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Protein

Beta-glucosidase 7

Gene

BGLU7

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

Functioni

Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, oligosaccharides, pyridoxine beta-D-glucoside and the cyanogenic glucosides amygdalin, prunasin and dhurrin. Possesses pyridoxine transglucosylation activity.3 Publications

Catalytic activityi

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

Kineticsi

  1. KM=0.2 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0)3 Publications
  2. KM=0.23 mM for p-nitrophenyl beta-D-fucoside (at pH 5.0)3 Publications
  3. KM=3.2 mM for p-nitrophenyl beta-D-galactoside (at pH 5.0)3 Publications
  4. KM=1.3 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0)3 Publications
  5. KM=1.3 mM for p-nitrophenyl beta-D-xyloside (at pH 5.0)3 Publications
  6. KM=1.2 mM for p-nitrophenyl beta-L-arabinoside (at pH 5.0)3 Publications
  7. KM=0.78 mM for p-nitrophenyl beta-D-cellobioside (at pH 5.0)3 Publications
  8. KM=22 mM for cellobiose (at pH 5.0)3 Publications
  9. KM=0.22 mM for cellotriose (at pH 5.0)3 Publications
  10. KM=0.28 mM for cellotetraose (at pH 5.0)3 Publications
  11. KM=0.24 mM for cellopentaose (at pH 5.0)3 Publications
  12. KM=0.22 mM for cellohexaose (at pH 5.0)3 Publications
  13. KM=2.05 mM for laminaribiose (at pH 5.0)3 Publications
  14. KM=1.92 mM for laminaritriose (at pH 5.0)3 Publications
  15. KM=13.9 mM for sophorose (at pH 5.0)3 Publications
  16. KM=38.3 mM for gentiobiose (at pH 5.0)3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571Substrate
    Metal bindingi93 – 931Zinc; shared with dimeric partner
    Metal bindingi96 – 961Zinc; shared with dimeric partner
    Binding sitei158 – 1581Substrate
    Binding sitei203 – 2031Substrate
    Active sitei204 – 2041Proton donorBy similarity
    Binding sitei343 – 3431Substrate
    Active sitei414 – 4141NucleophileBy similarity
    Binding sitei461 – 4611Substrate

    GO - Molecular functioni

    • amygdalin beta-glucosidase activity Source: UniProtKB
    • beta-D-fucosidase activity Source: UniProtKB
    • beta-galactosidase activity Source: UniProtKB
    • beta-gentiobiose beta-glucosidase activity Source: UniProtKB
    • beta-glucosidase activity Source: UniProtKB
    • beta-L-arabinosidase activity Source: UniProtKB
    • beta-mannosidase activity Source: UniProtKB
    • cellobiose glucosidase activity Source: UniProtKB
    • glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • prunasin beta-glucosidase activity Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    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-RKQ75I93.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase 7 (EC:3.2.1.21)
    Short name:
    Os3bglu7
    Gene namesi
    Name:BGLU7
    Synonyms:BGLU1
    Ordered Locus Names:Os03g0703000, LOC_Os03g49600
    ORF Names:OSJNBa0004L11.16
    OrganismiOryza sativa subsp. japonica (Rice)
    Taxonomic identifieri39947 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
    ProteomesiUP000000763 Componenti: Chromosome 3

    Organism-specific databases

    GrameneiQ75I93.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi207 – 2071I → V: Increases KM for substrate about 5-fold. 1 Publication
    Mutagenesisi218 – 2181N → H: Decreases KM for substrate about 2-fold. 1 Publication
    Mutagenesisi273 – 2731N → V: Increases KM for substrate about 5-fold. 1 Publication
    Mutagenesisi470 – 4701L → R: No effect on KM. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 504478Beta-glucosidase 7PRO_0000383461Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi223 ↔ 226By similarity
    Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi422 – 4221N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ75I93.

    Interactioni

    Subunit structurei

    Homodimer. Formation of the homodimer is zinc-dependent. Dimerization does not increase activity.1 Publication

    Protein-protein interaction databases

    STRINGi39947.LOC_Os03g49600.1.

