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Protein

Beta-xylosidase/alpha-L-arabinofuranosidase 1

Gene

Xyl1

Organism
Medicago sativa subsp. varia (Alfalfa) (Medicago varia)
Status
Reviewed-Annotation score: Annotation score: 4 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. 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

    GO - Biological processi

    Complete GO annotation...

    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 11 PublicationImported
    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

    GO - Cellular componenti

    Complete GO annotation...

    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

    « Hide

            10         20         30         40         50
    ANTKNREPKV SSVFLCFSIF YVTVLLNCNH VYGQTSTVFA CDVAKNTNVS
    60 70 80 90 100
    SYGFCDNSLS VEDRVSDLVK RLTLQEKIGN LGNSAVEVSR LGIPKYEWWS
    110 120 130 140 150
    EALHGVSNIG PGTHFSSLVP GATNFPMPIL TAASFNTSLF QAIGSVVSNE
    160 170 180 190 200
    ARAMYNVGLA GLTYWSPNIN IFRDPRWGRG QETPGEDPLL SSKYAAGYVK
    210 220 230 240 250
    GLQQTDDGDS DKLKVAACCK HYTAYDVDNW KGVQRYTFDA VVSQQDLDDT
    260 270 280 290 300
    FQPPFKSCVI DGNVASVMCS YNKVNGKPTC ADPDLLKGVI RGKWKLNGYI
    310 320 330 340 350
    VSDCDSVEVL YKDQHYTKTP EEAAAKTILS GLDLDCGSYL GQYTGGAVKQ
    360 370 380 390 400
    GLVDEASITN AVSNNFATLM RLGFFDGDPS KQPYGNLGPK DVCTPENQEL
    410 420 430 440 450
    AREAARQGIV LLKNSPRSLP LSSKAIKSLA VIGPNANATR VMIGNYEGIP
    460 470 480 490 500
    CKYTSPLQGL TAFVPTSYAP GCPDVQCANA QIDDAAKIAA SADATIIVVG
    510 520 530 540 550
    ANLAIEAESL DRVNILLPGQ QQQLVNEVAN VSKGPVILVI MSGGGMDVSF
    560 570 580 590 600
    AKTNDKITSI LWVGYPGEAG GAAIADVIFG SYNPSGRLPM TWYPQSYVEK
    610 620 630 640 650
    VPMTNMNMRA DPATGYPGRT YRFYKGETVF SFGDGMSFGT VEHKIVKAPQ
    660 670 680 690 700
    LVSVPLAEDH ECRSLECKSL DVADKHCQNL AFDIHLSVKN MGKMSSSHSV
    710 720 730 740 750
    LLFFTPPNVH NAPQKHLLGF EKVQLAGKSE GMVRFKVDVC NDLSVVDELG
    760 770
    NRKVPLGDHM LHVGNLKHSL SVRI
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF569968 mRNA. Translation: ABQ45227.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF569968 mRNA. Translation: ABQ45227.1.

    3D structure databases

    ProteinModelPortaliA5JTQ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH3. Glycoside Hydrolase Family 3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    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.
    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: 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: January 7, 2015
    This is version 29 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

    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.