P86450 (XYL1_MEDSA) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 15, 2010.
Version 3.
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: Beta-xylosidase/alpha-L-arabinofuranosidase 1 Alternative name(s): Xylan 1,4-beta-xylosidase/Alpha-N-arabinofuranosidase 1 Including the following 2 domains:
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| Gene names |
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| Organism | Medicago sativa (Alfalfa) | ||
| Taxonomic identifier | 3879 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago![]() |
Protein attributes
| Sequence length | 45 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo-enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls By similarity. UniProtKB A5JTQ2 |
| Catalytic activity | Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini. UniProtKB A5JTQ2 Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. UniProtKB A5JTQ2 |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity UniProtKB Q9FLG1. |
| Tissue specificity | Strongly expressed in young roots, significantly reduced expression in older roots. Highest expression levels seen in root tips, some expression seen in root nodules and in the flowers, but not seen in other aerial parts of the plant such as in the stems, hypocotyls or leaves. Ref.1 |
| Sequence similarities | Belongs to the glycoside hydrolase 3 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Xylan degradation |
| Cellular component | Extracellular matrix Secreted |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Direct protein sequencing Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological_process | xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | alpha-N-arabinofuranosidase activity Inferred from electronic annotation. Source: EC xylan 1,4-beta-xylosidase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Molecular cloning of a bifunctional beta-xylosidase/alpha-L-arabinosidase from alfalfa roots: heterologous expression in Medicago truncatula and substrate specificity of the purified enzyme." Xiong J.S., Balland-Vanney M., Xie Z.P., Schultze M., Kondorosi A., Kondorosi E., Staehelin C. J. Exp. Bot. 58:2799-2810(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, TISSUE SPECIFICITY. Strain: cv. Sitel. Tissue: Root nodule. |
Cross-references
3D structure databases | |
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| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| PROSITE | PS00775. GLYCOSYL_HYDROL_F3. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | XYL1_MEDSA | ||||||||
| Accession | Primary (citable) accession number: P86450 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
