BGL06_ORYSJ
ID BGL06_ORYSJ Reviewed; 521 AA.
AC Q8L7J2; A0A0P0VUN5;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Beta-glucosidase 6 {ECO:0000305};
DE Short=Os3bglu6 {ECO:0000303|PubMed:17196101};
DE EC=3.2.1.21 {ECO:0000269|PubMed:19587102};
DE Flags: Precursor;
GN Name=BGLU6 {ECO:0000305};
GN OrderedLocusNames=Os03g0212800 {ECO:0000312|EMBL:BAF11272.1},
GN LOC_Os03g11420 {ECO:0000312|EMBL:ABF94615.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 38-521
RP IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISULFIDE BOND.
RC STRAIN=cv. Yukihikari;
RX PubMed=19587102; DOI=10.1104/pp.109.139436;
RA Seshadri S., Akiyama T., Opassiri R., Kuaprasert B., Cairns J.K.;
RT "Structural and enzymatic characterization of Os3BGlu6, a rice beta-
RT glucosidase hydrolyzing hydrophobic glycosides and (1->3)- and (1->2)-
RT linked disaccharides.";
RL Plant Physiol. 151:47-58(2009).
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., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT 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 GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
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 [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 Os4bglu12
RT beta-glucosidase.";
RL BMC Plant Biol. 6:33-33(2006).
RN [8]
RP MUTAGENESIS OF MET-284.
RX PubMed=22341501; DOI=10.1016/j.carres.2012.01.010;
RA Sansenya S., Maneesan J., Cairns J.R.;
RT "Exchanging a single amino acid residue generates or weakens a +2
RT cellooligosaccharide binding subsite in rice beta-glucosidases.";
RL Carbohydr. Res. 351:130-133(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 38-521 IN COMPLEX WITH GLUCOSE,
RP FUNCTION, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BOND, AND
RP MUTAGENESIS OF GLU-211 AND GLU-427.
RX PubMed=23811195; DOI=10.1016/j.abb.2013.06.005;
RA Hua Y., Sansenya S., Saetang C., Wakuta S., Ketudat Cairns J.R.;
RT "Enzymatic and structural characterization of hydrolysis of gibberellin A4
RT glucosyl ester by a rice beta-D-glucosidase.";
RL Arch. Biochem. Biophys. 537:39-48(2013).
CC -!- FUNCTION: Hydrolyzes glycosides, oligosaccharides and hydrophobic
CC glycosides (PubMed:19587102). Possesses gibberellin ester beta-D-
CC glucosidase activity. Can hydrolyze gibberellin A4 beta-D-glucosyl
CC ester in vitro (PubMed:23811195). {ECO:0000269|PubMed:19587102,
CC ECO:0000269|PubMed:23811195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000269|PubMed:19587102};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.3 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0)
CC {ECO:0000269|PubMed:19587102};
CC KM=0.5 mM for p-nitrophenyl beta-D-fucoside (at pH 5.0)
CC {ECO:0000269|PubMed:19587102};
CC KM=6.06 mM for p-nitrophenyl beta-D-galactoside (at pH 5.0)
CC {ECO:0000269|PubMed:19587102};
CC KM=4.5 mM for n-octyl-beta-D-glucoside (at pH 5.0)
CC {ECO:0000269|PubMed:19587102};
CC KM=5.0 mM for n-heptyl-beta-D-glucoside (at pH 5.0)
CC {ECO:0000269|PubMed:19587102};
CC KM=3.6 mM for laminaribiose (at pH 5.0)
CC {ECO:0000269|PubMed:19587102};
CC KM=8.7 mM for laminaritriose (at pH 5.0)
CC {ECO:0000269|PubMed:19587102};
CC KM=15.3 mM for cellobiose (at pH 5.0) {ECO:0000269|PubMed:19587102};
CC KM=9.8 mM for sophorose (at pH 5.0) {ECO:0000269|PubMed:19587102};
CC KM=14.9 mM for gentiobiose (at pH 5.0) {ECO:0000269|PubMed:19587102};
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:23811195};
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AY129294; AAN01354.1; -; mRNA.
DR EMBL; DP000009; ABF94615.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11272.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82933.1; -; Genomic_DNA.
DR EMBL; AK119546; BAG99682.1; -; mRNA.
DR RefSeq; XP_015628023.1; XM_015772537.1.
DR PDB; 3GNO; X-ray; 1.83 A; A=38-521.
DR PDB; 3GNP; X-ray; 1.80 A; A=38-521.
DR PDB; 3GNR; X-ray; 1.81 A; A=38-521.
DR PDB; 3WBA; X-ray; 1.90 A; A=38-521.
DR PDB; 3WBE; X-ray; 1.97 A; A=38-521.
DR PDBsum; 3GNO; -.
DR PDBsum; 3GNP; -.
DR PDBsum; 3GNR; -.
DR PDBsum; 3WBA; -.
DR PDBsum; 3WBE; -.