    Structurei

    Secondary structure

    1
    504
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni34 – 374Combined sources
    Helixi40 – 423Combined sources
    Beta strandi48 – 525Combined sources
    Helixi55 – 584Combined sources
    Helixi71 – 766Combined sources
    Helixi83 – 853Combined sources
    Beta strandi88 – 903Combined sources
    Helixi94 – 10714Combined sources
    Beta strandi112 – 1165Combined sources
    Helixi119 – 1224Combined sources
    Beta strandi126 – 1283Combined sources
    Helixi132 – 14716Combined sources
    Beta strandi151 – 1566Combined sources
    Helixi163 – 1697Combined sources
    Helixi171 – 1733Combined sources
    Helixi177 – 19216Combined sources
    Turni193 – 1953Combined sources
    Beta strandi198 – 2036Combined sources
    Helixi205 – 2139Combined sources
    Turni232 – 2343Combined sources
    Helixi235 – 25723Combined sources
    Helixi259 – 2624Combined sources
    Beta strandi265 – 2717Combined sources
    Beta strandi274 – 2818Combined sources
    Helixi282 – 29514Combined sources
    Helixi297 – 3059Combined sources
    Helixi310 – 3167Combined sources
    Helixi317 – 3193Combined sources
    Helixi325 – 3317Combined sources
    Beta strandi336 – 3416Combined sources
    Beta strandi345 – 3495Combined sources
    Helixi361 – 3644Combined sources
    Beta strandi368 – 3736Combined sources
    Beta strandi376 – 3794Combined sources
    Helixi392 – 40413Combined sources
    Beta strandi410 – 4145Combined sources
    Beta strandi419 – 4224Combined sources
    Helixi425 – 4295Combined sources
    Helixi432 – 45019Combined sources
    Beta strandi455 – 4617Combined sources
    Helixi469 – 4746Combined sources
    Beta strandi479 – 4824Combined sources
    Turni484 – 4863Combined sources
    Beta strandi489 – 4913Combined sources
    Helixi493 – 5019Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RGLX-ray2.20A/B29-504[»]
    2RGMX-ray1.55A/B29-504[»]
    3AHTX-ray2.80A/B29-504[»]
    3AHVX-ray1.75A/B29-504[»]
    3F4VX-ray1.65A/B29-504[»]
    3F5JX-ray1.95A/B29-504[»]
    3F5KX-ray1.80A/B29-504[»]
    3F5LX-ray1.37A/B29-504[»]
    3SCNX-ray2.20A/B29-504[»]
    3SCOX-ray1.95A/B29-504[»]
    3SCPX-ray2.10A/B29-504[»]
    3SCQX-ray2.10A/B29-504[»]
    3SCRX-ray1.80A/B29-504[»]
    3SCSX-ray1.85A/B29-504[»]
    3SCTX-ray1.60A/B29-504[»]
    3SCUX-ray1.58A/B29-504[»]
    3SCVX-ray2.11A/B29-504[»]
    3SCWX-ray1.90A/B29-504[»]
    ProteinModelPortaliQ75I93.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ75I93.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni468 – 4692Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    InParanoidiQ75I93.
    KOiK05350.
    OMAiFNTLERH.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q75I93-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAARRANCAL VLVLALALLA ARDAGAAAVP KPNWLGGLSR AAFPKRFVFG
    60 70 80 90 100
    TATSAYQVEG MAASGGRGPS IWDAFAHTPG NVAGNQNGDV ATDQYHRYKE
    110 120 130 140 150
    DVNLMKSLNF DAYRFSISWS RIFPDGEGRV NQEGVAYYNN LINYLLQKGI
    160 170 180 190 200
    TPYVNLYHYD LPLALEKKYG GWLNAKMADL FTEYADFCFK TFGNRVKHWF
    210 220 230 240 250
    TFNEPRIVAL LGYDQGTNPP KRCTKCAAGG NSATEPYIVA HNFLLSHAAA
    260 270 280 290 300
    VARYRTKYQA AQQGKVGIVL DFNWYEALSN STEDQAAAQR ARDFHIGWYL
    310 320 330 340 350
    DPLINGHYPQ IMQDLVKDRL PKFTPEQARL VKGSADYIGI NQYTASYMKG
    360 370 380 390 400
    QQLMQQTPTS YSADWQVTYV FAKNGKPIGP QANSNWLYIV PWGMYGCVNY
    410 420 430 440 450
    IKQKYGNPTV VITENGMDQP ANLSRDQYLR DTTRVHFYRS YLTQLKKAID
    460 470 480 490 500
    EGANVAGYFA WSLLDNFEWL SGYTSKFGIV YVDFNTLERH PKASAYWFRD

    MLKH
    Length:504
    Mass (Da):56,872
    Last modified:July 5, 2004 - v1
    Checksum:i4C36D2A5AF452CE9
    GO

    Sequence cautioni

    The sequence AAS07255.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence ABF98424.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence ABF98425.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence ABF98426.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521A → V in AAA84906 (Ref. 1) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U28047 mRNA. Translation: AAA84906.3.
    AC091670 Genomic DNA. Translation: AAX95519.1.
    AC133334 Genomic DNA. Translation: AAS07254.1.
    AC133334 Genomic DNA. Translation: AAS07255.1. Sequence problems.
    DP000009 Genomic DNA. Translation: ABF98423.1.
    DP000009 Genomic DNA. Translation: ABF98424.1. Sequence problems.
    DP000009 Genomic DNA. Translation: ABF98425.1. Sequence problems.
    DP000009 Genomic DNA. Translation: ABF98426.1. Sequence problems.
    AP008209 Genomic DNA. Translation: BAF12927.1.
    AK100165 mRNA. Translation: BAG94472.1.
    PIRiT03296.
    RefSeqiNP_001051013.1. NM_001057548.1.
    UniGeneiOs.5072.

