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   24-JAN-2024, entry version 79.
DE   RecName: Full=Beta-glucosidase 26;
DE            Short=Os7bglu26;
DE            EC=3.2.1.21 {ECO:0000269|PubMed:19766588};
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, 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 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         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=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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 39947.A3BMZ5; -.
DR   GlyCosmos; A3BMZ5; 4 sites, No reported glycans.
DR   PaxDb; 39947-A3BMZ5; -.
DR   KEGG; osa:4344146; -.
DR   InParanoid; A3BMZ5; -.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF217; BETA-GLUCOSIDASE 26; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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|UniProtKB:Q7XSK0"
FT   ACT_SITE        416
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         59
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         160
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         205..206
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         345
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         416
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         463
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         470..471
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         479
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        225..228
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
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
//