ID BGL07_ORYSJ Reviewed; 504 AA.
AC Q75I93; Q10EB0; Q10EB1; Q10EB2; Q42975; Q75I92;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-APR-2013, entry version 65.
DE RecName: Full=Beta-glucosidase 7;
DE Short=Os3bglu7;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU7; Synonyms=BGLU1;
GN OrderedLocusNames=Os03g0703000, LOC_Os03g49600;
GN ORFNames=OSJNBa0004L11.16;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC Ehrhartoideae; Oryzeae; Oryza.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare; TISSUE=Root;
RA Esen A., Opassiri R., Ketudat Cairns J.R., Akiyama T.;
RT "Oryza sativa beta-glucosidase mRNA.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R.,
RA Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L.,
RA Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S.,
RA Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S.,
RA Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J.,
RA de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H.,
RA Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F.,
RA Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A.,
RA Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J.,
RA Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L.,
RA Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A.,
RA Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W.,
RA Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome
RT 3 and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14692878; DOI=10.1042/BJ20031485;
RA Opassiri R., Hua Y., Wara-Aswapati O., Akiyama T., Svasti J., Esen A.,
RA Ketudat Cairns J.R.;
RT "Beta-glucosidase, exo-beta-glucanase and pyridoxine transglucosylase
RT activities of rice BGlu1.";
RL Biochem. J. 379:125-131(2004).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17196101; DOI=10.1186/1471-2229-6-33;
RA Opassiri R., Pomthong B., Onkoksoong T., Akiyama T., Esen A.,
RA Ketudat Cairns J.R.;
RT "Analysis of rice glycosyl hydrolase family 1 and expression of
RT Os4bglu12 beta-glucosidase.";
RL BMC Plant Biol. 6:33-33(2006).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19766588; DOI=10.1016/j.abb.2009.09.004;
RA Kuntothom T., Luang S., Harvey A.J., Fincher G.B., Opassiri R.,
RA Hrmova M., Ketudat Cairns J.R.;
RT "Rice family GH1 glycoside hydrolases with beta-D-glucosidase and
RT beta-D-mannosidase activities.";
RL Arch. Biochem. Biophys. 491:85-95(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 29-504 IN COMPLEX WITH ZINC
RP IONS AND SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND MUTAGENESIS OF ILE-207; ASN-218; ASN-273 AND LEU-470.
RX PubMed=18308333; DOI=10.1016/j.jmb.2008.01.076;
RA Chuenchor W., Pengthaisong S., Robinson R.C., Yuvaniyama J.,
RA Oonanant W., Bevan D.R., Esen A., Chen C.J., Opassiri R., Svasti J.,
RA Cairns J.R.;
RT "Structural insights into rice BGlu1 beta-glucosidase oligosaccharide
RT hydrolysis and transglycosylation.";
RL J. Mol. Biol. 377:1200-1215(2008).
CC -!- FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl
CC beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl
CC beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl
CC beta-L-arabinoside, oligosaccharides, pyridoxine beta-D-glucoside
CC and the cyanogenic glucosides amigdalin, prunasin and dhurrin.
CC Possesses pyridoxine transglucosylation activity.
CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-
CC glucosyl residues with release of beta-D-glucose.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0);
CC KM=0.23 mM for p-nitrophenyl beta-D-fucoside (at pH 5.0);
CC KM=3.2 mM for p-nitrophenyl beta-D-galactoside (at pH 5.0);
CC KM=1.3 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0);
CC KM=1.3 mM for p-nitrophenyl beta-D-xyloside (at pH 5.0);
CC KM=1.2 mM for p-nitrophenyl beta-L-arabinoside (at pH 5.0);
CC KM=0.78 mM for p-nitrophenyl beta-D-cellobioside (at pH 5.0);
CC KM=22 mM for cellobiose (at pH 5.0);
CC KM=0.22 mM for cellotriose (at pH 5.0);
CC KM=0.28 mM for cellotetraose (at pH 5.0);
CC KM=0.24 mM for cellopentaose (at pH 5.0);
CC KM=0.22 mM for cellohexaose (at pH 5.0);
CC KM=2.05 mM for laminaribiose (at pH 5.0);
CC KM=1.92 mM for laminaritriose (at pH 5.0);
CC KM=13.9 mM for sophorose (at pH 5.0);
CC KM=38.3 mM for gentiobiose (at pH 5.0);
CC -!- SUBUNIT: Homodimer. Formation of the homodimer is zinc-dependent.
