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A5JTQ2

- XYL1_MEDSV

UniProt

A5JTQ2 - XYL1_MEDSV

Protein

Beta-xylosidase/alpha-L-arabinofuranosidase 1

Gene

Xyl1

Organism
Medicago sativa subsp. varia (Alfalfa) (Medicago varia)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (26 Jun 2007)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

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

    Kineticsi

    1. KM=0.59 mM for pNP-beta-D-xlyoside (at 37 degrees Celsius)1 Publication
    2. KM=0.94 mM for pNP-alpha-L-arabinofuranoside (at 37 degrees Celsius)1 Publication
    3. KM=1.20 mM for pNP-alpha-L-arabinopyranoside (at 37 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei303 – 3031By similarity

    GO - Molecular functioni

    1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC
    2. xylan 1,4-beta-xylosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Protein family/group databases

    CAZyiGH3. Glycoside Hydrolase Family 3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-xylosidase/alpha-L-arabinofuranosidase 1Imported1 Publication
    Alternative name(s):
    Xylan 1,4-beta-xylosidase/Alpha-L-arabinofuranosidase 1
    Short name:
    MsXyl11 Publication
    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:Xyl1Imported
    OrganismiMedicago sativa subsp. varia (Alfalfa) (Medicago varia)
    Taxonomic identifieri36902 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix By similarity

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei‹1 – 33›33Sequence AnalysisAdd
    BLAST
    Chaini34 – 774741Beta-xylosidase/alpha-L-arabinofuranosidase 1Sequence AnalysisPRO_0000392640Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliA5JTQ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycoside hydrolase 3 family.Sequence Analysis

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    3.40.50.1700. 1 hit.
    InterProiIPR026891. Fn3-like.
    IPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR30620. PTHR30620. 1 hit.
    PfamiPF14310. Fn3-like. 1 hit.
    PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    [Graphical view]
    PRINTSiPR00133. GLHYDRLASE3.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A5JTQ2-1 [UniParc]FASTAAdd to Basket

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    ANTKNREPKV SSVFLCFSIF YVTVLLNCNH VYGQTSTVFA CDVAKNTNVS    50
    SYGFCDNSLS VEDRVSDLVK RLTLQEKIGN LGNSAVEVSR LGIPKYEWWS 100
    EALHGVSNIG PGTHFSSLVP GATNFPMPIL TAASFNTSLF QAIGSVVSNE 150
    ARAMYNVGLA GLTYWSPNIN IFRDPRWGRG QETPGEDPLL SSKYAAGYVK 200
    GLQQTDDGDS DKLKVAACCK HYTAYDVDNW KGVQRYTFDA VVSQQDLDDT 250
    FQPPFKSCVI DGNVASVMCS YNKVNGKPTC ADPDLLKGVI RGKWKLNGYI 300
    VSDCDSVEVL YKDQHYTKTP EEAAAKTILS GLDLDCGSYL GQYTGGAVKQ 350
    GLVDEASITN AVSNNFATLM RLGFFDGDPS KQPYGNLGPK DVCTPENQEL 400
    AREAARQGIV LLKNSPRSLP LSSKAIKSLA VIGPNANATR VMIGNYEGIP 450
    CKYTSPLQGL TAFVPTSYAP GCPDVQCANA QIDDAAKIAA SADATIIVVG 500
    ANLAIEAESL DRVNILLPGQ QQQLVNEVAN VSKGPVILVI MSGGGMDVSF 550
    AKTNDKITSI LWVGYPGEAG GAAIADVIFG SYNPSGRLPM TWYPQSYVEK 600
    VPMTNMNMRA DPATGYPGRT YRFYKGETVF SFGDGMSFGT VEHKIVKAPQ 650
    LVSVPLAEDH ECRSLECKSL DVADKHCQNL AFDIHLSVKN MGKMSSSHSV 700
    LLFFTPPNVH NAPQKHLLGF EKVQLAGKSE GMVRFKVDVC NDLSVVDELG 750
    NRKVPLGDHM LHVGNLKHSL SVRI 774
    Length:774
    Mass (Da):83,727
    Last modified:June 26, 2007 - v1
    Checksum:i6C45493BA13ABF5F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11Imported

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF569968 mRNA. Translation: ABQ45227.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF569968 mRNA. Translation: ABQ45227.1 .

    3D structure databases

    ProteinModelPortali A5JTQ2.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH3. Glycoside Hydrolase Family 3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.300. 1 hit.
    3.40.50.1700. 1 hit.
    InterProi IPR026891. Fn3-like.
    IPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR30620. PTHR30620. 1 hit.
    Pfami PF14310. Fn3-like. 1 hit.
    PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00133. GLHYDRLASE3.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 1 hit.
    ProtoNeti Search...

    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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTEOLYTIC PROCESSING.
      Strain: cv. A21 Publication.
      Tissue: Root noduleImported.

    Entry informationi

    Entry nameiXYL1_MEDSV
    AccessioniPrimary (citable) accession number: A5JTQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 2010
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 27 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

    Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3