ID BGL22_ORYSJ Reviewed; 533 AA. AC Q60DX8; A0A0P0WLG6; DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=Beta-glucosidase 22; DE Short=Os5bglu22; DE EC=3.2.1.21 {ECO:0000250|UniProtKB:Q75I94}; DE Flags: Precursor; GN Name=BGLU22; OrderedLocusNames=Os05g0366600, LOC_Os05g30350; GN ORFNames=OSJNBa0090H02.10; 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=16261349; DOI=10.1007/s00438-005-0039-y; RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J., RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F., RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.; RT "A fine physical map of the rice chromosome 5."; RL Mol. Genet. Genomics 274:337-345(2005). 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=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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [6] 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}. 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; AC137618; AAV31358.1; -; Genomic_DNA. DR EMBL; AP008211; BAF17245.1; -; Genomic_DNA. DR EMBL; AP014961; BAS93647.1; -; Genomic_DNA. DR EMBL; AK071469; BAG92509.1; -; mRNA. DR RefSeq; XP_015640028.1; XM_015784542.1. DR AlphaFoldDB; Q60DX8; -. DR SMR; Q60DX8; -. DR STRING; 39947.Q60DX8; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR GlyCosmos; Q60DX8; 4 sites, No reported glycans. DR PaxDb; 39947-Q60DX8; -. DR EnsemblPlants; Os05t0366600-01; Os05t0366600-01; Os05g0366600. DR GeneID; 4338560; -. DR Gramene; Os05t0366600-01; Os05t0366600-01; Os05g0366600. DR KEGG; osa:4338560; -. DR eggNOG; KOG0626; Eukaryota. DR HOGENOM; CLU_001859_1_0_1; -. DR InParanoid; Q60DX8; -. DR OMA; NWSWINS; -. DR OrthoDB; 3373839at2759; -. DR Proteomes; UP000000763; Chromosome 5. DR Proteomes; UP000059680; Chromosome 5. 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:SF61; BETA-GLUCOSIDASE 22; 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; Q60DX8; OS. PE 2: Evidence at transcript level; KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome; KW Signal. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..533 FT /note="Beta-glucosidase 22" FT /id="PRO_0000390339" FT ACT_SITE 207 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT ACT_SITE 421 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 61 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 161 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 206..207 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q8GU20" FT BINDING 350 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 421 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 482 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q1XH05" FT CARBOHYD 41 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 238 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 435 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 226..234 FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" SQ SEQUENCE 533 AA; 59543 MW; AEFE37457D9D166B CRC64; MAVSSSTSTC SSFSLLLLLL LLAAAPWRSG EAAAAAARAL NFTRQDFPGE FVFGAGTSAY QYEGATDEDG RSPSIWDTFT HAGKMPDKST GDMGAGGYHK YKEDVKLMSD TSLEAYRFSI SWSRLIPRGR GPVNPKGLEY YNSLIDELVE RGIEIHVTLY HLDFPQILED EYHGWLSPRV IDDFTAYADV CFREFGDRVR HWTTMDEPNV LSIAAYDSGA FPPCRCSPPF GANCTAGNST VEPYVVAHNS ILAHASVTRL YRDKYQATQE GFVGMNIYSF WNYPFSSSSA DIAATQRALD FMVGWILDPL VYGDYPEIMK KKAGSRIPSF TEEQSELIRG SADFIGINHY TSVYISDASN GETVGPRDYS ADMAATFRIS RNDTPSGQFV PTRLPRDPKG LQCMLEYLRD TYQGIPVYIQ ENGFGHFGKD DDSLNDTDRV DYLSSYMGST LAALRNGANV KGYFVWSFLD VFELLAGYHS PFGLHYVDFE DPNLPRQPKL SAHWYSKFLR GEIGINIEST ISPDEHEHEH ADQ //