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   27-MAR-2024, entry version 128.
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 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; 39947.Q8L7J2; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q8L7J2; 3 sites, No reported glycans.
DR   PaxDb; 39947-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; YGGWGSR; -.
DR   OrthoDB; 3373839at2759; -.
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   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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF313; BETA-GLUCOSIDASE 6; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   Genevisible; Q8L7J2; OS.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..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="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:19587102,
FT                   ECO:0000305|PubMed:23811195, ECO:0007744|PDB:3GNP,
FT                   ECO:0007744|PDB:3WBA"
FT   BINDING         165
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:23811195,
FT                   ECO:0007744|PDB:3WBA"
FT   BINDING         210..211
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:19587102,
FT                   ECO:0000305|PubMed:23811195, ECO:0007744|PDB:3GNP,
FT                   ECO:0007744|PDB:3WBA"
FT   BINDING         354
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:19587102,
FT                   ECO:0000305|PubMed:23811195, ECO:0007744|PDB:3GNP,
FT                   ECO:0007744|PDB:3WBA"
FT   BINDING         427
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         477
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:19587102,
FT                   ECO:0000305|PubMed:23811195, ECO:0007744|PDB:3GNP,
FT                   ECO:0007744|PDB:3WBA"
FT   BINDING         484..485
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:19587102,
FT                   ECO:0000305|PubMed:23811195, ECO:0007744|PDB:3GNP,
FT                   ECO:0007744|PDB:3WBA"
FT   BINDING         493
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        230..238
FT                   /evidence="ECO:0000269|PubMed:19587102,
FT                   ECO:0000269|PubMed:23811195, ECO:0007744|PDB:3GNO,
FT                   ECO:0007744|PDB:3GNP, ECO:0007744|PDB:3GNR,
FT                   ECO:0007744|PDB:3WBA, ECO:0007744|PDB:3WBE"
FT   MUTAGEN         211
FT                   /note="E->A: Decreases activity toward gibberellin A4
FT                   beta-D-glucosyl ester 5-fold."
FT                   /evidence="ECO:0000269|PubMed:23811195"
FT   MUTAGEN         211
FT                   /note="E->Q: Decreases activity toward gibberellin A4
FT                   beta-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
FT                   beta-D-glucosyl ester 70-fold."
FT                   /evidence="ECO:0000269|PubMed:23811195"
FT   MUTAGEN         427
FT                   /note="E->Q: Decreases activity toward gibberellin A4
FT                   beta-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
//