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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.1 Publication

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)DescriptionActionsGraphical viewLength
    Binding sitei57SubstrateCombined sources3 Publications1
    Binding sitei158SubstrateCombined sources2 Publications1
    Binding sitei203SubstrateCombined sources3 Publications1
    Active sitei204Proton donor1 Publication1
    Binding sitei343SubstrateCombined sources3 Publications1
    Active sitei414Nucleophile1 Publication1
    Binding sitei461SubstrateCombined sourcesCurated1

    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
    • 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-RKQ75I93.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase 7Curated (EC:3.2.1.211 Publication)
    Short name:
    Os3bglu71 Publication
    Gene namesi
    Name:BGLU7Curated
    Synonyms:BGLU11 Publication
    Ordered Locus Names:Os03g0703000Imported, LOC_Os03g49600Imported
    ORF Names:OSJNBa0004L11.16
    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
    Mutagenesisi207I → V: Increases KM for substrate about 5-fold. Increases kcat/Km values 9 to 24-fold depending on the substrate. 2 Publications1
    Mutagenesisi218N → H: Decreases KM for substrate about 2-fold. 1 Publication1
    Mutagenesisi273N → V: Increases KM for substrate about 5-fold. 1 Publication1
    Mutagenesisi470L → R: No effect on KM. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 26Sequence analysisAdd BLAST26
    ChainiPRO_000038346127 – 504Beta-glucosidase 7Add BLAST478

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi223 ↔ 226By similarity
    Glycosylationi280N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi422N-linked (GlcNAc...)Sequence analysis1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ75I93.
    PRIDEiQ75I93.

    Expressioni

    Gene expression databases

    ExpressionAtlasiQ75I93. baseline and differential.
    GenevisibleiQ75I93. OS.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    STRINGi39947.LOC_Os03g49600.1.

    Structurei

    Secondary structure

    1504
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni34 – 37Combined sources4
    Helixi40 – 42Combined sources3
    Beta strandi48 – 52Combined sources5
    Helixi55 – 58Combined sources4
    Helixi71 – 76Combined sources6
    Helixi83 – 85Combined sources3
    Beta strandi88 – 90Combined sources3
    Helixi94 – 107Combined sources14
    Beta strandi112 – 116Combined sources5
    Helixi119 – 122Combined sources4
    Beta strandi126 – 128Combined sources3
    Helixi132 – 147Combined sources16
    Beta strandi151 – 156Combined sources6
    Helixi163 – 169Combined sources7
    Helixi171 – 173Combined sources3
    Helixi177 – 192Combined sources16
    Turni193 – 195Combined sources3
    Beta strandi198 – 203Combined sources6
    Helixi205 – 213Combined sources9
    Beta strandi223 – 225Combined sources3
    Turni232 – 234Combined sources3
    Helixi235 – 257Combined sources23
    Helixi259 – 262Combined sources4
    Beta strandi265 – 271Combined sources7
    Beta strandi274 – 281Combined sources8
    Helixi282 – 295Combined sources14
    Helixi297 – 305Combined sources9
    Helixi310 – 316Combined sources7
    Helixi317 – 319Combined sources3
    Helixi325 – 331Combined sources7
    Beta strandi336 – 341Combined sources6
    Beta strandi345 – 349Combined sources5
    Helixi361 – 364Combined sources4
    Beta strandi368 – 373Combined sources6
    Beta strandi376 – 379Combined sources4
    Helixi392 – 404Combined sources13
    Beta strandi410 – 414Combined sources5
    Beta strandi419 – 422Combined sources4
    Helixi425 – 429Combined sources5
    Helixi432 – 450Combined sources19
    Beta strandi455 – 461Combined sources7
    Helixi469 – 474Combined sources6
    Beta strandi479 – 482Combined sources4
    Turni484 – 486Combined sources3
    Beta strandi489 – 491Combined sources3
    Helixi493 – 501Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4QLJX-ray1.95A/B29-504[»]
    4QLKX-ray1.83A/B29-504[»]
    4QLLX-ray1.85A/B29-504[»]
    ProteinModelPortaliQ75I93.
    SMRiQ75I93.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ75I93.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni468 – 469Substrate bindingCombined sources3 Publications2

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG0626. Eukaryota.
    COG2723. LUCA.
    HOGENOMiHOG000088630.
    InParanoidiQ75I93.
    KOiK05350.
    OMAiCTINEPA.
    OrthoDBiEOG093606U3.

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti52A → V in AAA84906 (Ref. 1) Curated1

    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.
    AP014959 Genomic DNA. Translation: BAS85953.1.
    AK100165 mRNA. Translation: BAG94472.1.
    PIRiT03296.
    RefSeqiXP_015630897.1. XM_015775411.1.
    UniGeneiOs.5072.

    Genome annotation databases

    EnsemblPlantsiOS03T0703000-01; OS03T0703000-01; OS03G0703000.
    GeneIDi4333841.
    GrameneiOS03T0703000-01; OS03T0703000-01; OS03G0703000.
    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.
    AP014959 Genomic DNA. Translation: BAS85953.1.
    AK100165 mRNA. Translation: BAG94472.1.
    PIRiT03296.
    RefSeqiXP_015630897.1. XM_015775411.1.
    UniGeneiOs.5072.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4QLJX-ray1.95A/B29-504[»]
    4QLKX-ray1.83A/B29-504[»]
    4QLLX-ray1.85A/B29-504[»]
    ProteinModelPortaliQ75I93.
    SMRiQ75I93.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi39947.LOC_Os03g49600.1.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Proteomic databases

    PaxDbiQ75I93.
    PRIDEiQ75I93.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiOS03T0703000-01; OS03T0703000-01; OS03G0703000.
    GeneIDi4333841.
    GrameneiOS03T0703000-01; OS03T0703000-01; OS03G0703000.
    KEGGiosa:4333841.

    Phylogenomic databases

    eggNOGiKOG0626. Eukaryota.
    COG2723. LUCA.
    HOGENOMiHOG000088630.
    InParanoidiQ75I93.
    KOiK05350.
    OMAiCTINEPA.
    OrthoDBiEOG093606U3.

    Enzyme and pathway databases

    BRENDAi3.2.1.21. 4460.
    SABIO-RKQ75I93.

    Miscellaneous databases

    EvolutionaryTraceiQ75I93.

    Gene expression databases

    ExpressionAtlasiQ75I93. baseline and differential.
    GenevisibleiQ75I93. OS.

    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...

    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: November 2, 2016
    This is version 90 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.