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Beta-xylosidase/alpha-L-arabinofuranosidase 1



Medicago sativa (Alfalfa)
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli


A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo-enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls (By similarity).By similarity

Catalytic activityi

Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.By similarity
Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.By similarity

GO - Molecular functioni

GO - Biological processi


Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-xylosidase/alpha-L-arabinofuranosidase 11 Publication
Alternative name(s):
Xylan 1,4-beta-xylosidase/Alpha-L-arabinofuranosidase 1
Including the following 2 domains:
Alternative name(s):
1,4-beta-D-xylan xylohydrolaseBy similarity
Xylan 1,4-beta-xylosidase
Alpha-L-arabinofuranosidase (EC:
Short name:
ArabinosidaseBy similarity
Gene namesi
Name:Xyl11 Publication
OrganismiMedicago sativa (Alfalfa)
Taxonomic identifieri3879 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000392639‹1 – ›45Beta-xylosidase/alpha-L-arabinofuranosidase 1Add BLAST›45


Tissue specificityi

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.1 Publication

Family & Domainsi

Sequence similaritiesi

Belongs to the glycoside hydrolase 3 family.Sequence analysis


Sequence statusi: Fragments.

P86450-1 [UniParc]FASTAAdd to basket

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        10         20         30         40 
Mass (Da):4,785
Last modified:March 23, 2010 - v1

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11 Publication1
Non-adjacent residuesi15 – 161 Publication2
Non-adjacent residuesi30 – 311 Publication2
Non-terminal residuei451 Publication1

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiXYL1_MEDSA
AccessioniPrimary (citable) accession number: P86450
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: January 7, 2015
This is version 11 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program


Keywords - Technical termi

Direct protein sequencing, Multifunctional enzyme


  1. SIMILARITY comments
    Index of protein domains and families