Beta-glucosidase 7 precursor - Oryza sativa subsp. japonica (Rice)

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Reviewed, UniProtKB/Swiss-Prot Q75I93 (BGL07_ORYSJ)

Last modified November 24, 2009. Version 36. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Beta-glucosidase 7
      Short name=Os3bglu7
    EC=3.2.1.21

Gene names

Name:	BGLU7
Synonyms:	BGLU1
Ordered Locus Names:	Os03g0703000, LOC_Os03g49600
ORF Names:	OSJNBa0004L11.16

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

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Protein attributes

Sequence length	504 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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 amigdalin, prunasin and dhurrin. Possesses pyridoxine transglucosylation activity.
Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Subunit structure	Homodimer. Formation of the homodimer is zinc-dependent. Dimerization does not increase activity.
Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the glycosyl hydrolase 1 family.
Biophysicochemical properties	Kinetic parameters: K_M=0.2 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0) K_M=0.23 mM for p-nitrophenyl beta-D-fucoside (at pH 5.0) K_M=3.2 mM for p-nitrophenyl beta-D-galactoside (at pH 5.0) K_M=1.3 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0) K_M=1.3 mM for p-nitrophenyl beta-D-xyloside (at pH 5.0) K_M=1.2 mM for p-nitrophenyl beta-L-arabinoside (at pH 5.0) K_M=0.78 mM for p-nitrophenyl beta-D-cellobioside (at pH 5.0) K_M=22 mM for cellobiose (at pH 5.0) K_M=0.22 mM for cellotriose (at pH 5.0) K_M=0.28 mM for cellotetraose (at pH 5.0) K_M=0.24 mM for cellopentaose (at pH 5.0) K_M=0.22 mM for cellohexaose (at pH 5.0) K_M=2.05 mM for laminaribiose (at pH 5.0) K_M=1.92 mM for laminaritriose (at pH 5.0) K_M=13.9 mM for sophorose (at pH 5.0) K_M=38.3 mM for gentiobiose (at pH 5.0)
Sequence caution	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.

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Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	beta-glucosidase activity Ref.9 Inferred from direct assay. Source: UniProtKB cellobiose glucosidase activity Ref.9 Inferred from direct assay. Source: UniProtKB protein homodimerization activity Ref.9 Inferred from physical interaction. Source: UniProtKB zinc ion binding Ref.9 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

Potential

Chain

27 – 504

478

Beta-glucosidase 7

PRO_0000383461

Sites

Active site

204

Proton donor By similarity

Active site

414

Nucleophile By similarity

Metal binding

Zinc; shared with dimeric partner

Metal binding

Zinc; shared with dimeric partner

Binding site

Substrate

Binding site

203

Substrate

Binding site

414

Substrate

Binding site

468

Substrate

Binding site

469

Substrate

Amino acid modifications

Glycosylation

280

N-linked (GlcNAc...) Potential

Glycosylation

422

N-linked (GlcNAc...) Potential

Disulfide bond

223 ↔ 226

By similarity

Experimental info

Mutagenesis

207

I → V: Increases KM for substrate about 5-fold. Ref.9

Mutagenesis

218

N → H: Decreases KM for substrate about 2-fold. Ref.9

Mutagenesis

273

N → V: Increases KM for substrate about 5-fold. Ref.9

Mutagenesis

470

L → R: No effect on KM. Ref.9

Sequence conflict

A → V in AAA84906. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q75I93-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4C36D2A5AF452CE9
Show »

FASTA

504

56,872

        10         20         30         40         50         60 
MAARRANCAL VLVLALALLA ARDAGAAAVP KPNWLGGLSR AAFPKRFVFG TATSAYQVEG 

        70         80         90        100        110        120 
MAASGGRGPS IWDAFAHTPG NVAGNQNGDV ATDQYHRYKE DVNLMKSLNF DAYRFSISWS 

       130        140        150        160        170        180 
RIFPDGEGRV NQEGVAYYNN LINYLLQKGI TPYVNLYHYD LPLALEKKYG GWLNAKMADL 

       190        200        210        220        230        240 
FTEYADFCFK TFGNRVKHWF TFNEPRIVAL LGYDQGTNPP KRCTKCAAGG NSATEPYIVA 

       250        260        270        280        290        300 
HNFLLSHAAA VARYRTKYQA AQQGKVGIVL DFNWYEALSN STEDQAAAQR ARDFHIGWYL 

       310        320        330        340        350        360 
DPLINGHYPQ IMQDLVKDRL PKFTPEQARL VKGSADYIGI NQYTASYMKG QQLMQQTPTS 

       370        380        390        400        410        420 
YSADWQVTYV FAKNGKPIGP QANSNWLYIV PWGMYGCVNY IKQKYGNPTV VITENGMDQP 

       430        440        450        460        470        480 
ANLSRDQYLR DTTRVHFYRS YLTQLKKAID EGANVAGYFA WSLLDNFEWL SGYTSKFGIV 

       490        500 
YVDFNTLERH PKASAYWFRD MLKH

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Jackson S. Genome Res. 15:1284-1291(2005) [PubMed: 16109971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[3]	"The map-based sequence of the rice genome." International rice genome sequencing project (IRGSP) Nature 436:793-800(2005) [PubMed: 16100779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[4]	"Curated genome annotation of Oryza sativa ssp. japonica and comparative genome analysis with Arabidopsis thaliana." The rice annotation project (RAP) Genome Res. 17:175-183(2007) [PubMed: 17210932] [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: 12869764] [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: 14692878] [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: 17196101] [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. 0:0-0(2009) [PubMed: 19766588] [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: 18308333] [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.

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Cross-references

Sequence databases

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.

PIR

T03296.

RefSeq

NP_001051013.1.

UniGene

Os.5072

3D structure databases

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	[»]

ModBase

Search...

Genome annotation databases

GeneID

4333841.

GenomeReviews

Gene locus BGLU1 in contig AP008209_GR.

KEGG

osa:4333841.

Organism-specific databases

Gramene

Q75I93.

Phylogenomic databases

PhylomeDB

Q75I93.

Family and domain databases

InterPro

IPR001360. Glyco_hydro_1.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

PANTHER

PTHR10353. Glyco_hydro_1. 1 hit.

Pfam

PF00232. Glyco_hydro_1. 1 hit.
[Graphical view]

PRINTS

PR00131. GLHYDRLASE1.

PROSITE

PS00572. GLYCOSYL_HYDROL_F1_1. False negative.
PS00653. GLYCOSYL_HYDROL_F1_2. False negative.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

BGL07_ORYSJ

Accession

Primary (citable) accession number: Q75I93
Secondary accession number(s): Q10EB0

Q75I92

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	July 5, 2004
Last modified:	November 24, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

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