CC Dimerization does not increase activity.
CC -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS07255.1; Type=Erroneous gene model prediction;
CC Sequence=ABF98424.1; Type=Erroneous gene model prediction;
CC Sequence=ABF98425.1; Type=Erroneous gene model prediction;
CC Sequence=ABF98426.1; Type=Erroneous gene model prediction;
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DR EMBL; U28047; AAA84906.3; -; mRNA.
DR EMBL; AC091670; AAX95519.1; -; Genomic_DNA.
DR EMBL; AC133334; AAS07254.1; -; Genomic_DNA.
DR EMBL; AC133334; AAS07255.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF98423.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98424.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF98425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF98426.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008209; BAF12927.1; -; Genomic_DNA.
DR EMBL; AK100165; BAG94472.1; -; mRNA.
DR PIR; T03296; T03296.
DR RefSeq; NP_001051013.1; NM_001057548.1.
DR UniGene; Os.5072; -.
DR PDB; 2RGL; X-ray; 2.20 A; A/B=29-504.
DR PDB; 2RGM; X-ray; 1.55 A; A/B=29-504.
DR PDB; 3AHT; X-ray; 2.80 A; A/B=29-504.
DR PDB; 3AHV; X-ray; 1.75 A; A/B=29-504.
DR PDB; 3F4V; X-ray; 1.65 A; A/B=29-504.
DR PDB; 3F5J; X-ray; 1.95 A; A/B=29-504.
DR PDB; 3F5K; X-ray; 1.80 A; A/B=29-504.
DR PDB; 3F5L; X-ray; 1.37 A; A/B=29-504.
DR PDB; 3SCN; X-ray; 2.20 A; A/B=29-504.
DR PDB; 3SCO; X-ray; 1.95 A; A/B=29-504.
DR PDB; 3SCP; X-ray; 2.10 A; A/B=29-504.
DR PDB; 3SCQ; X-ray; 2.10 A; A/B=29-504.
DR PDB; 3SCR; X-ray; 1.80 A; A/B=29-504.
DR PDB; 3SCS; X-ray; 1.85 A; A/B=29-504.
DR PDB; 3SCT; X-ray; 1.60 A; A/B=29-504.
DR PDB; 3SCU; X-ray; 1.58 A; A/B=29-504.
DR PDB; 3SCV; X-ray; 2.11 A; A/B=29-504.
DR PDB; 3SCW; X-ray; 1.90 A; A/B=29-504.
DR PDBsum; 2RGL; -.
DR PDBsum; 2RGM; -.
DR PDBsum; 3AHT; -.
DR PDBsum; 3AHV; -.
DR PDBsum; 3F4V; -.
DR PDBsum; 3F5J; -.
DR PDBsum; 3F5K; -.
DR PDBsum; 3F5L; -.
DR PDBsum; 3SCN; -.
DR PDBsum; 3SCO; -.
DR PDBsum; 3SCP; -.
DR PDBsum; 3SCQ; -.
DR PDBsum; 3SCR; -.
DR PDBsum; 3SCS; -.
DR PDBsum; 3SCT; -.
DR PDBsum; 3SCU; -.
DR PDBsum; 3SCV; -.
DR PDBsum; 3SCW; -.
DR ProteinModelPortal; Q75I93; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PRIDE; Q75I93; -.
DR EnsemblPlants; LOC_Os03g49600.1; LOC_Os03g49600.1; LOC_Os03g49600.
DR GeneID; 4333841; -.
DR KEGG; dosa:Os03t0703000-01; -.
DR KEGG; osa:4333841; -.
DR Gramene; Q75I93; -.
DR eggNOG; COG2723; -.
DR HOGENOM; HOG000088630; -.
DR KO; K05350; -.
DR OMA; NTINEPY; -.
DR ProtClustDB; CLSN2694209; -.
DR SABIO-RK; Q75I93; -.
DR EvolutionaryTrace; Q75I93; -.
DR ArrayExpress; Q75I93; -.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:EnsemblPlants/Gramene.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IEA:EnsemblPlants/Gramene.
DR GO; GO:0080081; F:4-methylumbelliferyl-beta-D-glucopyranoside beta-glucosidase activity; IEA:EnsemblPlants/Gramene.
DR GO; GO:0047668; F:amygdalin beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0033907; F:beta-D-fucosidase activity; IDA:UniProtKB.
