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Protein

Beta-glucosidase 6

Gene

BGLU6

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes glycosides, oligosaccharides and hydrophobic glycosides (PubMed:19587102). Possesses gibberellin ester beta-D-glucosidase activity. Can hydrolyze gibberellin A4 beta-D-glucosyl ester in vitro (PubMed:23811195).2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=6.3 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0)1 Publication
  2. KM=0.5 mM for p-nitrophenyl beta-D-fucoside (at pH 5.0)1 Publication
  3. KM=6.06 mM for p-nitrophenyl beta-D-galactoside (at pH 5.0)1 Publication
  4. KM=4.5 mM for n-octyl-beta-D-glucoside (at pH 5.0)1 Publication
  5. KM=5.0 mM for n-heptyl-beta-D-glucoside (at pH 5.0)1 Publication
  6. KM=3.6 mM for laminaribiose (at pH 5.0)1 Publication
  7. KM=8.7 mM for laminaritriose (at pH 5.0)1 Publication
  8. KM=15.3 mM for cellobiose (at pH 5.0)1 Publication
  9. KM=9.8 mM for sophorose (at pH 5.0)1 Publication
  10. KM=14.9 mM for gentiobiose (at pH 5.0)1 Publication

    pH dependencei

    Optimum pH is 4.5.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei64SubstrateCombined sources2 Publications1
    Binding sitei165SubstrateCombined sources1 Publication1
    Binding sitei210SubstrateCombined sources2 Publications1
    Active sitei211Proton donor1 Publication1
    Binding sitei354SubstrateCombined sources2 Publications1
    Active sitei427Nucleophile1 Publication1
    Binding sitei477SubstrateCombined sources2 Publications1

    GO - Molecular functioni

    • beta-D-fucosidase activity Source: UniProtKB
    • beta-galactosidase activity Source: UniProtKB
    • beta-gentiobiose beta-glucosidase activity Source: UniProtKB
    • beta-glucosidase activity Source: UniProtKB
    • cellobiose glucosidase activity Source: UniProtKB
    • glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB
    • hydrolase activity, acting on glycosyl bonds Source: UniProtKB
    • scopolin beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi3.2.1.21. 4460.
    SABIO-RKQ8L7J2.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase 6Curated (EC:3.2.1.211 Publication)
    Short name:
    Os3bglu61 Publication
    Gene namesi
    Name:BGLU6Curated
    Ordered Locus Names:Os03g0212800Imported, LOC_Os03g11420Imported
    OrganismiOryza sativa subsp. japonica (Rice)
    Taxonomic identifieri39947 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
    Proteomesi
    • UP000059680 Componenti: Chromosome 3

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi211E → A: Decreases activity toward gibberellin A4 beta-D-glucosyl ester 5-fold. 1 Publication1
    Mutagenesisi211E → Q: Decreases activity toward gibberellin A4 beta-D-glucosyl ester 10-fold. 1 Publication1
    Mutagenesisi284M → N: Decreases the kcat/Km values 7 to 30-fold depending on the substrate. 1 Publication1
    Mutagenesisi427E → D: Decreases activity toward gibberellin A4 beta-D-glucosyl ester 70-fold. 1 Publication1
    Mutagenesisi427E → Q: Decreases activity toward gibberellin A4 beta-D-glucosyl ester 200-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 31Sequence analysisAdd BLAST31
    ChainiPRO_000038749532 – 521Beta-glucosidase 6Add BLAST490

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi230 ↔ 2382 Publications
    Glycosylationi291N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi362N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi372N-linked (GlcNAc...)Sequence analysis1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ8L7J2.
    PRIDEiQ8L7J2.

    Expressioni

    Gene expression databases

    GenevisibleiQ8L7J2. OS.

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Protein-protein interaction databases

    STRINGi39947.LOC_Os03g11420.1.

    Structurei

    Secondary structure

    1521
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi47 – 49Combined sources3
    Beta strandi55 – 59Combined sources5
    Helixi62 – 65Combined sources4
    Helixi71 – 73Combined sources3
    Helixi78 – 83Combined sources6
    Helixi101 – 115Combined sources15
    Beta strandi119 – 123Combined sources5
    Helixi126 – 129Combined sources4
    Beta strandi133 – 136Combined sources4
    Helixi139 – 154Combined sources16
    Beta strandi158 – 166Combined sources9
    Helixi170 – 176Combined sources7
    Helixi178 – 180Combined sources3
    Helixi183 – 199Combined sources17
    Turni200 – 202Combined sources3
    Beta strandi205 – 210Combined sources6
    Helixi212 – 220Combined sources9
    Turni232 – 234Combined sources3
    Turni243 – 245Combined sources3
    Helixi246 – 268Combined sources23
    Helixi270 – 273Combined sources4
    Beta strandi276 – 282Combined sources7
    Beta strandi285 – 292Combined sources8
    Helixi293 – 306Combined sources14
    Helixi308 – 316Combined sources9
    Helixi321 – 327Combined sources7
    Helixi328 – 330Combined sources3
    Helixi336 – 342Combined sources7
    Beta strandi347 – 352Combined sources6
    Beta strandi356 – 361Combined sources6
    Beta strandi366 – 368Combined sources3
    Helixi369 – 371Combined sources3
    Helixi374 – 377Combined sources4
    Beta strandi380 – 386Combined sources7
    Beta strandi389 – 392Combined sources4
    Helixi405 – 418Combined sources14
    Beta strandi423 – 428Combined sources6
    Helixi440 – 443Combined sources4
    Helixi447 – 465Combined sources19
    Beta strandi471 – 477Combined sources7
    Helixi485 – 490Combined sources6
    Beta strandi495 – 498Combined sources4
    Turni500 – 504Combined sources5
    Beta strandi506 – 508Combined sources3
    Helixi510 – 519Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3GNOX-ray1.83A38-521[»]
    3GNPX-ray1.80A38-521[»]
    3GNRX-ray1.81A38-521[»]
    3WBAX-ray1.90A38-521[»]
    3WBEX-ray1.97A38-521[»]
    ProteinModelPortaliQ8L7J2.
    SMRiQ8L7J2.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8L7J2.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni484 – 485Substrate bindingCombined sources2 Publications2

