BGLS_TRIRP
ID BGLS_TRIRP Reviewed; 493 AA.
AC P26204;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Non-cyanogenic beta-glucosidase;
DE EC=3.2.1.21;
DE Flags: Precursor;
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 135-157.
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).
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 -!- TISSUE SPECIFICITY: Leaves.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; X56734; CAA40058.1; -; mRNA.
DR PIR; S16581; GLJY31.
DR AlphaFoldDB; P26204; -.
DR SMR; P26204; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
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 PRINTS; PR00131; GLHYDRLASE1.
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 Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..493
FT /note="Non-cyanogenic beta-glucosidase"
FT /id="PRO_0000011764"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 422
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 478..479
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 493 AA; 55960 MW; B6B3BAA5BBFFCB8F CRC64;
MDFIVAIFAL FVISSFTITS TNAVEASTLL DIGNLSRSSF PRGFIFGAGS SAYQFEGAVN
EGGRGPSIWD TFTHKYPEKI RDGSNADITV DQYHRYKEDV GIMKDQNMDS YRFSISWPRI
LPKGKLSGGI NHEGIKYYNN LINELLANGI QPFVTLFHWD LPQVLEDEYG GFLNSGVIND
FRDYTDLCFK EFGDRVRYWS TLNEPWVFSN SGYALGTNAP GRCSASNVAK PGDSGTGPYI
VTHNQILAHA EAVHVYKTKY QAYQKGKIGI TLVSNWLMPL DDNSIPDIKA AERSLDFQFG
LFMEQLTTGD YSKSMRRIVK NRLPKFSKFE SSLVNGSFDF IGINYYSSSY ISNAPSHGNA
KPSYSTNPMT NISFEKHGIP LGPRAASIWI YVYPYMFIQE DFEIFCYILK INITILQFSI
TENGMNEFND ATLPVEEALL NTYRIDYYYR HLYYIRSAIR AGSNVKGFYA WSFLDCNEWF
AGFTVRFGLN FVD