    Genome annotation databases

    EnsemblPlantsiOS03T0703000-01; OS03T0703000-01; OS03G0703000.
    GeneIDi4333841.
    KEGGiosa:4333841.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U28047 mRNA. Translation: AAA84906.3.
    AC091670 Genomic DNA. Translation: AAX95519.1.
    AC133334 Genomic DNA. Translation: AAS07254.1.
    AC133334 Genomic DNA. Translation: AAS07255.1. Sequence problems.
    DP000009 Genomic DNA. Translation: ABF98423.1.
    DP000009 Genomic DNA. Translation: ABF98424.1. Sequence problems.
    DP000009 Genomic DNA. Translation: ABF98425.1. Sequence problems.
    DP000009 Genomic DNA. Translation: ABF98426.1. Sequence problems.
    AP008209 Genomic DNA. Translation: BAF12927.1.
    AK100165 mRNA. Translation: BAG94472.1.
    PIRiT03296.
    RefSeqiNP_001051013.1. NM_001057548.1.
    UniGeneiOs.5072.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RGLX-ray2.20A/B29-504[»]
    2RGMX-ray1.55A/B29-504[»]
    3AHTX-ray2.80A/B29-504[»]
    3AHVX-ray1.75A/B29-504[»]
    3F4VX-ray1.65A/B29-504[»]
    3F5JX-ray1.95A/B29-504[»]
    3F5KX-ray1.80A/B29-504[»]
    3F5LX-ray1.37A/B29-504[»]
    3SCNX-ray2.20A/B29-504[»]
    3SCOX-ray1.95A/B29-504[»]
    3SCPX-ray2.10A/B29-504[»]
    3SCQX-ray2.10A/B29-504[»]
    3SCRX-ray1.80A/B29-504[»]
    3SCSX-ray1.85A/B29-504[»]
    3SCTX-ray1.60A/B29-504[»]
    3SCUX-ray1.58A/B29-504[»]
    3SCVX-ray2.11A/B29-504[»]
    3SCWX-ray1.90A/B29-504[»]
    ProteinModelPortaliQ75I93.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi39947.LOC_Os03g49600.1.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Proteomic databases

    PRIDEiQ75I93.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiOS03T0703000-01; OS03T0703000-01; OS03G0703000.
    GeneIDi4333841.
    KEGGiosa:4333841.

    Organism-specific databases

    GrameneiQ75I93.

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    InParanoidiQ75I93.
    KOiK05350.
    OMAiFNTLERH.

    Enzyme and pathway databases

    BRENDAi3.2.1.21. 4460.
    SABIO-RKQ75I93.

    Miscellaneous databases

    EvolutionaryTraceiQ75I93.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Oryza sativa beta-glucosidase mRNA."
      Esen A., Opassiri R., Ketudat Cairns J.R., Akiyama T.
      Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Nipponbare.
      Tissue: Root.
    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. "Beta-glucosidase, exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlu1."
      Opassiri R., Hua Y., Wara-Aswapati O., Akiyama T., Svasti J., Esen A., Ketudat Cairns J.R.
      Biochem. J. 379:125-131(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "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.
    8. "Rice family GH1 glycoside hydrolases with beta-D-glucosidase and beta-D-mannosidase activities."
      Kuntothom T., Luang S., Harvey A.J., Fincher G.B., Opassiri R., Hrmova M., Ketudat Cairns J.R.
      Arch. Biochem. Biophys. 491:85-95(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Structural insights into rice BGlu1 beta-glucosidase oligosaccharide hydrolysis and transglycosylation."
      Chuenchor W., Pengthaisong S., Robinson R.C., Yuvaniyama J., Oonanant W., Bevan D.R., Esen A., Chen C.J., Opassiri R., Svasti J., Cairns J.R.
      J. Mol. Biol. 377:1200-1215(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 29-504 IN COMPLEX WITH ZINC IONS AND SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ILE-207; ASN-218; ASN-273 AND LEU-470.

    Entry informationi

    Entry nameiBGL07_ORYSJ
    AccessioniPrimary (citable) accession number: Q75I93
    Secondary accession number(s): Q10EB0
    , Q10EB1, Q10EB2, Q42975, Q75I92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: July 5, 2004
    Last modified: June 24, 2015
    This is version 78 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.