Q5B9Z8 (AXHA1_EMENI) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 39.
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 alpha-L-arabinofuranosidase axhA-1 EC=3.2.1.55 Alternative name(s): Arabinoxylan arabinofuranohydrolase axhA-1 | ||||
| Gene names |
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| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome] | ||||
| Taxonomic identifier | 227321 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella › ![]() |
Protein attributes
| Sequence length | 327 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Alpha-L-arabinofuranosidase 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. Releases L-arabinose from arabinoxylan By similarity. |
| Catalytic activity | Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 62 family. |
| Sequence caution | The sequence CBF84318.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAA62979.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Xylan degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | L-arabinose metabolic process Inferred from electronic annotation. Source: InterPro xylan catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | alpha-N-arabinofuranosidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AACD01000045 Genomic DNA. Translation: EAA62979.1. Sequence problems. BN001306 Genomic DNA. Translation: CBF84318.1. Sequence problems. |
| RefSeq | XP_660236.1. XM_655144.1. |
3D structure databases | |
| ProteinModelPortal | Q5B9Z8. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | CADANIAT00010488; CADANIAP00010488; CADANIAG00010488. |
| GeneID | 2874537. |
| KEGG | ani:AN2632.2. |
Phylogenomic databases | |
| eggNOG | NOG81570. |
| HOGENOM | HOG000164911. |
| OrthoDB | EOG4XH383. |
Family and domain databases | |
| InterPro | IPR005193. GH62_arabinosidase. IPR023296. Glyco_hydro_beta-prop. [Graphical view] |
| Pfam | PF03664. Glyco_hydro_62. 1 hit. [Graphical view] |
| SUPFAM | SSF75005. Glyco_hydro_43_beta-prop. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | AXHA1_EMENI | ||||||||
| Accession | Primary (citable) accession number: Q5B9Z8 Secondary accession number(s): C8VHH2 | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with
