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Protein

Beta-xylosidase/alpha-L-arabinofuranosidase 1

Gene

Xyl1

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

Functioni

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

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate 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:3.2.1.55)
Short name:
ArabinosidaseBy similarity
Gene namesi
Name:Xyl11 Publication
OrganismiMedicago sativa (Alfalfa)
Taxonomic identifieri3879 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›45›45Beta-xylosidase/alpha-L-arabinofuranosidase 1PRO_0000392639Add
BLAST

Expressioni

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

Sequencei

Sequence statusi: Fragments.

P86450-1 [UniParc]FASTAAdd to basket

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        10         20         30         40 
GVQRYTFDAV VSQQDTILSG LDLDCGSYLG YTSPLQGLTA FVPTS
Length:45
Mass (Da):4,785
Last modified:March 23, 2010 - v1
Checksum:i83339885B81AEA45
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 111 Publication
Non-adjacent residuesi15 – 1621 Publication
Non-adjacent residuesi30 – 3121 Publication
Non-terminal residuei45 – 4511 Publication

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  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. Sitel1 Publication.
    Tissue: Root nodule1 Publication.

Entry informationi

Entry nameiXYL1_MEDSA
AccessioniPrimary (citable) accession number: P86450
Entry historyi
Integrated 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. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.