Reviewed,
UniProtKB/Swiss-Prot P48793 (XYN_TRIHA)
Last modified
June 16, 2009.
Version 56.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Endo-1,4-beta-xylanase Short name=Xylanase EC=3.2.1.8 Alternative name(s): 1,4-beta-D-xylan xylanohydrolase |
| Organism | Trichoderma harzianum (Hypocrea lixii) |
| Taxonomic identifier | 5544 [NCBI] |
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea |
Protein attributes
| Sequence length | 190 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. |
| Pathway | |
| Sequence similarities | Belongs to the glycosyl hydrolase 11 (cellulase G) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Xylan degradation |
| Molecular function | Glycosidase Hydrolase |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 190 | 190 | Endo-1,4-beta-xylanase | PRO_0000184072 | ||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||
| Active site | 86 | 1 | Nucleophile | |||||||||||||||||||||||||||||||||||
| Active site | 177 | 1 | Proton donor | |||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 5 – 12 | 8 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 14 – 19 | 6 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 25 – 29 | 5 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 34 – 41 | 8 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 44 – 53 | 10 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 81 | 23 | ||||||||||||||||||||||||||||||||||||
| Turn | 82 – 84 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 85 – 93 | 9 | ||||||||||||||||||||||||||||||||||||
| Turn | 98 – 101 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 103 – 110 | 8 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 113 – 125 | 13 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 130 – 143 | 14 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 146 – 151 | 6 | ||||||||||||||||||||||||||||||||||||
| Helix | 152 – 161 | 10 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 168 – 180 | 13 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 182 – 189 | 8 | ||||||||||||||||||||||||||||||||||||
Sequences
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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 | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | A44593. | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | GH11. Glycoside Hydrolase Family 11. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.2.1.8. 3745. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12_cat. IPR018208. Glyco_hydro_11_AS. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit. | ||||||||||||
| Pfam | PF00457. Glyco_hydro_11. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00911. GLHYDRLASE11. | ||||||||||||
| PROSITE | PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | XYN_TRIHA | ||||||||
| Accession | Primary (citable) accession number: P48793 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (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 |

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