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Reviewed, UniProtKB/Swiss-Prot P55333 (XYNB_EMENI)

Last modified September 22, 2009. Version 56. 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
    24 kDa xylanase
    Xylanase X24
Gene names
Name: xlnB
ORF Names: AN9365
OrganismEmericella nidulans (Aspergillus nidulans) [Complete proteome]
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Ontologies

Keywords
   Biological processXylan degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionendo-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

Signal peptide1 – 1818 Potential
Chain19 – 221203Endo-1,4-beta-xylanase B
PRO_0000008005

Sites

Active site1171Nucleophile By similarity
Active site2081Proton donor By similarity

Experimental info

Sequence conflict731N → K in CAA90074. Ref.1
Sequence conflict981N → I in CAA90074. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P55333-1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: B762F0BB4B3F77C3

FASTA22123,504
        10         20         30         40         50         60 
MVSFSSLLLA CSAVTAFAAP SDQSIAERSL SERSTPSSTG TSGGYYYSFW TDGGGDVTYT 

        70         80         90        100        110        120 
NGDGGSYTVE WTNVGNFVGG KGWNPGSSQT ISYSGSFNPS GNGYLSVYGW TQNPLIEYYI 

       130        140        150        160        170        180 
VESYGDYNPG TAGTHQGTLE SDGSTYDIYT ATRENAPSIE GTATFTQFWS VRQSKRTSGS 

       190        200        210        220 
VTTQNHFDAW SQLGMTLGTH NYQIVAVEGY QSSGSASITV S 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression in Saccharomyces cerevisiae of two Aspergillus nidulans xylanase genes."
Perez-Gonzalez J.A., de Graaff L.H., Visser J., Ramon D.
Appl. Environ. Microbiol. 62:2179-2182(1996) [PubMed: 8787417] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC 4.

Cross-references

Sequence databases

Z49893 Genomic DNA. Translation: CAA90074.1.
AACD01000172 Genomic DNA. Translation: EAA66432.1.
PIRS57469.
RefSeqXP_682634.1.

3D structure databases

HSSPHSSP built from PDB template 1XND based on UniProtKB P48793.
ModBaseSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Genome annotation databases

GeneID2867930.
KEGGani:AN9365.2.

Enzyme and pathway databases

BRENDA3.2.1.8. 3859.

Family and domain databases

InterProIPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
Gene3DG3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNB_EMENI
AccessionPrimary (citable) accession number: P55333
Secondary accession number(s): Q00176, Q5AQR5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: September 22, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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