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Reviewed, UniProtKB/Swiss-Prot P55329 (XYN1_ASPNG)

Last modified June 16, 2009. Version 63. 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

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Names and origin

Protein namesRecommended name:
    Endo-1,4-beta-xylanase I
      Short name=Xylanase I
    EC=3.2.1.8
Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase I
Gene names
Name: xynA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

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Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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

pH dependence:

Optimum pH is 3.0.

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Ontologies

Keywords
   Biological processXylan degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 211184Endo-1,4-beta-xylanase I
PRO_0000007992

Sites

Active site1061Nucleophile
Active site1971Proton donor

Amino acid modifications

Disulfide bond119 ↔ 138

Secondary structure

1 ............................ 211
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P55329-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 82BEBEE12ED79303

FASTA21122,642
        10         20         30         40         50         60 
MKVTAAFAGL LVTAFAAPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG 

        70         80         90        100        110        120 
VSSDFVVGLG WTTGSSKAIT YSAEYSASGS SSYLAVYGWV NYPQAEYYIV EDYGDYNPCS 

       130        140        150        160        170        180 
SATSLGTVYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVANHFNFWA 

       190        200        210 
QHGFGNSDFN YQVMAVEAWS GAGSASVTIS S

« Hide

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References

[1]"Xylanase production."
Hessing J.G.M., van Gorcom R.F.M., Verbakel J.M.A., Roza M., Maat J.
Patent number WO9119782, 26-DEC-1991
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus niger: molecular basis for its low pH optimum."
Krengel U., Dijkstra B.W.
J. Mol. Biol. 263:70-78(1996) [PubMed: 8890913] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

A19535 Unassigned DNA. Translation: CAA01470.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1T6GX-ray1.80C/D28-211[»]
1UKRX-ray2.40A/B/C/D28-211[»]
2QZ2X-ray2.80A28-211[»]
ModBaseSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Enzyme and pathway databases

BRENDA3.2.1.8. 277.

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...

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Entry information

Entry nameXYN1_ASPNG
AccessionPrimary (citable) accession number: P55329
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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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