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Reviewed, UniProtKB/Swiss-Prot P23030 (XYNB_PSEFL)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismPseudomonas fluorescens
Taxonomic identifier294 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length592 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 – 592555Endo-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

Sequences

Sequence LengthMass (Da)Tools
P23030-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: E081F6308EA2B93A

FASTA59263,411
        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 ITSGICGGQD LDRRLRFDPG QWHTAPGNDV VD 

« Hide

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: 2125205] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-46.
Strain: Sp. Cellulosa.

Cross-references

Sequence databases

X54523 Genomic DNA. Translation: CAA38389.1.

3D structure databases

HSSPHSSP built from PDB template 1EXG based on UniProtKB P07986.
ModBaseSearch...

Protein family/group databases

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

Enzyme and pathway databases

BRENDA3.2.1.8. 329.

Family and domain databases

InterProIPR001919. CBD_bac.
IPR012291. CBD_carb_bd.
IPR018366. CBM2_CS.
IPR005084. CBM_6.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
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]
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_PSEFL
AccessionPrimary (citable) accession number: P23030
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents