Reviewed,
UniProtKB/Swiss-Prot P81536 (XYNA_PAEVA)
Last modified
November 24, 2009.
Version 46.
History...
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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 PVX |
| Organism | Paecilomyces variotii |
| Taxonomic identifier | 45996 [NCBI] |
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Paecilomyces |
Protein attributes
| Sequence length | 194 AA. |
| Sequence status | Complete. |
| 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. |
| Biophysicochemical properties | Temperature dependence: Thermostable. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Xylan degradation |
| Molecular function | Glycosidase Hydrolase |
| PTM | Acetylation Disulfide bond |
| 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 – 194 | 194 | Endo-1,4-beta-xylanase | PRO_0000184069 | |||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||
| Active site | 86 | 1 | Nucleophile By similarity | ||||||||||||||||||||||||||||||||||
| Active site | 178 | 1 | Proton donor By similarity | ||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||
| Modified residue | 1 | 1 | N-acetylglycine | ||||||||||||||||||||||||||||||||||
| Disulfide bond | 110 ↔ 154 | ||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 6 – 10 | 5 | |||||||||||||||||||||||||||||||||||
| Beta strand | 13 – 19 | 7 | |||||||||||||||||||||||||||||||||||
| Beta strand | 25 – 29 | 5 | |||||||||||||||||||||||||||||||||||
| Beta strand | 34 – 39 | 6 | |||||||||||||||||||||||||||||||||||
| Beta strand | 41 – 53 | 13 | |||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 81 | 23 | |||||||||||||||||||||||||||||||||||
| Turn | 82 – 84 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 85 – 96 | 12 | |||||||||||||||||||||||||||||||||||
| Turn | 98 – 101 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 102 – 110 | 9 | |||||||||||||||||||||||||||||||||||
| Beta strand | 113 – 127 | 15 | |||||||||||||||||||||||||||||||||||
| Beta strand | 130 – 143 | 14 | |||||||||||||||||||||||||||||||||||
| Beta strand | 146 – 151 | 6 | |||||||||||||||||||||||||||||||||||
| Helix | 152 – 161 | 10 | |||||||||||||||||||||||||||||||||||
| Beta strand | 168 – 182 | 15 | |||||||||||||||||||||||||||||||||||
| Beta strand | 184 – 192 | 9 | |||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
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 |
| ||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | GH11. Glycoside Hydrolase Family 11. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.2.1.8. 353. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR008985. ConA-like_lec_gl. 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 | XYNA_PAEVA | ||||||||
| Accession | Primary (citable) accession number: P81536 | ||||||||
| 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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