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Q75I93

- BGL07_ORYSJ

UniProt

Q75I93 - BGL07_ORYSJ

Protein

Beta-glucosidase 7

Gene

BGLU7

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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

    1. 4-methylumbelliferyl-beta-D-glucopyranoside beta-glucosidase activity Source: EnsemblPlants/Gramene
    2. amygdalin beta-glucosidase activity Source: UniProtKB
    3. beta-D-fucosidase activity Source: UniProtKB
    4. beta-galactosidase activity Source: UniProtKB
    5. beta-gentiobiose beta-glucosidase activity Source: UniProtKB
    6. beta-glucosidase activity Source: UniProtKB
    7. beta-L-arabinosidase activity Source: UniProtKB
    8. beta-mannosidase activity Source: UniProtKB
    9. cellobiose glucosidase activity Source: UniProtKB
    10. esculin beta-glucosidase activity Source: EnsemblPlants/Gramene
    11. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB
    12. protein homodimerization activity Source: UniProtKB
    13. prunasin beta-glucosidase activity Source: UniProtKB
    14. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza
    ProteomesiUP000000763: Chromosome 3

    Organism-specific databases

    GrameneiQ75I93.

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. cytosolic ribosome Source: EnsemblPlants/Gramene
    2. extracellular region Source: UniProtKB-SubCell
    3. plant-type cell wall Source: EnsemblPlants/Gramene

    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

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK05350.
    OMAiRDENISC.

    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

    MAARRANCAL VLVLALALLA ARDAGAAAVP KPNWLGGLSR AAFPKRFVFG    50
    TATSAYQVEG MAASGGRGPS IWDAFAHTPG NVAGNQNGDV ATDQYHRYKE 100
    DVNLMKSLNF DAYRFSISWS RIFPDGEGRV NQEGVAYYNN LINYLLQKGI 150
    TPYVNLYHYD LPLALEKKYG GWLNAKMADL FTEYADFCFK TFGNRVKHWF 200
    TFNEPRIVAL LGYDQGTNPP KRCTKCAAGG NSATEPYIVA HNFLLSHAAA 250
    VARYRTKYQA AQQGKVGIVL DFNWYEALSN STEDQAAAQR ARDFHIGWYL 300
    DPLINGHYPQ IMQDLVKDRL PKFTPEQARL VKGSADYIGI NQYTASYMKG 350
    QQLMQQTPTS YSADWQVTYV FAKNGKPIGP QANSNWLYIV PWGMYGCVNY 400
    IKQKYGNPTV VITENGMDQP ANLSRDQYLR DTTRVHFYRS YLTQLKKAID 450
    EGANVAGYFA WSLLDNFEWL SGYTSKFGIV YVDFNTLERH PKASAYWFRD 500
    MLKH 504
    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.
    The sequence ABF98424.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABF98425.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABF98426.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi T03296.
    RefSeqi NP_001051013.1. NM_001057548.1.
    UniGenei Os.5072.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RGL X-ray 2.20 A/B 29-504 [» ]
    2RGM X-ray 1.55 A/B 29-504 [» ]
    3AHT X-ray 2.80 A/B 29-504 [» ]
    3AHV X-ray 1.75 A/B 29-504 [» ]
    3F4V X-ray 1.65 A/B 29-504 [» ]
    3F5J X-ray 1.95 A/B 29-504 [» ]
    3F5K X-ray 1.80 A/B 29-504 [» ]
    3F5L X-ray 1.37 A/B 29-504 [» ]
    3SCN X-ray 2.20 A/B 29-504 [» ]
    3SCO X-ray 1.95 A/B 29-504 [» ]
    3SCP X-ray 2.10 A/B 29-504 [» ]
    3SCQ X-ray 2.10 A/B 29-504 [» ]
    3SCR X-ray 1.80 A/B 29-504 [» ]
    3SCS X-ray 1.85 A/B 29-504 [» ]
    3SCT X-ray 1.60 A/B 29-504 [» ]
    3SCU X-ray 1.58 A/B 29-504 [» ]
    3SCV X-ray 2.11 A/B 29-504 [» ]
    3SCW X-ray 1.90 A/B 29-504 [» ]
    ProteinModelPortali Q75I93.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Proteomic databases

    PRIDEi Q75I93.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi OS03T0703000-01 ; OS03T0703000-01 ; OS03G0703000 .
    GeneIDi 4333841.
    KEGGi osa:4333841.

    Organism-specific databases

    Gramenei Q75I93.

    Phylogenomic databases

    eggNOGi COG2723.
    HOGENOMi HOG000088630.
    KOi K05350.
    OMAi RDENISC.

    Enzyme and pathway databases

    SABIO-RK Q75I93.

    Miscellaneous databases

    EvolutionaryTracei Q75I93.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 73 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