Reviewed,
UniProtKB/Swiss-Prot P36218 (XYN1_TRIRE)
Last modified
June 16, 2009.
Version 67.
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 1 Short name=Xylanase 1 EC=3.2.1.8 Alternative name(s): 1,4-beta-D-xylan xylanohydrolase 1 | ||
| Gene names |
| ||
| Organism | Trichoderma reesei (Hypocrea jecorina) | ||
| Taxonomic identifier | 51453 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea |
Protein attributes
| Sequence length | 229 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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 |
| Domain | Signal |
| 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 | |||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 51 | 51 | Potential | ||||||||||||||||||||||||||||||
| Chain | 52 – 229 | 178 | Endo-1,4-beta-xylanase 1 | PRO_0000008013 | |||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||
| Active site | 126 | 1 | Nucleophile By similarity | ||||||||||||||||||||||||||||||
| Active site | 215 | 1 | Proton donor By similarity | ||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||
| Beta strand | 56 – 61 | 6 | |||||||||||||||||||||||||||||||
| Beta strand | 63 – 70 | 8 | |||||||||||||||||||||||||||||||
| Beta strand | 72 – 83 | 12 | |||||||||||||||||||||||||||||||
| Beta strand | 85 – 93 | 9 | |||||||||||||||||||||||||||||||
| Beta strand | 99 – 121 | 23 | |||||||||||||||||||||||||||||||
| Turn | 122 – 124 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 125 – 135 | 11 | |||||||||||||||||||||||||||||||
| Beta strand | 140 – 148 | 9 | |||||||||||||||||||||||||||||||
| Beta strand | 151 – 165 | 15 | |||||||||||||||||||||||||||||||
| Beta strand | 168 – 181 | 14 | |||||||||||||||||||||||||||||||
| Beta strand | 184 – 188 | 5 | |||||||||||||||||||||||||||||||
| Helix | 190 – 199 | 10 | |||||||||||||||||||||||||||||||
| Beta strand | 206 – 228 | 23 | |||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The two major xylanases from Trichoderma reesei: characterization of both enzymes and genes." Toerroenen A., Mach R.L., Messner R., Gonzalez R., Kalkkinen N., Harkki A., Kubicek C.P. Biotechnology (N.Y.) 10:1461-1465(1992) [PubMed: 1369024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: QM9414 / Rut C-30. |
| [2] | "Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei." Toerroenen A., Rouvinen J. Biochemistry 34:847-856(1995) [PubMed: 7827044] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X69574 Genomic DNA. Translation: CAA49294.1. | |||||||||||||
| PIR | S39155. | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | GH11. Glycoside Hydrolase Family 11. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.2.1.8. 280374. | ||||||||||||
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 | XYN1_TRIRE | ||||||||
| Accession | Primary (citable) accession number: P36218 | ||||||||
| 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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