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BGL29_ORYSJ
ID   BGL29_ORYSJ             Reviewed;         494 AA.
AC   A3C053; A0A0P0XNI9; Q0J0P0;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Beta-glucosidase 29;
DE            Short=Os9bglu29;
DE            EC=3.2.1.21;
DE   Flags: Precursor;
GN   Name=BGLU29; OrderedLocusNames=Os09g0490400, LOC_Os09g31410;
GN   ORFNames=OsJ_29835;
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).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF25452.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAZ45192.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP008215; BAF25452.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014965; BAT08726.1; -; Genomic_DNA.
DR   EMBL; CM000146; EAZ45192.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A3C053; -.
DR   SMR; A3C053; -.
DR   STRING; 4530.OS09T0490400-00; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PRIDE; A3C053; -.
DR   EnsemblPlants; Os09t0490400-00; Os09t0490400-00; Os09g0490400.
DR   Gramene; Os09t0490400-00; Os09t0490400-00; Os09g0490400.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; A3C053; -.
DR   OMA; DMFRIME; -.
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000007752; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
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   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
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.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..494
FT                   /note="Beta-glucosidase 29"
FT                   /id="PRO_0000390346"
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        398
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         447
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         454..455
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        203..211
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  56153 MW;  E090F33B47BD0FD4 CRC64;
     MAWLGIGMGR QIVPVLVFVA VLCSGVDASF NRYSFPKDFI FGTGSAAYQY EGAAKEGGKI
     LNGDTGDVAD DFYHRYKEDV NLLKDMNMDA FRFSISWSRI LPNGTLSGGV NKEGVAFYNN
     LINEIIAKGM KPFVTIFHWD TPQALESKYG GFLSENIIKD YVDFAEVCFR EFGDRVKFWA
     TFNEPWTYCS QGYGTGIHAL GRCSPYVSTS CAGGDSSREP YLAAHHVILA HATAVHLYRT
     KYQPTQHGQI GITAVSHWFV PYNDTAADRR VVQRSLDFMY GWFLDPIVHG DYPGTMRGWL
     GARLPAFTAE QAAAVRGSYD FIGVNYYTTY YAKSVPLPSS NRLSYDTDIR ANTTGFRNGK
     PIGPQEFTPI FFNYPPGLRE LLLYTKRRYN NPIIYVTENG IAEGNNKSLP ITEALKDGHR
     IEFHSKHLQF VNHAIKNGVN VKGYFTWTFM DCFEWGDGYL DRFGLIYIDR LNNLKRYHKQ
     SSYWIANFLK RKKY
 
 
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