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P23030

- XYNB_CELJU

UniProt

P23030 - XYNB_CELJU

Protein

Endo-1,4-beta-xylanase B

Gene

xynB

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (20 Apr 2010)
      Previous versions | rss
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    Functioni

    Xylanase B contributes to hydrolyze hemicellulose, the major component of plant cell-walls.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei431 – 4311Proton donorBy similarity
    Active sitei530 – 5301NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW
    2. xylan catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BioCyciCJAP498211:GHIT-3269-MONOMER.
    UniPathwayiUPA00697.

    Protein family/group databases

    CAZyiCBM2. Carbohydrate-Binding Module Family 2.
    CBM35. Carbohydrate-Binding Module Family 35.
    GH10. 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
    Synonyms:xyn10B
    Ordered Locus Names:CJA_3280
    OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
    Taxonomic identifieri498211 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
    ProteomesiUP000001036: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 37371 PublicationAdd
    BLAST
    Chaini38 – 599562Endo-1,4-beta-xylanase BPRO_0000007978Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi39 ↔ 133By similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi498211.CJA_3280.

    Structurei

    3D structure databases

    ProteinModelPortaliP23030.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 13699CBM2Add
    BLAST
    Domaini163 – 289127CBM6PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi135 – 16228Ser-rich (linker)Add
    BLAST
    Compositional biasi300 – 32021Ser-rich (linker)Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OrthoDBiEOG6BPDFR.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR018366. CBM2_CS.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR005084. CMB_fam6.
    IPR008979. Galactose-bd-like.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00553. CBM_2. 1 hit.
    PF03422. CBM_6. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00637. CBD_II. 1 hit.
    SM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS51173. CBM2. 1 hit.
    PS00561. CBM2_A. 1 hit.
    PS51175. CBM6. 1 hit.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23030-1 [UniParc]FASTAAdd to Basket

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    MTISASDYRH PGNFLKRTTA LLCVGTALTA LAFNASAACT YTIDSEWSTG    50
    FTANITLKND TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW 100
    NGSIAPGQSI SFGLQGEKNG STAERPTVTG AACNSATTSS VASSSSTPTT 150
    SSSSASSVAS ALLLQEAQAG FCRVDGTIDN NHTGFTGSGF ANTNNAQGAA 200
    VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN YTVSLPTTGA 250
    WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS 300
    VSSSSSVQSS SSSSSSSAAS AKKFIGNITT SGAVRSDFTR YWNQITPENE 350
    SKWGSVEGTR NVYNWAPLDR IYAYARQNNI PVKAHTFVWG AQSPSWLNNL 400
    SGPEVAVEIE QWIRDYCARY PDTAMIDVVN EAVPGHQPAG YAQRAFGNNW 450
    IQRVFQLARQ YCPNSILILN DYNNIRWQHN EFIALAKAQG NYIDAVGLQA 500
    HELKGMTAAQ VKTAIDNIWN QVGKPIYISE YDIGDTNDQV QLQNFQAHFP 550
    VFYNHPHVHG ITLWGYVVGR TWIEGSGLIQ DNGTPRPAMT WLINNYLNQ 599
    Length:599
    Mass (Da):64,363
    Last modified:April 20, 2010 - v2
    Checksum:iD2DE51E5FD4B33E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti563 – 59836LWGYV…NNYLN → SGICGGQDLDRRLRFDPGQW HTAPGNDVVD in CAA38389. (PubMed:2125205)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54523 Genomic DNA. Translation: CAA38389.1.
    CP000934 Genomic DNA. Translation: ACE84499.1.
    RefSeqiYP_001983734.1. NC_010995.1.

    Genome annotation databases

    EnsemblBacteriaiACE84499; ACE84499; CJA_3280.
    GeneIDi6416364.
    KEGGicja:CJA_3280.
    PATRICi21329951. VBICelJap122165_3240.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54523 Genomic DNA. Translation: CAA38389.1 .
    CP000934 Genomic DNA. Translation: ACE84499.1 .
    RefSeqi YP_001983734.1. NC_010995.1.

    3D structure databases

    ProteinModelPortali P23030.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 498211.CJA_3280.

    Protein family/group databases

    CAZyi CBM2. Carbohydrate-Binding Module Family 2.
    CBM35. Carbohydrate-Binding Module Family 35.
    GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACE84499 ; ACE84499 ; CJA_3280 .
    GeneIDi 6416364.
    KEGGi cja:CJA_3280.
    PATRICi 21329951. VBICelJap122165_3240.

    Phylogenomic databases

    OrthoDBi EOG6BPDFR.

    Enzyme and pathway databases

    UniPathwayi UPA00697 .
    BioCyci CJAP498211:GHIT-3269-MONOMER.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR018366. CBM2_CS.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR005084. CMB_fam6.
    IPR008979. Galactose-bd-like.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00553. CBM_2. 1 hit.
    PF03422. CBM_6. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00637. CBD_II. 1 hit.
    SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS51173. CBM2. 1 hit.
    PS00561. CBM2_A. 1 hit.
    PS51175. CBM6. 1 hit.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose-binding domains and are encoded by adjacent genes."
      Kellett L.E., Poole D.M., Ferreira L.M.A., Durrant A.J., Hazlewood G.P., Gilbert H.J.
      Biochem. J. 272:369-376(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-46.
    2. "Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
      DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
      J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ueda107.

    Entry informationi

    Entry nameiXYNB_CELJU
    AccessioniPrimary (citable) accession number: P23030
    Secondary accession number(s): B3PEH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 99 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

    Complete proteome, Direct protein sequencing, Reference proteome

    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