BGLT_TRIRP
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 03-AUG-2022, entry version 105.
DE RecName: Full=Cyanogenic beta-glucosidase;
DE EC=3.2.1.21;
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 -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Leaves.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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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 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 InterPro; IPR001360; Glyco_hydro_1.
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 SUPFAM; SSF51445; SSF51445; 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 ACT_SITE 408
FT /note="Nucleophile"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 213..221
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
