BGL26_ORYSJ
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 03-AUG-2022, entry version 74.
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; 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=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 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 [4]
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 [5]
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 [6]
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 and
CC sophorose. {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=0.52 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0)
CC {ECO:0000269|PubMed:19766588};
CC KM=19.6 mM for cellobiose (at pH 5.0) {ECO:0000269|PubMed:19766588};
CC KM=0.52 mM for cellotriose (at pH 5.0) {ECO:0000269|PubMed:19766588};
CC KM=0.09 mM for cellotetraose (at pH 5.0)
CC {ECO:0000269|PubMed:19766588};
CC KM=0.06 mM for cellopentaose (at pH 5.0)
CC {ECO:0000269|PubMed:19766588};
CC KM=0.05 mM for cellohexaose (at pH 5.0)
CC {ECO:0000269|PubMed:19766588};
CC KM=0.86 mM for laminaribiose (at pH 5.0)
CC {ECO:0000269|PubMed:19766588};
CC KM=8.7 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=BAF22416.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP008213; BAF22416.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000144; EAZ40934.1; -; Genomic_DNA.
DR RefSeq; XP_015647146.1; XM_015791660.1.
DR RefSeq; XP_015647147.1; XM_015791661.1.
DR AlphaFoldDB; A3BMZ5; -.
DR SMR; A3BMZ5; -.
DR STRING; 4530.OS07T0656200-01; -.
DR PaxDb; A3BMZ5; -.
DR PRIDE; A3BMZ5; -.
DR KEGG; osa:4344146; -.
DR InParanoid; A3BMZ5; -.
DR OrthoDB; 408001at2759; -.
DR SABIO-RK; A3BMZ5; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR GO; GO:0033907; F:beta-D-fucosidase activity; IDA:UniProtKB.
DR GO; GO:0004565; F:beta-galactosidase 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..510
FT /note="Beta-glucosidase 26"
FT /id="PRO_0000390343"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 416
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 470..471
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 225..228
FT /evidence="ECO:0000250"
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
