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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.1 Publication

Catalytic activityi

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

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei64 – 641Substrate
    Metal bindingi100 – 1001Zinc; shared with dimeric partnerSequence Analysis
    Metal bindingi103 – 1031Zinc; shared with dimeric partnerSequence Analysis
    Binding sitei165 – 1651Substrate
    Binding sitei210 – 2101Substrate
    Active sitei211 – 2111Proton donorBy similarity
    Binding sitei354 – 3541Substrate
    Active sitei427 – 4271NucleophileBy similarity
    Binding sitei477 – 4771Substrate

    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
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    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 6 (EC:3.2.1.21)
    Short name:
    Os3bglu6
    Gene namesi
    Name:BGLU6
    Ordered Locus Names:Os03g0212800, LOC_Os03g11420
    OrganismiOryza sativa subsp. japonica (Rice)
    Taxonomic identifieri39947 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
    ProteomesiUP000000763 Componenti: Chromosome 3

    Organism-specific databases

    GrameneiQ8L7J2.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 521490Beta-glucosidase 6PRO_0000387495Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi230 ↔ 2381 Publication
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ8L7J2.

    Expressioni

    Gene expression databases

    ExpressionAtlasiQ8L7J2. baseline and differential.

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Protein-protein interaction databases

    STRINGi39947.LOC_Os03g11420.1.

    Structurei

    Secondary structure

    1
    521
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi47 – 493Combined sources
    Beta strandi55 – 595Combined sources
    Helixi62 – 654Combined sources
    Helixi71 – 733Combined sources
    Helixi78 – 836Combined sources
    Helixi101 – 11515Combined sources
    Beta strandi119 – 1235Combined sources
    Helixi126 – 1294Combined sources
    Beta strandi133 – 1364Combined sources
    Helixi139 – 15416Combined sources
    Beta strandi158 – 1669Combined sources
    Helixi170 – 1767Combined sources
    Helixi178 – 1803Combined sources
    Helixi183 – 19917Combined sources
    Turni200 – 2023Combined sources
    Beta strandi205 – 2106Combined sources
    Helixi212 – 2209Combined sources
    Turni232 – 2343Combined sources
    Turni243 – 2453Combined sources
    Helixi246 – 26823Combined sources
    Helixi270 – 2734Combined sources
    Beta strandi276 – 2827Combined sources
    Beta strandi285 – 2928Combined sources
    Helixi293 – 30614Combined sources
    Helixi308 – 3169Combined sources
    Helixi321 – 3277Combined sources
    Helixi328 – 3303Combined sources
    Helixi336 – 3427Combined sources
    Beta strandi347 – 3526Combined sources
    Beta strandi356 – 3616Combined sources
    Beta strandi366 – 3683Combined sources
    Helixi369 – 3713Combined sources
    Helixi374 – 3774Combined sources
    Beta strandi380 – 3867Combined sources
    Beta strandi389 – 3924Combined sources
    Helixi405 – 41814Combined sources
    Beta strandi423 – 4286Combined sources
    Helixi440 – 4434Combined sources
    Helixi447 – 46519Combined sources
    Beta strandi471 – 4777Combined sources
    Helixi485 – 4906Combined sources
    Beta strandi495 – 4984Combined sources
    Turni500 – 5045Combined sources
    Beta strandi506 – 5083Combined sources
    Helixi510 – 51910Combined sources

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ8L7J2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni484 – 4852Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2723.
    InParanoidiQ8L7J2.
    KOiK01188.
    OMAiMTGVGLP.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    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.
    AK119546 mRNA. Translation: BAG99682.1.
    RefSeqiNP_001049358.1. NM_001055893.1.
    UniGeneiOs.15799.

    Genome annotation databases

    EnsemblPlantsiOS03T0212800-01; OS03T0212800-01; OS03G0212800.
    GeneIDi4332041.
    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.
    AK119546 mRNA. Translation: BAG99682.1.
    RefSeqiNP_001049358.1. NM_001055893.1.
    UniGeneiOs.15799.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi39947.LOC_Os03g11420.1.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Proteomic databases

    PRIDEiQ8L7J2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    GrameneiQ8L7J2.

    Phylogenomic databases

    eggNOGiCOG2723.
    InParanoidiQ8L7J2.
    KOiK01188.
    OMAiMTGVGLP.

    Enzyme and pathway databases

    BRENDAi3.2.1.21. 4460.
    SABIO-RKQ8L7J2.

    Miscellaneous databases

    EvolutionaryTraceiQ8L7J2.

    Gene expression databases

    ExpressionAtlasiQ8L7J2. baseline and differential.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Structural and enzymatic characterization of Os3BGlu6, a rice beta-glucosidase hydrolyzing hydrophobic glycosides and (1->3)- and (1->2)-linked disaccharides."
      Seshadri S., Akiyama T., Opassiri R., Kuaprasert B., Cairns J.K.
      Plant Physiol. 151:47-58(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 38-521 IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BONDS.
      Strain: cv. Yukihikari.
    2. "Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species."
      The rice chromosome 3 sequencing consortium
      Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S.
      , Johri S., Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., Lee H.R., Jiang J., Jackson S.
      Genome Res. 15:1284-1291(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    4. "The rice annotation project database (RAP-DB): 2008 update."
      The rice annotation project (RAP)
      Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: cv. Nipponbare.
    5. "Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
      The rice full-length cDNA consortium
      Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Nipponbare.
    6. "Analysis of rice glycosyl hydrolase family 1 and expression of Os4bglu12 beta-glucosidase."
      Opassiri R., Pomthong B., Onkoksoong T., Akiyama T., Esen A., Ketudat Cairns J.R.
      BMC Plant Biol. 6:33-33(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiBGL06_ORYSJ
    AccessioniPrimary (citable) accession number: Q8L7J2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 3, 2009
    Last sequence update: October 1, 2002
    Last modified: July 22, 2015
    This is version 83 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

    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.