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG0626. Eukaryota.
    COG2723. LUCA.
    InParanoidiQ8L7J2.
    KOiK01188.
    OMAiGYAEGRH.
    OrthoDBiEOG093606FR.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR033132. Glyco_hydro_1_N_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8L7J2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGRIKSSSGR CSTARLEAVA VLVVVFGVAS SSLRGCIAQQ SGGGLTRGSF
    60 70 80 90 100
    PEGFVFGTAS AAYQYEGAVK EDGRGQTIWD TFAHTFGKIT DFSNADVAVD
    110 120 130 140 150
    QYHRFEEDIQ LMADMGMDAY RFSIAWSRIY PNGVGQVNQA GIDHYNKLID
    160 170 180 190 200
    ALLAKGIQPY VTLYHWDLPQ ALEDKYKGWL DRQIVDDFAA YAETCFREFG
    210 220 230 240 250
    DRVKHWITLN EPHTVAIQGY DAGLQAPGRC SVLLHLYCKA GNSGTEPYVV
    260 270 280 290 300
    AHHFILAHAA AASIYRTKYK ATQNGQLGIA FDVMWFEPMS NTTIDIEAAK
    310 320 330 340 350
    RAQEFQLGWF ADPFFFGDYP ATMRARVGER LPRFTADEAA VVKGALDFVG
    360 370 380 390 400
    INHYTTYYTR HNNTNIIGTL LNNTLADTGT VSLPFKNGKP IGDRANSIWL
    410 420 430 440 450
    YIVPRGMRSL MNYVKERYNS PPVYITENGM DDSNNPFISI KDALKDSKRI
    460 470 480 490 500
    KYHNDYLTNL AASIKEDGCD VRGYFAWSLL DNWEWAAGYS SRFGLYFVDY
    510 520
    KDNLKRYPKN SVQWFKALLK T
    Length:521
    Mass (Da):58,539
    Last modified:October 1, 2002 - v1
    Checksum:i0554435869F3BD21
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY129294 mRNA. Translation: AAN01354.1.
    DP000009 Genomic DNA. Translation: ABF94615.1.
    AP008209 Genomic DNA. Translation: BAF11272.1.
    AP014959 Genomic DNA. Translation: BAS82933.1.
    AK119546 mRNA. Translation: BAG99682.1.
    RefSeqiXP_015628023.1. XM_015772537.1.
    UniGeneiOs.15799.

    Genome annotation databases

    EnsemblPlantsiOS03T0212800-01; OS03T0212800-01; OS03G0212800.
    GeneIDi4332041.
    GrameneiOS03T0212800-01; OS03T0212800-01; OS03G0212800.
    KEGGiosa:4332041.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY129294 mRNA. Translation: AAN01354.1.
    DP000009 Genomic DNA. Translation: ABF94615.1.
    AP008209 Genomic DNA. Translation: BAF11272.1.
    AP014959 Genomic DNA. Translation: BAS82933.1.
    AK119546 mRNA. Translation: BAG99682.1.
    RefSeqiXP_015628023.1. XM_015772537.1.
    UniGeneiOs.15799.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3GNOX-ray1.83A38-521[»]
    3GNPX-ray1.80A38-521[»]
    3GNRX-ray1.81A38-521[»]
    3WBAX-ray1.90A38-521[»]
    3WBEX-ray1.97A38-521[»]
    ProteinModelPortaliQ8L7J2.
    SMRiQ8L7J2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi39947.LOC_Os03g11420.1.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Proteomic databases

    PaxDbiQ8L7J2.
    PRIDEiQ8L7J2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiOS03T0212800-01; OS03T0212800-01; OS03G0212800.
    GeneIDi4332041.
    GrameneiOS03T0212800-01; OS03T0212800-01; OS03G0212800.
    KEGGiosa:4332041.

    Phylogenomic databases

    eggNOGiKOG0626. Eukaryota.
    COG2723. LUCA.
    InParanoidiQ8L7J2.
    KOiK01188.
    OMAiGYAEGRH.
    OrthoDBiEOG093606FR.

    Enzyme and pathway databases

    BRENDAi3.2.1.21. 4460.
    SABIO-RKQ8L7J2.

    Miscellaneous databases

    EvolutionaryTraceiQ8L7J2.

    Gene expression databases

    GenevisibleiQ8L7J2. OS.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR033132. Glyco_hydro_1_N_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiBGL06_ORYSJ
    AccessioniPrimary (citable) accession number: Q8L7J2
    Secondary accession number(s): A0A0P0VUN5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 3, 2009
    Last sequence update: October 1, 2002
    Last modified: November 30, 2016
    This is version 96 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Oryza sativa (rice)
      Index of Oryza sativa entries and their corresponding gene designations
    4. SIMILARITY comments
      Index of protein domains and families

    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 one 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.