrio-related bacteria."
      Cepeljnik T., Krizaj I., Marinsek-Logar R.
      Enzyme Microb. Technol. 34:219-227(2004)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-193, PROTEIN SEQUENCE OF 15-39, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, BIOTECHNOLOGY.
      Strain: Mz5T.

    Entry informationi

    Entry nameiXY11A_PSEXY
    AccessioniPrimary (citable) accession number: P83513
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 14, 2003
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 66 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing, Multifunctional enzyme

    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