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Protein

Beta-glucosidase 23

Gene

BGLU23

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Beta-D-glucosidase active on scopolin > esculin >> 4-MU-glucoside >> DIMBOA-glucoside. No activity with pNP-glucoside, oNP-glucoside and sinigrin as substrates. May possess beta-D-fucosidase activity. Required for the beneficial interaction with the endophytic fungus P.indica. May participate in the control of root colonization by P.indica by repressing defense responses and modulating other responses required for a mutualistic interaction.4 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.1 Publication

Enzyme regulationi

Activated by tissue damage and upon binding to PBP1 or PBP2.2 Publications

Kineticsi

  1. KM=0.81 mM for scopolin (with recombinant enzyme)1 Publication
  2. KM=0.73 mM for scopolin (with native enzyme)1 Publication
  3. KM=9.7 mM for esculin (with recombinant enzyme)1 Publication
  4. KM=5.8 mM for esculin (with native enzyme)1 Publication

    pH dependencei

    Optimum pH is 5.5.1 Publication

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei54SubstrateBy similarity1
    Binding sitei157SubstrateBy similarity1
    Binding sitei202SubstrateBy similarity1
    Active sitei203Proton donorBy similarity1
    Binding sitei346SubstrateBy similarity1
    Active sitei418NucleophileBy similarity1
    Binding sitei468SubstrateBy similarity1

    GO - Molecular functioni

    • beta-glucosidase activity Source: TAIR
    • copper ion binding Source: TAIR
    • fucosidase activity Source: TAIR
    • protease binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • scopolin beta-glucosidase activity Source: UniProtKB-EC
    • thioglucosidase activity Source: TAIR

    GO - Biological processi

    • carbohydrate metabolic process Source: InterPro
    • cellular response to cold Source: TAIR
    • ER body organization Source: TAIR
    • glucosinolate catabolic process Source: TAIR
    • glucosinolate metabolic process Source: TAIR
    • indole glucosinolate catabolic process Source: TAIR
    • indole glucosinolate metabolic process Source: TAIR
    • negative regulation of defense response Source: UniProtKB
    • response to cytokinin Source: TAIR
    • response to osmotic stress Source: TAIR
    • response to salt stress Source: TAIR
    • response to symbiotic fungus Source: TAIR

    Keywordsi

    Molecular functionGlycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciARA:AT3G09260-MONOMER
    BRENDAi3.2.1.21 399
    ReactomeiR-ATH-189085 Digestion of dietary carbohydrate

    Protein family/group databases

    CAZyiGH1 Glycoside Hydrolase Family 1

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase 23 (EC:3.2.1.21)
    Short name:
    AtBGLU23
    Alternative name(s):
    Protein PHOSPHATE STARVATION-RESPONSE 3.1
    Gene namesi
    Name:BGLU23
    Synonyms:PSR3.1, PYK10
    Ordered Locus Names:At3g09260
    ORF Names:F3L24.13
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 3

    Organism-specific databases

    AraportiAT3G09260
    TAIRilocus:2083524 AT3G09260

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi29C → Y in leb-1; loss of homodimerization resulting in fewer and larger ER bodies. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 241 PublicationAdd BLAST24
    ChainiPRO_000038958525 – 524Beta-glucosidase 23Add BLAST500

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi60N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi222 ↔ 230By similarity
    Glycosylationi461N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi494N-linked (GlcNAc...) asparagineSequence analysis1

    Post-translational modificationi

    Forms interchain disulfide bonds.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9SR37
    PRIDEiQ9SR37

    PTM databases

    SwissPalmiQ9SR37

    Expressioni

    Tissue specificityi

    Expressed exclusively in roots.2 Publications

    Inductioni

    Up-regulated by wounding, 2,4-D and methyl jasmonate (MeJA). Down-regulated by salt and manitol.2 Publications

    Gene expression databases

    ExpressionAtlasiQ9SR37 baseline and differential
    GenevisibleiQ9SR37 AT

    Interactioni

    Subunit structurei

    Homodimers. Binds to the deubiquitinating enzyme AMSH3. The inactive form interacts with PBP1/JAL30 to form the PYK10 complex, at least composed of PYK10/BGLU23, BGLU21, BGLU22, JAL22, JAL23, PBP1/JAL30, PBP2/JAL31, JAL32, JAL33, JAL34, JAL35, GLL22 and GLL23.4 Publications

    GO - Molecular functioni

    • protease binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi5416, 5 interactors
    STRINGi3702.AT3G09260.1

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SR37
    SMRiQ9SR37
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni475 – 476Substrate bindingBy similarity2

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi521 – 524Prevents secretion from ERPROSITE-ProRule annotation4

