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Reviewed, UniProtKB/Swiss-Prot O69231 (XYNB_PAEBA)

Last modified June 16, 2009. Version 37. 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
OrganismPaenibacillus barcinonensis
Taxonomic identifier198119 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. Ref.1 Ref.2

Catalytic activity

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

Enzyme regulation

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. Ref.2

Pathway

Glycan degradation; xylan degradation.

Subcellular location

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

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. Shows more than 75% of maximum activity from pH 5 to 10. Is still active at pH 12.

Temperature dependence:

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

Ontologies

Keywords
   Biological processXylan degradation
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

endo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 332331Endo-1,4-beta-xylanase B
PRO_0000366196

Sites

Active site1341Proton donor By similarity
Active site2411Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
O69231-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: DDEF7BCF17C8A72E

FASTA33238,561
        10         20         30         40         50         60 
MSTEIPSLSA SYANSFKIGA AVHTRMLQTE GEFIAKHYNS VTAENQMKFE EVHPREHEYT 

        70         80         90        100        110        120 
FEAADEIVDF AVARGIGVRG HTLVWHNQTP AWMFEDASGG TASREMMLSR LKQHIDTVVG 

       130        140        150        160        170        180 
RYKDQIYAWD VVNEAIEDKT DLIMRDTKWL RLLGEDYLVQ AFNMAHEADP NALLFYNDYN 

       190        200        210        220        230        240 
ETDPVKREKI YNLVRSLLDQ GAPVHGIGMQ GHWNIHGPSM DEIRQAIERY ASLDVQLHVT 

       250        260        270        280        290        300 
ELDLSVFRHE DQRTDLTEPT AEMAELQQKR YEDIFGLFRE YRSNITSVTF WGVADNYTWL 

       310        320        330 
DNFPVRGRKN WPFVFDTELQ PKDSFWRIIG QD 

« Hide

References

[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: 12698280] [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: 8998999] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: DSM 15478 / CECT 7022 / BP-23.

Cross-references

Sequence databases

AJ006646 Genomic DNA. Translation: CAA07174.1.

3D structure databases

HSSPHSSP built from PDB template 1HIZ based on UniProtKB P40943.
ModBaseSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.

Family and domain databases

InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
PROSITEPS00591. GLYCOSYL_HYDROL_F10. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNB_PAEBA
AccessionPrimary (citable) accession number: O69231
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 37 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