ID   BGL08_ORYSJ             Reviewed;         568 AA.
AC   Q75I94; A0A0P0W1Y4; Q53RI4;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Beta-glucosidase 8;
DE            Short=Os3bglu8;
DE            EC=3.2.1.21 {ECO:0000269|PubMed:19766588};
DE   Flags: Precursor;
GN   Name=BGLU8; OrderedLocusNames=Os03g0703100, LOC_Os03g49610;
GN   ORFNames=OsJ_12263, OSJNBa0004L11.15;
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 [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   [2]
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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX   PubMed=19766588; DOI=10.1016/j.abb.2009.09.004;
RA   Kuntothom T., Luang S., Harvey A.J., Fincher G.B., Opassiri R., Hrmova M.,
RA   Ketudat Cairns J.R.;
RT   "Rice family GH1 glycoside hydrolases with beta-D-glucosidase and beta-D-
RT   mannosidase activities.";
RL   Arch. Biochem. Biophys. 491:85-95(2009).
CC   -!- FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl
CC       beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-
CC       D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-
CC       arabinoside, cello-oligosaccharides, laminari-oligosaccharides,
CC       sophorose and gentiobiose. {ECO:0000269|PubMed:19766588}.
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:19766588};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.27 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0)
CC         {ECO:0000269|PubMed:19766588};
CC         KM=1.6 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0)
CC         {ECO:0000269|PubMed:19766588};
CC         KM=26 mM for cellobiose (at pH 5.0) {ECO:0000269|PubMed:19766588};
CC         KM=0.56 mM for cellotriose (at pH 5.0) {ECO:0000269|PubMed:19766588};
CC         KM=0.25 mM for cellotetraose (at pH 5.0)
CC         {ECO:0000269|PubMed:19766588};
CC         KM=0.15 mM for cellopentaose (at pH 5.0)
CC         {ECO:0000269|PubMed:19766588};
CC         KM=0.12 mM for cellohexaose (at pH 5.0)
CC         {ECO:0000269|PubMed:19766588};
CC         KM=0.32 mM for laminaribiose (at pH 5.0)
CC         {ECO:0000269|PubMed:19766588};
CC         KM=6 mM for laminaritriose (at pH 5.0) {ECO:0000269|PubMed:19766588};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX95520.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC091670; AAX95520.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC133334; AAS07251.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF98427.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF12928.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS85955.1; -; Genomic_DNA.
DR   EMBL; CM000140; EEE59768.1; -; Genomic_DNA.
DR   EMBL; AK120790; BAH00173.1; -; mRNA.
DR   RefSeq; XP_015630330.1; XM_015774844.1.
DR   AlphaFoldDB; Q75I94; -.
DR   SMR; Q75I94; -.
DR   STRING; 39947.Q75I94; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q75I94; 2 sites, No reported glycans.
DR   PaxDb; 39947-Q75I94; -.
DR   EnsemblPlants; Os03t0703100-01; Os03t0703100-01; Os03g0703100.
DR   GeneID; 4333842; -.
DR   Gramene; Os03t0703100-01; Os03t0703100-01; Os03g0703100.
DR   KEGG; osa:4333842; -.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q75I94; -.
DR   OMA; QYNFERN; -.
DR   OrthoDB; 339053at2759; -.
DR   SABIO-RK; Q75I94; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000007752; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   ExpressionAtlas; Q75I94; baseline and differential.
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: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:0004338; F:glucan exo-1,3-beta-glucosidase activity; 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; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF69; BETA-GLUCOSIDASE 8; 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   Genevisible; Q75I94; OS.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..568
FT                   /note="Beta-glucosidase 8"
FT                   /id="PRO_0000390325"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   ACT_SITE        421
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         64
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         165
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         210..211
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         350
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         421
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         468
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         475..476
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         484
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        230..233
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ   SEQUENCE   568 AA;  63098 MW;  67F1C9B4B9E22F6D CRC64;
     MGCAPAAHYL PGGGWRRLLV VVVALVVLDR AGARVRAADD DTGGLSRAAF PKGFVFGTAT
     SAFQVEGMAA SGGRGPSIWD PFVHTPGNIA GNGNADVTTD EYHRYKEDVD LLKSLNFDAY
     RFSISWSRIF PDGEGKVNTE GVAYYNNLID YVIKQGLIPY VNLNHYDLPL ALQKKYEGWL
     SPKIVGVFSD YAEFCFKTYG DRVKNWFTFN EPRIVAALGH DTGTDPPNRC TKCAAGGNSA
     TEPYIVAHNI ILSHATAVDR YRNKFQASQK GKIGIVLDFN WYEPLTNSTE DQAAAQRARD
     FHVGWFLDPL INGQYPKNMR DIVKERLPTF TPEQAKLVKG SADYFGINQY TANYMADQPA
     PQQAATSYSS DWHVSFIFQR NGVPIGQQAN SNWLYIVPTG MYGAVNYIKE KYNNPTIIIS
     ENGMDQSGNL TREEFLHDTE RIEFYKNYLT ELKKAIDDGA NVVAYFAWSL LDNFEWLSGY
     TSKFGIVYVD FTTLKRYPKD SANWFKNMLQ ASGPGSKSGS GTSDSQVGSA TSASHPVGSA
     ISSSHRLLLP LLVSLHFLFP SFFMFLSL
//