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG0626 Eukaryota
    COG2723 LUCA
    HOGENOMiHOG000088630
    InParanoidiQ9SR37
    KOiK01188
    OMAiITWESKN
    OrthoDBiEOG093612GV
    PhylomeDBiQ9SR37

    Family and domain databases

    InterProiView protein in InterPro
    IPR001360 Glyco_hydro_1
    IPR033132 Glyco_hydro_1_N_CS
    IPR017853 Glycoside_hydrolase_SF
    PANTHERiPTHR10353 PTHR10353, 1 hit
    PfamiView protein in Pfam
    PF00232 Glyco_hydro_1, 1 hit
    PRINTSiPR00131 GLHYDRLASE1
    SUPFAMiSSF51445 SSF51445, 1 hit
    PROSITEiView protein in PROSITE
    PS00014 ER_TARGET, 1 hit
    PS00653 GLYCOSYL_HYDROL_F1_2, 1 hit

    Sequencei

    Sequence statusi: Complete.

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

    Q9SR37-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVLQKLPLIG LLLLLTIVAS PANADGPVCP PSNKLSRASF PEGFLFGTAT
    60 70 80 90 100
    AAYQVEGAIN ETCRGPALWD IYCRRYPERC NNDNGDVAVD FFHRYKEDIQ
    110 120 130 140 150
    LMKNLNTDAF RMSIAWPRIF PHGRKEKGVS QAGVQFYHDL IDELIKNGIT
    160 170 180 190 200
    PFVTVFHWDT PQDLEDEYGG FLSERIVKDF REYADFVFQE YGGKVKHWIT
    210 220 230 240 250
    FNEPWVFSHA GYDVGKKAPG RCSSYVNAKC QDGRSGYEAY LVTHNLLISH
    260 270 280 290 300
    AEAVEAYRKC EKCKGGKIGI AHSPAWFEAH DLADSQDGAS IDRALDFILG
    310 320 330 340 350
    WHLDTTTFGD YPQIMKDIVG HRLPKFTTEQ KAKLKASTDF VGLNYYTSVF
    360 370 380 390 400
    SNHLEKPDPS KPRWMQDSLI TWESKNAQNY AIGSKPLTAA LNVYSRGFRS
    410 420 430 440 450
    LLKYIKDKYA NPEIMIMENG YGEELGASDS VAVGTADHNR KYYLQRHLLS
    460 470 480 490 500
    MQEAVCIDKV NVTGYFVWSL LDNFEWQDGY KNRFGLYYVD FKNNLTRYEK
    510 520
    ESGKYYKDFL SQGVRPSALK KDEL
    Length:524
    Mass (Da):59,721
    Last modified:May 1, 2000 - v1
    Checksum:i4758EA7A9B8336E1
    GO

    Sequence cautioni

    The sequence AAB38783 differs from that shown. Reason: Frameshift at positions 56 and 63.Curated
    The sequence BAD94012 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti208S → L in CAB50792 (PubMed:11448764).Curated1
    Sequence conflicti208S → L in CAA61592 (PubMed:11448764).Curated1
    Sequence conflicti222C → S in AAB38783 (Ref. 1) Curated1
    Sequence conflicti400S → G in BAD94012 (Ref. 6) Curated1
    Sequence conflicti459K → E in BAH20034 (PubMed:19423640).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U72153 mRNA Translation: AAB38783.1 Frameshift.
    X89413 mRNA Translation: CAA61592.1
    AJ243490 Genomic DNA Translation: CAB50792.1
    AC011436 Genomic DNA Translation: AAF14024.1
    CP002686 Genomic DNA Translation: AEE74744.1
    AF386967 mRNA Translation: AAK62412.1
    AY136440 mRNA Translation: AAM97105.1
    AY140060 mRNA Translation: AAM98201.1
    BT000230 mRNA Translation: AAN15549.1
    AK221291 mRNA Translation: BAD94012.1 Different initiation.
    AK226844 mRNA Translation: BAE98937.1
    AK230345 mRNA Translation: BAF02144.1
    AK317362 mRNA Translation: BAH20034.1
    AK317443 mRNA Translation: BAH20110.1
    PIRiS57621
    RefSeqiNP_187537.1, NM_111760.3
    UniGeneiAt.18035
    At.47576
    At.71001

    Genome annotation databases

    EnsemblPlantsiAT3G09260.1; AT3G09260.1; AT3G09260
    GeneIDi820082
    GrameneiAT3G09260.1; AT3G09260.1; AT3G09260
    KEGGiath:AT3G09260

    Similar proteinsi

    Entry informationi

    Entry nameiBGL23_ARATH
    AccessioniPrimary (citable) accession number: Q9SR37
    Secondary accession number(s): B9DH17
    , O24433, Q42585, Q56YN0
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 24, 2009
    Last sequence update: May 1, 2000
    Last modified: April 25, 2018
    This is version 131 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

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