Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P48793 (XYN_TRIHA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismTrichoderma harzianum (Hypocrea lixii)
Taxonomic identifier5544 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Protein attributes

Sequence length190 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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190Endo-1,4-beta-xylanase
PRO_0000184072

Sites

Active site861Nucleophile
Active site1771Proton donor

Secondary structure

.............................. 190
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P48793 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 6A0F4D1C3599C698

FASTA19020,703
        10         20         30         40         50         60 
QTIGPGTGYS NGYYYSYWND GHAGVTYTNG GGGSFTVNWS NSGNFVAGKG WQPGTKNKVI 

        70         80         90        100        110        120 
NFSGSYNPNG NSYLSIYGWS RNPLIEYYIV ENFGTYNPST GATKLGEVTS DGSVYDIYRT 

       130        140        150        160        170        180 
QRVNQPSIIG TATFYQYWSV RRNHRSSGSV NTANHFNAWA SHGLTLGTMD YQIVAVEGYF 

       190 
SSGSASITVS 

« Hide

References

[1]"The amino acid sequence of the 20 Kd xylanase from Trichoderma harzianum E58."
Yaguchi M., Roy C., Watson D.C., Rollin F., Tan L.U.L., Senior D.J., Saddler J.N.
(In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J. (eds.); Xylans and xylanases, pp.435-438, Elsevier, Amsterdam (1992)
Cited for: PROTEIN SEQUENCE.
Strain: E58.
[2]"High-resolution structures of xylanases from B.circulans and T.harzianum identify a new folding pattern and implications for the atomic basis of the catalysis."
Campbell R.L., Rose D.R., Wakarchuk W.W., To R.J., Sung W., Yaguchi M.
(In) Suominen P., Reinikainen T. (eds.); Trichoderma reesei cellulases and other hydrolases, pp.63-72, Foundation for Biotechnical and Industrial Fermentation Research, Helsinki (1993)
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

PIRA44593.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XNDX-ray2.00A1-190[»]
ProteinModelPortalP48793.
SMRP48793. Positions 1-190.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11A_TRIHA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP48793.

Entry information

Entry nameXYN_TRIHA
AccessionPrimary (citable) accession number: P48793
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 13, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries