ID BGL26_ORYSJ Reviewed; 510 AA.
AC A3BMZ5; Q0D407;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 01-MAY-2013, entry version 38.
DE RecName: Full=Beta-glucosidase 26;
DE Short=Os7bglu26;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU26; OrderedLocusNames=Os07g0656200, LOC_Os07g46280;
GN ORFNames=OsJ_25416;
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 [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 [2]
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 [3]
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.,
RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA 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 [4]
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 [5]
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).
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, cello-oligosaccharides, laminari-
CC oligosaccharides and sophorose.
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=0.27 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0);
CC KM=0.52 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0);
CC KM=19.6 mM for cellobiose (at pH 5.0);
CC KM=0.52 mM for cellotriose (at pH 5.0);
CC KM=0.09 mM for cellotetraose (at pH 5.0);
CC KM=0.06 mM for cellopentaose (at pH 5.0);
CC KM=0.05 mM for cellohexaose (at pH 5.0);
CC KM=0.86 mM for laminaribiose (at pH 5.0);
CC KM=8.7 mM for laminaritriose (at pH 5.0);
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF22416.1; Type=Erroneous gene model prediction;
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DR EMBL; AP008213; BAF22416.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000144; EAZ40934.1; -; Genomic_DNA.
DR RefSeq; NP_001060502.1; NM_001067037.1.
DR UniGene; Os.20617; -.
DR ProteinModelPortal; A3BMZ5; -.
DR PRIDE; A3BMZ5; -.
DR EnsemblPlants; LOC_Os07g46280.2; LOC_Os07g46280.2; LOC_Os07g46280.
DR GeneID; 4344146; -.
DR KEGG; dosa:Os07t0656200-01; -.
DR KEGG; osa:4344146; -.
DR Gramene; A3BMZ5; -.
DR eggNOG; COG2723; -.
DR SABIO-RK; A3BMZ5; -.
DR ArrayExpress; A3BMZ5; -.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:EnsemblPlants/Gramene.
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; IEA:EnsemblPlants/Gramene.
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; IEA:EnsemblPlants/Gramene.
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:0004338; F:glucan exo-1,3-beta-glucosidase activity; 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 Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Reference proteome; Signal.
FT SIGNAL 1 27 Potential.
FT CHAIN 28 510 Beta-glucosidase 26.
FT /FTId=PRO_0000390343.
FT REGION 470 471 Substrate binding (By similarity).
FT ACT_SITE 206 206 Proton donor (By similarity).
FT ACT_SITE 416 416 Nucleophile (By similarity).
FT BINDING 59 59 Substrate (By similarity).
FT BINDING 160 160 Substrate (By similarity).
FT BINDING 205 205 Substrate (By similarity).
FT BINDING 345 345 Substrate (By similarity).
FT BINDING 463 463 Substrate (By similarity).
FT CARBOHYD 87 87 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 127 127 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 233 233 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 424 424 N-linked (GlcNAc...) (Potential).
FT DISULFID 225 228 By similarity.
SQ SEQUENCE 510 AA; 58498 MW; 9EBEAE24EE62833E CRC64;
MRKFIAALRL ALAAAAHLLL TLPPAQCYWL NPEIYDAGGL SRRAFPEGFV FGTAASAYQV
EGMAKQGGRG PSIWDAFIEK PGTIPNNATA DVTVDEYHRY KEDVNIMKNM GFDAYRFSIS
WSRIFPNGTG MVNQEGVDYY NRLIDYMVKK GIKPYANLYH YDLPLALHEQ YLGWLSPNIV
EAFADYADFC FQTFGDRVKD WFTFNEPRCV AALGYDNGFH APGRCSGCDA GGNSTTEPYL
AAHHLILSHA AAVKRYREKY QLYQKGRIGI LLDFVWYEPF SDSNADRAAA QRARDFHLGW
FLDPIIHGRY PYSMLEIVKD RMPTFSDEES RMVKDSIDYV GINHYTSFYM KDPGPWNLTP
TSYQDDWHVG FAYERNGVPI GAQANSYWLY IVPWGINKAV TYVKETYGNP TMILSENGMD
QPGNVSITQG VHDTVRIRYY RNYITELKKA IDDGAKVIGY FAWSLLDNFE WRLGYTSRFG
IVYVDYKTLK RYPKDSAFWF KNMLSSKKRN
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