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A5JTQ2 (XYL1_MEDSV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 25. 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 1
Alternative name(s):
Xylan 1,4-beta-xylosidase/Alpha-L-arabinofuranosidase 1
Short name=MsXyl1

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:Xyl1
OrganismMedicago sativa subsp. varia (Alfalfa) (Medicago varia)
Taxonomic identifier36902 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Protein attributes

Sequence length774 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Does not cleave xylan from oat spelts although xylan from oat spelts was degraded to xylose when this enzyme was used in combination with xylanase. Also releases xylose and arabinose from aryl glycosides, xylo-oligosaccharides, arabinan from sugar beet and arabino-oligosaccharides, arabinan from sugar beet and arabinoxylan from wheat. Ref.1

Catalytic activity

Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini. Ref.1

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. Ref.1

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity UniProtKB Q9FLG1.

Post-translational modification

Proteolytically cleaved in roots to form a 65 kDa protein. Ref.1

Sequence similarities

Belongs to the glycoside hydrolase 3 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.59 mM for pNP-beta-D-xlyoside (at 37 degrees Celsius) Ref.1

KM=0.94 mM for pNP-alpha-L-arabinofuranoside (at 37 degrees Celsius) Ref.1

KM=1.20 mM for pNP-alpha-L-arabinopyranoside (at 37 degrees Celsius)

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 peptide‹1 – 33›33 Potential
Chain34 – 774741Beta-xylosidase/alpha-L-arabinofuranosidase 1
PRO_0000392640

Sites

Active site3031 By similarity UniProtKB Q9FGY1

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Potential
Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation4371N-linked (GlcNAc...) Potential
Glycosylation5301N-linked (GlcNAc...) Potential

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
A5JTQ2 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 6C45493BA13ABF5F

FASTA77483,727
        10         20         30         40         50         60 
ANTKNREPKV SSVFLCFSIF YVTVLLNCNH VYGQTSTVFA CDVAKNTNVS SYGFCDNSLS 

        70         80         90        100        110        120 
VEDRVSDLVK RLTLQEKIGN LGNSAVEVSR LGIPKYEWWS EALHGVSNIG PGTHFSSLVP 

       130        140        150        160        170        180 
GATNFPMPIL TAASFNTSLF QAIGSVVSNE ARAMYNVGLA GLTYWSPNIN IFRDPRWGRG 

       190        200        210        220        230        240 
QETPGEDPLL SSKYAAGYVK GLQQTDDGDS DKLKVAACCK HYTAYDVDNW KGVQRYTFDA 

       250        260        270        280        290        300 
VVSQQDLDDT FQPPFKSCVI DGNVASVMCS YNKVNGKPTC ADPDLLKGVI RGKWKLNGYI 

       310        320        330        340        350        360 
VSDCDSVEVL YKDQHYTKTP EEAAAKTILS GLDLDCGSYL GQYTGGAVKQ GLVDEASITN 

       370        380        390        400        410        420 
AVSNNFATLM RLGFFDGDPS KQPYGNLGPK DVCTPENQEL AREAARQGIV LLKNSPRSLP 

       430        440        450        460        470        480 
LSSKAIKSLA VIGPNANATR VMIGNYEGIP CKYTSPLQGL TAFVPTSYAP GCPDVQCANA 

       490        500        510        520        530        540 
QIDDAAKIAA SADATIIVVG ANLAIEAESL DRVNILLPGQ QQQLVNEVAN VSKGPVILVI 

       550        560        570        580        590        600 
MSGGGMDVSF AKTNDKITSI LWVGYPGEAG GAAIADVIFG SYNPSGRLPM TWYPQSYVEK 

       610        620        630        640        650        660 
VPMTNMNMRA DPATGYPGRT YRFYKGETVF SFGDGMSFGT VEHKIVKAPQ LVSVPLAEDH 

       670        680        690        700        710        720 
ECRSLECKSL DVADKHCQNL AFDIHLSVKN MGKMSSSHSV LLFFTPPNVH NAPQKHLLGF 

       730        740        750        760        770 
EKVQLAGKSE GMVRFKVDVC NDLSVVDELG NRKVPLGDHM LHVGNLKHSL SVRI 

« 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], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTEOLYTIC PROCESSING.
Strain: cv. A2.
Tissue: Root nodule.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF569968 mRNA. Translation: ABQ45227.1.

3D structure databases

ProteinModelPortalA5JTQ2.
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 nameXYL1_MEDSV
AccessionPrimary (citable) accession number: A5JTQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 25 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