Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O69231

- XYNB_PAEBA

UniProt

O69231 - XYNB_PAEBA

Protein

Endo-1,4-beta-xylanase B

Gene

xynB

Organism
Paenibacillus barcinonensis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a role in plant xylan biodegradation, probably via the hydrolysis of short xylooligosaccharides resulting from extracellular xylan hydrolysis, once they have been transported inside cells. Shows similar activity on xylans of different rate of arabinose or methylglucuronic substitution. Also displays high activity on aryl-xylosides. Is active on xylotetraose and xylotriose, but does not hydrolyze xylobiose, indicating that XynB is a xylanase and not a beta-xylosidase.2 Publications

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.2 Publications

    Enzyme regulationi

    Completely inhibited by Ag2+, Cu2+, Hg2+, Mn2+, Pb2+ and Sn2+. Strongly inhibited by Fe2+ and Zn2+. Co2+ and Ni2+ cause little inhibition while Ca2+ and Mg2+ do not affect enzyme activity, and Ba2+ produces a small stimulating effect. Irreversibly inactivated by SDS in vitro.1 Publication

    pH dependencei

    Optimum pH is 5.5. Shows more than 75% of maximum activity from pH 5 to 10. Is still active at pH 12.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius. Loses 100% activity after incubation for 15 minutes at 50 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei134 – 1341Proton donorBy similarity
    Active sitei241 – 2411NucleophileBy similarity

    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 B (EC:3.2.1.8)
    Short name:
    Xylanase B
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase B
    Gene namesi
    Name:xynB
    OrganismiPaenibacillus barcinonensis
    Taxonomic identifieri198119 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Is not secreted to the medium but instead remains cell-associated, in the soluble fraction, even in late stationary-phase cultures.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 332331Endo-1,4-beta-xylanase BPRO_0000366196Add
    BLAST

    Structurei

    Secondary structure

    1
    332
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 123
    Turni13 – 153
    Beta strandi17 – 226
    Helixi24 – 3714
    Beta strandi39 – 457
    Helixi49 – 524
    Beta strandi54 – 574
    Helixi62 – 7211
    Turni73 – 753
    Beta strandi77 – 804
    Beta strandi86 – 883
    Helixi91 – 944
    Beta strandi99 – 1013
    Helixi104 – 12118
    Turni122 – 1254
    Beta strandi127 – 1337
    Helixi148 – 1525
    Helixi157 – 16812
    Beta strandi172 – 1809
    Helixi184 – 19916
    Beta strandi206 – 2094
    Beta strandi212 – 2143
    Helixi220 – 23112
    Turni232 – 2343
    Beta strandi236 – 24712
    Helixi261 – 28020
    Turni281 – 2844
    Beta strandi285 – 29410
    Helixi299 – 3013
    Beta strandi302 – 3054
    Beta strandi313 – 3153
    Helixi323 – 3286

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EMCX-ray2.10A2-332[»]
    3EMQX-ray2.73A2-332[»]
    3EMZX-ray2.08A2-332[»]
    ProteinModelPortaliO69231.
    SMRiO69231. Positions 2-330.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO69231.

    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.

    Sequencei

    Sequence statusi: Complete.

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

    O69231-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTEIPSLSA SYANSFKIGA AVHTRMLQTE GEFIAKHYNS VTAENQMKFE    50
    EVHPREHEYT FEAADEIVDF AVARGIGVRG HTLVWHNQTP AWMFEDASGG 100
    TASREMMLSR LKQHIDTVVG RYKDQIYAWD VVNEAIEDKT DLIMRDTKWL 150
    RLLGEDYLVQ AFNMAHEADP NALLFYNDYN ETDPVKREKI YNLVRSLLDQ 200
    GAPVHGIGMQ GHWNIHGPSM DEIRQAIERY ASLDVQLHVT ELDLSVFRHE 250
    DQRTDLTEPT AEMAELQQKR YEDIFGLFRE YRSNITSVTF WGVADNYTWL 300
    DNFPVRGRKN WPFVFDTELQ PKDSFWRIIG QD 332
    Length:332
    Mass (Da):38,561
    Last modified:August 1, 1998 - v1
    Checksum:iDDEF7BCF17C8A72E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006646 Genomic DNA. Translation: CAA07174.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006646 Genomic DNA. Translation: CAA07174.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EMC X-ray 2.10 A 2-332 [» ]
    3EMQ X-ray 2.73 A 2-332 [» ]
    3EMZ X-ray 2.08 A 2-332 [» ]
    ProteinModelPortali O69231.
    SMRi O69231. Positions 2-330.
    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 O69231.

    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.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a Paenibacillus cell-associated xylanase with high activity on aryl-xylosides: a new subclass of family 10 xylanases."
      Gallardo O., Diaz P., Pastor F.I.J.
      Appl. Microbiol. Biotechnol. 61:226-233(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
      Strain: DSM 15478 / CECT 7022 / BP-23.
    2. "Cloning of a Bacillus sp. BP-23 gene encoding a xylanase with high activity against aryl xylosides."
      Blanco A., Diaz P., Martinez J., Lopez O., Soler C., Pastor F.I.J.
      FEMS Microbiol. Lett. 137:285-290(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: DSM 15478 / CECT 7022 / BP-23.

    Entry informationi

    Entry nameiXYNB_PAEBA
    AccessioniPrimary (citable) accession number: O69231
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 3, 2009
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 56 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, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3