BGL08_ORYSJ
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 03-AUG-2022, entry version 103.
DE RecName: Full=Beta-glucosidase 8;
DE Short=Os3bglu8;
DE EC=3.2.1.21;
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, 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., 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 -!- 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=6.0 mM for laminaritriose (at pH 5.0)
CC {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; 4530.OS03T0703100-01; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q75I94; -.
DR PRIDE; 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; FTHRAMS; -.
DR OrthoDB; 408001at2759; -.
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 Genevisible; Q75I94; OS.
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 InterPro; IPR001360; Glyco_hydro_1.
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.
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"
FT ACT_SITE 421
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 475..476
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 230..233
FT /evidence="ECO:0000250"
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
