C5J411 (XYNC_ASPNG) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 21.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable endo-1,4-beta-xylanase C Short name=Xylanase C EC=3.2.1.8 Alternative name(s): 1,4-beta-D-xylan xylanohydrolase C | ||
| Gene names |
| ||
| Organism | Aspergillus niger | ||
| Taxonomic identifier | 5061 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus![]() |
Protein attributes
| Sequence length | 327 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose By similarity. |
| Catalytic activity | Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. |
| Pathway | |
| Subcellular location | Secreted By similarity. |
| Induction | Expressed in presence of xylan and repressed by glucose. |
| Sequence similarities | Belongs to the glycosyl hydrolase 10 (cellulase F) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Xylan degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond |
| Gene Ontology (GO) | |
| Biological_process | xylan catabolic process Inferred from sequence or structural similarity. Source: UniProtKB |
| Cellular_component | extracellular region Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | endo-1,4-beta-xylanase activity Inferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Potential | ||||||||
| Chain | 20 – 327 | 308 | Probable endo-1,4-beta-xylanase C | PRO_0000393190 | |||||||
Sites | |||||||||||
| Active site | 157 | 1 | Proton donor By similarity | ||||||||
| Active site | 263 | 1 | Nucleophile By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 281 ↔ 287 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 11 – 13 | 3 | MLF → KLI in ACR83565. Ref.1 | ||||||||
| Sequence conflict | 23 | 1 | D → E in ACR83565. Ref.1 | ||||||||
| Sequence conflict | 77 | 1 | W → R in ACR83565. Ref.1 | ||||||||
| Sequence conflict | 123 | 1 | S → A in ACR83565. Ref.1 | ||||||||
| Sequence conflict | 132 | 1 | E → G in ACR83565. Ref.1 | ||||||||
| Sequence conflict | 208 | 1 | S → P in ACR83565. Ref.1 | ||||||||
| Sequence conflict | 268 | 1 | G → D in ACR83565. Ref.1 | ||||||||
| Sequence conflict | 283 | 1 | N → D in ACR83565. Ref.1 | ||||||||
| Sequence conflict | 321 – 323 | 3 | DAI → FAV in ACR83565. Ref.1 | ||||||||
Sequences
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References
| [1] | "Gene cloning, sequencing, expression and characterization of a xylanase A gene from Aspergillus niger DMS1957." Nguyen S.L.T., Quyen D.T. Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: DMS1957. |
| [2] | Huang J.Z., Xu Y., Tian B.Y., Huang Q.G. Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: IME-216. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FJ986225 mRNA. Translation: ACR83565.1. EU848304 mRNA. Translation: ACJ26381.1. |
3D structure databases | |
| ProteinModelPortal | C5J411. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | COG3693. |
Enzyme and pathway databases | |
| UniPathway | UPA00114. |
Family and domain databases | |
| Gene3D | 3.20.20.80. 1 hit. |
| InterPro | IPR001000. Glyco_hydro_10. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Pfam | PF00331. Glyco_hydro_10. 1 hit. [Graphical view] |
| PRINTS | PR00134. GLHYDRLASE10. |
| SMART | SM00633. Glyco_10. 1 hit. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| PROSITE | PS00591. GLYCOSYL_HYDROL_F10. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | XYNC_ASPNG | ||||||||
| Accession | Primary (citable) accession number: C5J411 Secondary accession number(s): C6F1T1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
