ID BGLT_TRIRP Reviewed; 425 AA. AC P26205; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Cyanogenic beta-glucosidase; DE EC=3.2.1.21 {ECO:0000250|UniProtKB:O64879}; DE AltName: Full=Linamarase; DE Flags: Precursor; Fragment; GN Name=LI; OS Trifolium repens (Creeping white clover). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium. OX NCBI_TaxID=3899; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 12-25 AND 125-147. RC STRAIN=S100 (EG); TISSUE=Leaf; RX PubMed=1907511; DOI=10.1007/bf00039495; RA Oxtoby E., Dunn M.A., Pancoro A., Hughes M.A.; RT "Nucleotide and derived amino acid sequence of the cyanogenic beta- RT glucosidase (linamarase) from white clover (Trifolium repens L.)."; RL Plant Mol. Biol. 17:209-219(1991). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). RX PubMed=8535788; DOI=10.1016/s0969-2126(01)00229-5; RA Barrett T., Suresh C.G., Tolley S.P., Dodson E.J., Hughes M.A.; RT "The crystal structure of a cyanogenic beta-glucosidase from white clover, RT a family 1 glycosyl hydrolase."; RL Structure 3:951-960(1995). CC -!- FUNCTION: Hydrolyzes cyanoglucosides, contributing to the release of CC hydrocyanic acid, which functions as a defense mechanism against small CC predators, when the leaf tissue is damaged. 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:O64879}; CC -!- SUBUNIT: Homodimer. CC -!- TISSUE SPECIFICITY: Leaves. 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; X56733; CAA40057.1; -; mRNA. DR PIR; S16580; GLJY14. DR PDB; 1CBG; X-ray; 2.15 A; A=12-412. DR PDBsum; 1CBG; -. DR AlphaFoldDB; P26205; -. DR SMR; P26205; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR GlyCosmos; P26205; 2 sites, No reported glycans. DR EvolutionaryTrace; P26205; -. DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC. 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:SF237; BETA-GLUCOSIDASE 16; 1. DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1. DR Pfam; PF00232; Glyco_hydro_1; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1. DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Glycosidase; Hydrolase; Signal. FT SIGNAL <1..11 FT /evidence="ECO:0000269|PubMed:1907511" FT CHAIN 12..425 FT /note="Cyanogenic beta-glucosidase" FT /id="PRO_0000011765" FT ACT_SITE 194 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT ACT_SITE 408 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 44 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q8L7J2" FT BINDING 148 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q8L7J2" FT BINDING 193..194 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q8GU20" FT BINDING 337 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q8L7J2" FT BINDING 408 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q9SPP9" FT CARBOHYD 220 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 412 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 213..221 FT /evidence="ECO:0000269|PubMed:8535788, FT ECO:0007744|PDB:1CBG" FT NON_TER 1 FT HELIX 22..24 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 27..29 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 35..39 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 42..45 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 58..65 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 67..69 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 82..95 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 107..110 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 122..137 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 141..149 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 153..159 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 167..182 FT /evidence="ECO:0007829|PDB:1CBG" FT TURN 183..185 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 188..193 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 195..203 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 215..217 FT /evidence="ECO:0007829|PDB:1CBG" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 229..251 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 253..256 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 259..265 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 268..275 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 276..289 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 291..299 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 304..310 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 319..325 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 330..335 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 339..344 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 355..358 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 361..367 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:1CBG" FT HELIX 386..398 FT /evidence="ECO:0007829|PDB:1CBG" FT STRAND 404..408 FT /evidence="ECO:0007829|PDB:1CBG" SQ SEQUENCE 425 AA; 48325 MW; 20B983B65C47A678 CRC64; LLSITTTHIH AFKPLPISFD DFSDLNRSCF APGFVFGTAS SAFQYEGAAF EDGKGPSIWD TFTHKYPEKI KDRTNGDVAI DEYHRYKEDI GIMKDMNLDA YRFSISWPRV LPKGKLSGGV NREGINYYNN LINEVLANGM QPYVTLFHWD VPQALEDEYR GFLGRNIVDD FRDYAELCFK EFGDRVKHWI TLNEPWGVSM NAYAYGTFAP GRCSDWLKLN CTGGDSGREP YLAAHYQLLA HAAAARLYKT KYQASQNGII GITLVSHWFE PASKEKADVD AAKRGLDFML GWFMHPLTKG RYPESMRYLV RKRLPKFSTE ESKELTGSFD FLGLNYYSSY YAAKAPRIPN ARPAIQTDSL INATFEHNGK PLGPMAASSW LCIYPQGIRK LLLYVKNHYN NPVIYITENG RNSSTINTVT SRIPF //