DR AlphaFoldDB; Q8L7J2; -.
DR SMR; Q8L7J2; -.
DR STRING; 4530.OS03T0212800-01; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q8L7J2; -.
DR PRIDE; Q8L7J2; -.
DR EnsemblPlants; Os03t0212800-01; Os03t0212800-01; Os03g0212800.
DR GeneID; 4332041; -.
DR Gramene; Os03t0212800-01; Os03t0212800-01; Os03g0212800.
DR KEGG; osa:4332041; -.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q8L7J2; -.
DR OMA; DWVYVVP; -.
DR OrthoDB; 408001at2759; -.
DR BRENDA; 3.2.1.21; 4460.
DR SABIO-RK; Q8L7J2; -.
DR EvolutionaryTrace; Q8L7J2; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q8L7J2; OS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0080079; F:cellobiose glucosidase activity; IDA:UniProtKB.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:UniProtKB.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
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; SSF51445; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..521
FT /note="Beta-glucosidase 6"
FT /id="PRO_0000387495"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:23811195"
FT ACT_SITE 427
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:23811195"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19587102,
FT ECO:0000269|PubMed:23811195, ECO:0007744|PDB:3GNP,
FT ECO:0007744|PDB:3WBA"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23811195,
FT ECO:0007744|PDB:3WBA"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19587102,
FT ECO:0000269|PubMed:23811195, ECO:0007744|PDB:3GNP,
FT ECO:0007744|PDB:3WBA"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19587102,
FT ECO:0000269|PubMed:23811195, ECO:0007744|PDB:3GNP,
FT ECO:0007744|PDB:3WBA"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19587102,
FT ECO:0000269|PubMed:23811195, ECO:0007744|PDB:3GNP,
FT ECO:0007744|PDB:3WBA"
FT BINDING 484..485
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19587102,
FT ECO:0000269|PubMed:23811195, ECO:0007744|PDB:3GNP,
FT ECO:0007744|PDB:3WBA"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 230..238
FT /evidence="ECO:0000269|PubMed:19587102,
FT ECO:0000269|PubMed:23811195"
FT MUTAGEN 211
FT /note="E->A: Decreases activity toward gibberellin A4 beta-
FT D-glucosyl ester 5-fold."
FT /evidence="ECO:0000269|PubMed:23811195"
FT MUTAGEN 211
FT /note="E->Q: Decreases activity toward gibberellin A4 beta-
FT D-glucosyl ester 10-fold."
FT /evidence="ECO:0000269|PubMed:23811195"
FT MUTAGEN 284
FT /note="M->N: Decreases the kcat/Km values 7 to 30-fold
FT depending on the substrate."
FT /evidence="ECO:0000269|PubMed:22341501"
FT MUTAGEN 427
FT /note="E->D: Decreases activity toward gibberellin A4 beta-
FT D-glucosyl ester 70-fold."
FT /evidence="ECO:0000269|PubMed:23811195"
FT MUTAGEN 427
FT /note="E->Q: Decreases activity toward gibberellin A4 beta-
FT D-glucosyl ester 200-fold."
FT /evidence="ECO:0000269|PubMed:23811195"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:3GNP"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:3GNP"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3GNP"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 246..268
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 336..342
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:3GNR"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 405..418
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 447..465
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 471..477
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 485..490
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 495..498
FT /evidence="ECO:0007829|PDB:3GNP"
FT TURN 500..504
FT /evidence="ECO:0007829|PDB:3GNP"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:3GNP"
FT HELIX 510..519
FT /evidence="ECO:0007829|PDB:3GNP"
SQ SEQUENCE 521 AA; 58539 MW; 0554435869F3BD21 CRC64;
MGRIKSSSGR CSTARLEAVA VLVVVFGVAS SSLRGCIAQQ SGGGLTRGSF PEGFVFGTAS
AAYQYEGAVK EDGRGQTIWD TFAHTFGKIT DFSNADVAVD QYHRFEEDIQ LMADMGMDAY
RFSIAWSRIY PNGVGQVNQA GIDHYNKLID ALLAKGIQPY VTLYHWDLPQ ALEDKYKGWL
DRQIVDDFAA YAETCFREFG DRVKHWITLN EPHTVAIQGY DAGLQAPGRC SVLLHLYCKA
GNSGTEPYVV AHHFILAHAA AASIYRTKYK ATQNGQLGIA FDVMWFEPMS NTTIDIEAAK
RAQEFQLGWF ADPFFFGDYP ATMRARVGER LPRFTADEAA VVKGALDFVG INHYTTYYTR
HNNTNIIGTL LNNTLADTGT VSLPFKNGKP IGDRANSIWL YIVPRGMRSL MNYVKERYNS
PPVYITENGM DDSNNPFISI KDALKDSKRI KYHNDYLTNL AASIKEDGCD VRGYFAWSLL
DNWEWAAGYS SRFGLYFVDY KDNLKRYPKN SVQWFKALLK T
