ID BGL32_ORYSJ Reviewed; 508 AA. AC Q0J0G2; DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2009, sequence version 2. DT 24-JAN-2024, entry version 95. DE RecName: Full=Beta-glucosidase 32; DE Short=Os9bglu32; DE EC=3.2.1.21 {ECO:0000250|UniProtKB:Q75I94}; DE Flags: Precursor; GN Name=BGLU32; OrderedLocusNames=Os09g0511700, LOC_Os09g33690; 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 MRNA] (ISOFORM 2). RC STRAIN=cv. Nipponbare; RX PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). 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 Evidence={ECO:0000250|UniProtKB:Q75I94}; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q0J0G2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q0J0G2-2; Sequence=VSP_038514, VSP_038515; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {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; AP008215; BAF25553.1; -; Genomic_DNA. DR EMBL; AP014965; BAT08914.1; -; Genomic_DNA. DR EMBL; AK101420; BAG95059.1; -; mRNA. DR RefSeq; XP_015612589.1; XM_015757103.1. DR AlphaFoldDB; Q0J0G2; -. DR SMR; Q0J0G2; -. DR STRING; 39947.Q0J0G2; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR GlyCosmos; Q0J0G2; 2 sites, No reported glycans. DR PaxDb; 39947-Q0J0G2; -. DR EnsemblPlants; Os09t0511700-01; Os09t0511700-01; Os09g0511700. [Q0J0G2-2] DR GeneID; 4347546; -. DR Gramene; Os09t0511700-01; Os09t0511700-01; Os09g0511700. [Q0J0G2-2] DR KEGG; osa:4347546; -. DR eggNOG; KOG0626; Eukaryota. DR InParanoid; Q0J0G2; -. DR OMA; KYQVRPA; -. DR OrthoDB; 3373839at2759; -. DR Proteomes; UP000000763; 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 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; GLYCOSYL HYDROLASE; 1. DR PANTHER; PTHR10353:SF197; INACTIVE BETA-GLUCOSIDASE 33-RELATED; 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 2: Evidence at transcript level; KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; KW Reference proteome; Signal. FT SIGNAL 1..30 FT /evidence="ECO:0000255" FT CHAIN 31..508 FT /note="Beta-glucosidase 32" FT /id="PRO_0000390349" FT ACT_SITE 196 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT ACT_SITE 404 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 50 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 150 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 195..196 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 339 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 404 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q9SPP9" FT BINDING 451 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 458..459 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q8L7J2" FT BINDING 467 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q1XH05" FT CARBOHYD 222 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 441 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 215..223 FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT VAR_SEQ 256..274 FT /note="AIQGGQIGITLLGWWYEPY -> LATGNSRRSDRDHSAGLVV (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:12869764" FT /id="VSP_038514" FT VAR_SEQ 275..508 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12869764" FT /id="VSP_038515" SQ SEQUENCE 508 AA; 56799 MW; 52256C1319709A6C CRC64; MAAGARALVP SPFIVVVFLL LAAAARDASA LTRHDFPEGF VFGAGTSAFQ VEGAAAEDGR KPSIWDTFTH QGYSPGGAIA DVSADQYHHY KEDVKLMYDM GLDAYRFSIA WPRLIPDGRG EINPKGLEYY NNLIDELIMH GIQPHVTIYH FDLPQALQDE YGGILSPRFI EDYTAYAEVC FKNFGDRVKH WVTVNEPNIE PIGGYDAGVQ PPRRCSYPFG TNCTGGDSST EPYIVAHHLL LAHASAVSIY RQKYQAIQGG QIGITLLGWW YEPYTDAVAD AAAAIRMNEF HIGWFMNPLV HGDYPPVMRS RVGARLPSIT ASDSEKIRGS FDFIGINHYF VIFVQSSDAN HDQKLRDYYV DAGVQENGGG GFDKEHYQLH PWALGKMLHH LKLKYGNPPV MIHENGDADS PETPGKIDYD DDFRSDFLQS YLEVLHLSIR NGSNTRGYFV WSLLDGFEFL SGYGNRFGLC CVDFTAPART RYVRSSARWY SDFLNGGELR PVKPFVAL //