ID BGL27_ORYSJ Reviewed; 499 AA. AC Q84YK7; A0A0P0XIN7; Q7EXZ5; DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 24-JAN-2024, entry version 120. DE RecName: Full=Beta-glucosidase 27; DE Short=Os8bglu27; DE EC=3.2.1.21 {ECO:0000250|UniProtKB:Q75I94}; DE Flags: Precursor; GN Name=BGLU27; OrderedLocusNames=Os08g0509200, LOC_Os08g39860; GN ORFNames=B1168A08.29-1, B1168A08.29-2, OSJNBa0016N23.104-1, GN OSJNBa0016N23.104-2; 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=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] (ISOFORMS 1 AND 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=Q84YK7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q84YK7-2; Sequence=VSP_038511; 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; AP005816; BAD10670.1; -; Genomic_DNA. DR EMBL; AP005816; BAD10671.1; -; Genomic_DNA. DR EMBL; AP006049; BAC57391.1; -; Genomic_DNA. DR EMBL; AP006049; BAD10730.1; -; Genomic_DNA. DR EMBL; AP008214; BAF24115.1; -; Genomic_DNA. DR EMBL; AP014964; BAT06181.1; -; Genomic_DNA. DR EMBL; AP014964; BAT06182.1; -; Genomic_DNA. DR EMBL; AK067001; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK120430; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; XP_015650451.1; XM_015794965.1. DR AlphaFoldDB; Q84YK7; -. DR SMR; Q84YK7; -. DR STRING; 39947.Q84YK7; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR GlyCosmos; Q84YK7; 5 sites, No reported glycans. DR PaxDb; 39947-Q84YK7; -. DR EnsemblPlants; Os08t0509200-01; Os08t0509200-01; Os08g0509200. [Q84YK7-1] DR EnsemblPlants; Os08t0509200-02; Os08t0509200-02; Os08g0509200. [Q84YK7-2] DR GeneID; 4345995; -. DR Gramene; Os08t0509200-01; Os08t0509200-01; Os08g0509200. [Q84YK7-1] DR Gramene; Os08t0509200-02; Os08t0509200-02; Os08g0509200. [Q84YK7-2] DR KEGG; osa:4345995; -. DR eggNOG; KOG0626; Eukaryota. DR HOGENOM; CLU_001859_1_0_1; -. DR InParanoid; Q84YK7; -. DR OMA; ARAMSWN; -. DR OrthoDB; 345778at2759; -. DR Proteomes; UP000000763; Chromosome 8. DR Proteomes; UP000059680; Chromosome 8. 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:SF65; BETA-GLUCOSIDASE 27; 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. DR Genevisible; Q84YK7; OS. PE 2: Evidence at transcript level; KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; KW Reference proteome; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..499 FT /note="Beta-glucosidase 27" FT /id="PRO_0000390344" FT ACT_SITE 192 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT ACT_SITE 407 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 43 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 146 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 191..192 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 335 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 407 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q9SPP9" FT BINDING 456 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 463..464 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 472 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q1XH05" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 361 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 408 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 414 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 415 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 211..219 FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT VAR_SEQ 446..499 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12869764" FT /id="VSP_038511" FT CONFLICT 401 FT /note="P -> T (in Ref. 4; AK067001)" FT /evidence="ECO:0000305" SQ SEQUENCE 499 AA; 56804 MW; C49FA55790C20566 CRC64; MRWLLLALFL VALVSNGAAV HGAFNRFSFP EDFIFGTGSA AYQYEGAVNE GGRGPSIWDT YAHIPGKVED GSNGDVAVDF YHRYKEDLNF VTDMNMDAFR FSIAWSRILP NGTISGGINK EGIAFYNSLI NEVISRGLKP FVTIFHFDTP QALEDKYRSF LSENIVKDFV DYADVCFREF GDRVKSWNTF NEPMIFCAGG YGSGTKAPGR CSPYVSKKCA PGDSGNEPYV AGHNLLLAHA EAVRLYRQKY QATQKGQIGI TQVSHWFVPY SDAAADKHAV RRSLDFMYGW FMDPIVFGDY PGTMRKLVGD RLPKFTAEQS ELVKGSYDFI GLNYYTTNYA KSVLRRPSKL KPAYATDNWV NQTAYRNGVP IGPPAFTKIF FTYAPGLREL LLYTKRKYND PDIYIAENGT DEANNSTIPI AEALKDDNRI SFHYQHLRFT QLAIKEGVKV KGYFTWTFMD DFEWGDGYTG RFGLIYVDRE TLKRYRKKSS YWFADFLKR //