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Q75I93

- BGL07_ORYSJ

UniProt

Q75I93 - BGL07_ORYSJ

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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

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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

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. extracellular region Source: UniProtKB-KW
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

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.
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

        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. 1 PublicationCurated

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 .
PIRi T03296.
RefSeqi NP_001051013.1. NM_001057548.1.
UniGenei Os.5072.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi Q75I93.
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

« 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: November 26, 2014
This is version 75 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