DR GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0080083; F:beta-gentiobiose beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0047701; F:beta-L-arabinosidase activity; IDA:UniProtKB.
DR GO; GO:0004567; F:beta-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0080079; F:cellobiose glucosidase activity; IDA:UniProtKB.
DR GO; GO:0080082; F:esculin beta-glucosidase activity; IEA:EnsemblPlants/Gramene.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0050224; F:prunasin beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; -; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; Glyco_hydro_cat; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; FALSE_NEG.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Metal-binding; Reference proteome; Secreted;
KW Signal; Zinc.
FT SIGNAL 1 26 Potential.
FT CHAIN 27 504 Beta-glucosidase 7.
FT /FTId=PRO_0000383461.
FT REGION 468 469 Substrate binding.
FT ACT_SITE 204 204 Proton donor (By similarity).
FT ACT_SITE 414 414 Nucleophile (By similarity).
FT METAL 93 93 Zinc; shared with dimeric partner.
FT METAL 96 96 Zinc; shared with dimeric partner.
FT BINDING 57 57 Substrate.
FT BINDING 158 158 Substrate.
FT BINDING 203 203 Substrate.
FT BINDING 343 343 Substrate.
FT BINDING 461 461 Substrate.
FT CARBOHYD 280 280 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 422 422 N-linked (GlcNAc...) (Potential).
FT DISULFID 223 226 By similarity.
FT MUTAGEN 207 207 I->V: Increases KM for substrate about 5-
FT fold.
FT MUTAGEN 218 218 N->H: Decreases KM for substrate about 2-
FT fold.
FT MUTAGEN 273 273 N->V: Increases KM for substrate about 5-
FT fold.
FT MUTAGEN 470 470 L->R: No effect on KM.
FT CONFLICT 52 52 A -> V (in Ref. 1; AAA84906).
FT TURN 34 37
FT HELIX 40 42
FT STRAND 48 52
FT HELIX 55 58
FT HELIX 71 76
FT HELIX 83 85
FT STRAND 88 90
FT HELIX 94 107
FT STRAND 112 116
FT HELIX 119 122
FT STRAND 126 128
FT HELIX 132 147
FT STRAND 151 156
FT HELIX 163 169
FT HELIX 171 173
FT HELIX 177 192
FT TURN 193 195
FT STRAND 198 203
FT HELIX 205 213
FT TURN 232 234
FT HELIX 235 257
FT HELIX 259 262
FT STRAND 265 271
FT STRAND 274 281
FT HELIX 282 295
FT HELIX 297 305
FT HELIX 310 316
FT HELIX 317 319
FT HELIX 325 331
FT STRAND 336 341
FT STRAND 345 349
FT HELIX 361 364
FT STRAND 368 373
FT STRAND 376 379
FT HELIX 392 404
FT STRAND 410 414
FT STRAND 419 422
FT HELIX 425 429
FT HELIX 432 450
FT STRAND 455 461
FT HELIX 469 474
FT STRAND 479 482
FT TURN 484 486
FT STRAND 489 491
FT HELIX 493 501
SQ SEQUENCE 504 AA; 56872 MW; 4C36D2A5AF452CE9 CRC64;
MAARRANCAL VLVLALALLA ARDAGAAAVP KPNWLGGLSR AAFPKRFVFG TATSAYQVEG
MAASGGRGPS IWDAFAHTPG NVAGNQNGDV ATDQYHRYKE DVNLMKSLNF DAYRFSISWS
RIFPDGEGRV NQEGVAYYNN LINYLLQKGI TPYVNLYHYD LPLALEKKYG GWLNAKMADL
FTEYADFCFK TFGNRVKHWF TFNEPRIVAL LGYDQGTNPP KRCTKCAAGG NSATEPYIVA
HNFLLSHAAA VARYRTKYQA AQQGKVGIVL DFNWYEALSN STEDQAAAQR ARDFHIGWYL
DPLINGHYPQ IMQDLVKDRL PKFTPEQARL VKGSADYIGI NQYTASYMKG QQLMQQTPTS
YSADWQVTYV FAKNGKPIGP QANSNWLYIV PWGMYGCVNY IKQKYGNPTV VITENGMDQP
ANLSRDQYLR DTTRVHFYRS YLTQLKKAID EGANVAGYFA WSLLDNFEWL SGYTSKFGIV
YVDFNTLERH PKASAYWFRD MLKH
//
