Reviewed,
UniProtKB/Swiss-Prot P33557 (XYN3_ASPKA)
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 3 Short name=Xylanase 3 EC=3.2.1.8 Alternative name(s): 1,4-beta-D-xylan xylanohydrolase 3 Xylanase C | ||
| Gene names |
| ||
| Organism | Aspergillus kawachi (Aspergillus awamori var. kawachi) | ||
| Taxonomic identifier | 40384 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 211 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 | |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 11 (cellulase G) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Xylan degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 – 27 | 27 | Ref.1 | |||||||||||||||||||||||||||||||||
| Chain | 28 – 211 | 184 | Endo-1,4-beta-xylanase 3 | PRO_0000007991 | ||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||
| Active site | 106 | 1 | Nucleophile By similarity | |||||||||||||||||||||||||||||||||
| Active site | 197 | 1 | Proton donor | |||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||
| Disulfide bond | 119 ↔ 138 | |||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||
| Beta strand | 33 – 38 | 6 | ||||||||||||||||||||||||||||||||||
| Helix | 39 – 41 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 42 – 47 | 6 | ||||||||||||||||||||||||||||||||||
| Helix | 48 – 50 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 52 – 63 | 12 | ||||||||||||||||||||||||||||||||||
| Beta strand | 65 – 73 | 9 | ||||||||||||||||||||||||||||||||||
| Beta strand | 79 – 86 | 8 | ||||||||||||||||||||||||||||||||||
| Beta strand | 90 – 100 | 11 | ||||||||||||||||||||||||||||||||||
| Turn | 101 – 104 | 4 | ||||||||||||||||||||||||||||||||||
| Beta strand | 105 – 115 | 11 | ||||||||||||||||||||||||||||||||||
| Turn | 118 – 121 | 4 | ||||||||||||||||||||||||||||||||||
| Beta strand | 122 – 130 | 9 | ||||||||||||||||||||||||||||||||||
| Beta strand | 133 – 147 | 15 | ||||||||||||||||||||||||||||||||||
| Beta strand | 150 – 163 | 14 | ||||||||||||||||||||||||||||||||||
| Beta strand | 166 – 170 | 5 | ||||||||||||||||||||||||||||||||||
| Helix | 172 – 179 | 8 | ||||||||||||||||||||||||||||||||||
| Helix | 180 – 182 | 3 | ||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and sequencing of the xynC gene encoding acid xylanase of Aspergillus kawachii." Ito K., Iwashita K., Iwano K. Biosci. Biotechnol. Biochem. 56:1338-1340(1992) [PubMed: 1368843] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-34. Strain: IFO 4308. |
| [2] | "Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp-37 for catalysis at low pH." Fushinobu S., Ito K., Konno M., Wakagi T., Matsuzawa H. Protein Eng. 11:1121-1128(1998) [PubMed: 9930661] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-210. Strain: IFO 4308. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| S45138 Genomic DNA. Translation: AAC60542.1. D14848 Genomic DNA. Translation: BAA03576.1. | |||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | GH11. Glycoside Hydrolase Family 11. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.2.1.8. 279687. | ||||||||||||
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 | XYN3_ASPKA | ||||||||
| Accession | Primary (citable) accession number: P33557 | ||||||||
| 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 |

Clusters with


