Q75I93 (BGL07_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza › Oryza sativa

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

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. Ref.6 Ref.8 Ref.9
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: KM=0.2 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0) Ref.6 Ref.8 Ref.9 KM=0.23 mM for p-nitrophenyl beta-D-fucoside (at pH 5.0) KM=3.2 mM for p-nitrophenyl beta-D-galactoside (at pH 5.0) KM=1.3 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0) KM=1.3 mM for p-nitrophenyl beta-D-xyloside (at pH 5.0) KM=1.2 mM for p-nitrophenyl beta-L-arabinoside (at pH 5.0) KM=0.78 mM for p-nitrophenyl beta-D-cellobioside (at pH 5.0) KM=22 mM for cellobiose (at pH 5.0) KM=0.22 mM for cellotriose (at pH 5.0) KM=0.28 mM for cellotetraose (at pH 5.0) KM=0.24 mM for cellopentaose (at pH 5.0) KM=0.22 mM for cellohexaose (at pH 5.0) KM=2.05 mM for laminaribiose (at pH 5.0) KM=1.92 mM for laminaritriose (at pH 5.0) KM=13.9 mM for sophorose (at pH 5.0) KM=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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosolic ribosome Inferred from electronic annotation. Source: EnsemblPlants/Gramene extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell plant-type cell wall Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Molecular_function	4-methylumbelliferyl-beta-D-glucopyranoside beta-glucosidase activity Inferred from electronic annotation. Source: EnsemblPlants/Gramene amygdalin beta-glucosidase activity Inferred from direct assay Ref.6. Source: UniProtKB beta-D-fucosidase activity Inferred from direct assay Ref.6. Source: UniProtKB beta-L-arabinosidase activity Inferred from direct assay Ref.6. Source: UniProtKB beta-galactosidase activity Inferred from direct assay Ref.6. Source: UniProtKB beta-gentiobiose beta-glucosidase activity Inferred from direct assay Ref.6. Source: UniProtKB beta-mannosidase activity Inferred from direct assay Ref.6. Source: UniProtKB cellobiose glucosidase activity Inferred from direct assay Ref.9. Source: UniProtKB esculin beta-glucosidase activity Inferred from electronic annotation. Source: EnsemblPlants/Gramene glucan endo-1,3-beta-D-glucosidase activity Inferred from direct assay Ref.6. Source: UniProtKB prunasin beta-glucosidase activity Inferred from direct assay Ref.6. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 504

478

Beta-glucosidase 7

PRO_0000383461

Regions

Region

468 – 469

2

Substrate binding

Sites

Active site

204

1

Proton donor By similarity

Active site

414

1

Nucleophile By similarity

Metal binding

93

1

Zinc; shared with dimeric partner

Metal binding

96

1

Zinc; shared with dimeric partner

Binding site

57

1

Substrate

Binding site

158

1

Substrate

Binding site

203

1

Substrate

Binding site

343

1

Substrate

Binding site

461

1

Substrate

Amino acid modifications

Glycosylation

280

1

N-linked (GlcNAc...) Potential

Glycosylation

422

1

N-linked (GlcNAc...) Potential

Disulfide bond

223 ↔ 226

By similarity

Experimental info

Mutagenesis

207

1

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

Mutagenesis

218

1

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

Mutagenesis

273

1

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

Mutagenesis

470

1

L → R: No effect on KM. Ref.9

Sequence conflict

52

1

A → V in AAA84906. Ref.1

Secondary structure

1

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504

Helix Strand Turn

Details...

Turn

34 – 37

4

Helix

40 – 42

3

Beta strand

48 – 52

5

Helix

55 – 58

4

Helix

71 – 76

6

Helix

83 – 85

3

Beta strand

88 – 90

3

Helix

94 – 107

14

Beta strand

112 – 116

5

Helix

119 – 122

4

Beta strand

126 – 128

3

Helix

132 – 147

16

Beta strand

151 – 156

6

Helix

163 – 169

7

Helix

171 – 173

3

Helix

177 – 192

16

Turn

193 – 195

3

Beta strand

198 – 203

6

Helix

205 – 213

9

Turn

232 – 234

3

Helix

235 – 257

23

Helix

259 – 262

4

Beta strand

265 – 271

7

Beta strand

274 – 281

8

Helix

282 – 295

14

Helix

297 – 305

9

Helix

310 – 316

7

Helix

317 – 319

3

Helix

325 – 331

7

Beta strand

336 – 341

6

Beta strand

345 – 349

5

Helix

361 – 364

4

Beta strand

368 – 373

6

Beta strand

376 – 379

4

Helix

392 – 404

13

Beta strand

410 – 414

5

Beta strand

419 – 422

4

Helix

425 – 429

5

Helix

432 – 450

19

Beta strand

455 – 461

7

Helix

469 – 474

6

Beta strand

479 – 482

4

Turn

484 – 486

3

Beta strand

489 – 491

3

Helix

493 – 501

9

Sequences

	Sequence		Length	Mass (Da)
	Q75I93 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4C36D2A5AF452CE9	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

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. , 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]	"The map-based sequence of the rice genome." International rice genome sequencing project (IRGSP) Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_001057548.1.

UniGene

Os.5072.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q75I93.

ModBase

Search...

Protein family/group databases

CAZy

GH1. Glycoside Hydrolase Family 1.

Proteomic databases

PRIDE

Q75I93.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

LOC_Os03g49600.1; LOC_Os03g49600.1; LOC_Os03g49600.

GeneID

4333841.

KEGG

dosa:Os03t0703000-01.
osa:4333841.

Organism-specific databases

Gramene

Q75I93.

Phylogenomic databases

eggNOG

COG2723.

HOGENOM

HOG000088630.

KO

K05350.

OMA

NTINEPY.

ProtClustDB

CLSN2694209.

Enzyme and pathway databases

SABIO-RK

Q75I93.

Gene expression databases

ArrayExpress

Q75I93.

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR001360. Glyco_hydro_1.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

PANTHER

PTHR10353. PTHR10353. 1 hit.

Pfam

PF00232. Glyco_hydro_1. 1 hit.
[Graphical view]

PRINTS

PR00131. GLHYDRLASE1.

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

Q75I93.

Entry information

Entry name

BGL07_ORYSJ

Accession

Primary (citable) accession number: Q75I93
Secondary accession number(s): Q10EB0 , Q10EB1, Q10EB2, Q42975, Q75I92

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program