Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P81536 (XYNA_PAEVA)

Last modified November 24, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
      Short name=Xylanase
    EC=3.2.1.8
Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase
    PVX
OrganismPaecilomyces variotii
Taxonomic identifier45996 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaePaecilomyces

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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.

Biophysicochemical properties

Temperature dependence:

Thermostable.

Ontologies

Keywords
   Biological processXylan degradation
   Molecular functionGlycosidase
Hydrolase
   PTMAcetylation
Disulfide bond
   Technical term3D-structure
Direct protein sequencing
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

Chain1 – 194194Endo-1,4-beta-xylanase
PRO_0000184069

Sites

Active site861Nucleophile By similarity
Active site1781Proton donor By similarity

Amino acid modifications

Modified residue11N-acetylglycine
Disulfide bond110 ↔ 154

Secondary structure

............................. 194
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81536-1 [UniParc].

Last modified June 1, 2000. Version 1.
Checksum: 1D5C50AA4F6EDB90

FASTA19420,947
        10         20         30         40         50         60 
GTTPNSEGWH DGYYYSWWSD GGGDSTYTNN SGGTYEITWG NGGNLVGGKG WNPGLNARAI 

        70         80         90        100        110        120 
HFTGVYQPNG TSYLSVYGWT RNPLVEYYIV ENFGSSNPSS GSTDLGTVSC DGSTYTLGQS 

       130        140        150        160        170        180 
TRYNAPSIDG TQTFNQYWSV RQDKRSSGTV QTGCHFDAWA SAGLNVTGDH YYQIVATEGY 

       190 
FSSGYARITV ADVG 

« Hide

References

[1]"The tertiary structure at 1.59 A resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces varioti bainier."
Kumar P.R., Eswaramoorthy S., Vithayathil P.J., Viswamitra M.A.
J. Mol. Biol. 295:581-593(2000) [PubMed: 10623548] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS), PROTEIN SEQUENCE OF 50-58 AND 123-128.
Strain: Bainier.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PVXX-ray1.59A1-194[»]
ModBaseSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Enzyme and pathway databases

BRENDA3.2.1.8. 353.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR001137. 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 nameXYNA_PAEVA
AccessionPrimary (citable) accession number: P81536
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2000
Last modified: November 24, 2009
This is version 46 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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