ID   BGL11_ORYSJ             Reviewed;         529 AA.
AC   Q7XKV5;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Beta-glucosidase 11;
DE            Short=Os4bglu11;
DE            EC=3.2.1.21 {ECO:0000250|UniProtKB:Q75I94};
DE   Flags: Precursor;
GN   Name=BGLU11;
GN   OrderedLocusNames=Os04g0474700, Os04g0474600, LOC_Os04g39864;
GN   ORFNames=OSJNBa0022H21.2;
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=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
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=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   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).
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:0000250|UniProtKB:Q75I94};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; AL731582; CAE05482.2; -; Genomic_DNA.
DR   EMBL; AP014960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q7XKV5; -.
DR   SMR; Q7XKV5; -.
DR   STRING; 39947.Q7XKV5; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q7XKV5; 2 sites, No reported glycans.
DR   PaxDb; 39947-Q7XKV5; -.
DR   eggNOG; KOG0626; Eukaryota.
DR   InParanoid; Q7XKV5; -.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   GO; GO:0033907; F:beta-D-fucosidase activity; IEA:UniProt.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProt.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
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; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF137; BETA-GLUCOSIDASE 9-RELATED; 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   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..529
FT                   /note="Beta-glucosidase 11"
FT                   /id="PRO_0000390328"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         54
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         157
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         202..203
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         346
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         417
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         466
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         473..474
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         482
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        425
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        222..230
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ   SEQUENCE   529 AA;  59778 MW;  12A7B50F3B6B651F CRC64;
     MAVAGAMVMS GALLLLHLLA FTCVACNGGS ELPPISRRSF PKGFIFGTSS SSYQFEGGAV
     LGGRGPSIWD TFTHQSPDKI TDRSNGDVAC DSYHLYKEDV RSMKEMGMDA YRFSISWSRI
     LPSALSGGVN REGISYYNNL INELLSKGVQ PFVTLFHWDS PQALEDKYKG FLSPNIINDY
     KEYAETCFKE FGDRVKHWIT FNEPWTFCSM GYASGIMAPG RCSSWEVGKC RVGDSGREPY
     TACHHQLLAH AETVRLYKEK YQALQKGKIG IILNADWFVP LSQSKSSSDA ARRALDFMLG
     WFMDPLIRGD YPLSMRELVG NRLPEFSKEQ SGMVKGAFDF IGLNYYTSSY ADNDPPSHGH
     NNSYNTDAHA KITGSRNGIP IGPQAASFWF HIYPEGICEM LLYVKENYGN PTIYITENGV
     DEVNNKTMPL EEALKDDTRI EYYHKHLLAL LSAMRDGANV KGYFAWSLLD NFEWAEGYTV
     RFGINFVDYD DGMKRYPKNS ARWFKKFLQK SNRDGNKRLK RVAYNAFSN
//