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A5JTQ3 (XYL2_MEDSV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-xylosidase/alpha-L-arabinofuranosidase 2
Alternative name(s):
Xylan 1,4-beta-xylosidase/Alpha-L-arabinofuranosidase 2
Short name=MsXyl2

Including the following 2 domains:

  1. Beta-xylosidase
    EC=3.2.1.37
    Alternative name(s):
    1,4-beta-D-xylan xylohydrolase
    Xylan 1,4-beta-xylosidase
  2. Alpha-L-arabinofuranosidase
    Short name=Arabinosidase
    EC=3.2.1.55
Gene names
Name:Xyl2
OrganismMedicago sativa subsp. varia (Alfalfa) (Medicago varia)
Taxonomic identifier36902 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Protein attributes

Sequence length774 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

Secretedextracellular spaceextracellular matrix By similarity UniProtKB Q9FLG1.

Sequence similarities

Belongs to the glycoside hydrolase 3 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentExtracellular matrix
Secreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termMultifunctional enzyme
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-L-arabinofuranosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

xylan 1,4-beta-xylosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 774741Beta-xylosidase/alpha-L-arabinofuranosidase 2
PRO_0000392641

Sites

Active site3031 By similarity UniProtKB Q9FGY1

Amino acid modifications

Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation4371N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A5JTQ3 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: A709EB1AA6B3EF42

FASTA77483,383
        10         20         30         40         50         60 
MASVENRTPN VSVFLCFFVL FATLLLSGGR VSSQTSAVFA CDVAKNPALA NYGFCNKKLS 

        70         80         90        100        110        120 
VDARVKDLVR RLTLQEKVGN LVNSAVDVSR LGIPKYEWWS EALHGVSNIG PGTHFSNVIP 

       130        140        150        160        170        180 
GATSFPMPIL IAASFNASLF QTIGKVVSTE ARAMHNVGLA GLTYWSPNIN IFRDPRWGRG 

       190        200        210        220        230        240 
QETPGEDPLL ASKYAAGYVK GLQQTDDGDS NKLKVAACCK HYTAYDVDDW KGVQRYTFNA 

       250        260        270        280        290        300 
VVTQQDLDDT YQPPFKSCVI DGNVASVMCS YNQVNGKPTC ADPDLLKGVI RGKWKLNGYI 

       310        320        330        340        350        360 
VSDCDSVDVL FKNQHYTKTP EEAAAKSILA GLDLNCGSFL GRYTEGAVKQ GLIGEASINN 

       370        380        390        400        410        420 
AVYNNFATLM RLGFFDGDPS KQPYGNLGPK DVCTSANQEL AREAARQGIV LLKNCAGSLP 

       430        440        450        460        470        480 
LNAKAIKSLA VIGPNANATR AMIGNYEGIP CKYTSPLQGL TALVPTSFAA GCPDVQCTNA 

       490        500        510        520        530        540 
ALDDAKKIAA SADATVIVVG ANLAIEAESH DRINILLPGQ QQQLVTEVAN VAKGPVILAI 

       550        560        570        580        590        600 
MSGGGMDVSF AKTNKKITSI LWVGYPGEAG GAAIADVIFG YHNPSGRLPM TWYPQSYVDK 

       610        620        630        640        650        660 
VPMTNMNMRP DPATGYPGRT YRFYKGETVF SFGDGISYST FEHKLVKAPQ LVSVPLAEDH 

       670        680        690        700        710        720 
VCRSSKCKSL DVVGEHCQNL AFDIHLRIKN KGKMSSSQTV FLFSTPPAVH NAPQKHLLAF 

       730        740        750        760        770 
EKVLLTGKSE ALVSFKVDVC KDLGLVDELG NRKVALGKHM LHVGDLKHPL SVMI 

« Hide

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: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. A2.
Tissue: Root nodule.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF569969 mRNA. Translation: ABQ45228.1.

3D structure databases

ProteinModelPortalA5JTQ3.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXYL2_MEDSV
AccessionPrimary (citable) accession number: A5JTQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: June 26, 2007
Last modified: May 14, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families