Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23030 (XYNB_CELJU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase B

Short name=Xylanase B
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B
Gene names
Name:xynB
Synonyms:xyn10B
Ordered Locus Names:CJA_3280
OrganismCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP]
Taxonomic identifier498211 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Glycan metabolism; hemicellulose degradation.

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Contains 1 CBM2 (carbohydrate binding type-2) domain.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Ref.1
Chain38 – 599562Endo-1,4-beta-xylanase B
PRO_0000007978

Regions

Domain38 – 13699CBM2
Domain163 – 289127CBM6
Compositional bias135 – 16228Ser-rich (linker)
Compositional bias300 – 32021Ser-rich (linker)

Sites

Active site4311Proton donor By similarity
Active site5301Nucleophile By similarity

Amino acid modifications

Disulfide bond39 ↔ 133 By similarity

Experimental info

Sequence conflict563 – 59836LWGYV…NNYLN → SGICGGQDLDRRLRFDPGQW HTAPGNDVVD in CAA38389. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23030 [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: D2DE51E5FD4B33E5

FASTA59964,363
        10         20         30         40         50         60 
MTISASDYRH PGNFLKRTTA LLCVGTALTA LAFNASAACT YTIDSEWSTG FTANITLKND 

        70         80         90        100        110        120 
TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW NGSIAPGQSI SFGLQGEKNG 

       130        140        150        160        170        180 
STAERPTVTG AACNSATTSS VASSSSTPTT SSSSASSVAS ALLLQEAQAG FCRVDGTIDN 

       190        200        210        220        230        240 
NHTGFTGSGF ANTNNAQGAA VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN 

       250        260        270        280        290        300 
YTVSLPTTGA WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS 

       310        320        330        340        350        360 
VSSSSSVQSS SSSSSSSAAS AKKFIGNITT SGAVRSDFTR YWNQITPENE SKWGSVEGTR 

       370        380        390        400        410        420 
NVYNWAPLDR IYAYARQNNI PVKAHTFVWG AQSPSWLNNL SGPEVAVEIE QWIRDYCARY 

       430        440        450        460        470        480 
PDTAMIDVVN EAVPGHQPAG YAQRAFGNNW IQRVFQLARQ YCPNSILILN DYNNIRWQHN 

       490        500        510        520        530        540 
EFIALAKAQG NYIDAVGLQA HELKGMTAAQ VKTAIDNIWN QVGKPIYISE YDIGDTNDQV 

       550        560        570        580        590 
QLQNFQAHFP VFYNHPHVHG ITLWGYVVGR TWIEGSGLIQ DNGTPRPAMT WLINNYLNQ 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54523 Genomic DNA. Translation: CAA38389.1.
CP000934 Genomic DNA. Translation: ACE84499.1.
RefSeqYP_001983734.1. NC_010995.1.

3D structure databases

ProteinModelPortalP23030.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING498211.CJA_3280.

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
CBM35. Carbohydrate-Binding Module Family 35.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE84499; ACE84499; CJA_3280.
GeneID6416364.
KEGGcja:CJA_3280.
PATRIC21329951. VBICelJap122165_3240.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OrthoDBEOG6BPDFR.
ProtClustDBCLSK2544271.

Enzyme and pathway databases

BioCycCJAP498211:GHIT-3269-MONOMER.
UniPathwayUPA00697.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008965. 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]
PfamPF00553. CBM_2. 1 hit.
PF03422. CBM_6. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51175. CBM6. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNB_CELJU
AccessionPrimary (citable) accession number: P23030
Secondary accession number(s): B3PEH8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 20, 2010
Last modified: November 13, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries