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 01-MAY-2013, entry version 68.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; Trifolieae;
OC 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: Hydrolysis of terminal, non-reducing beta-D-
CC glucosyl residues with release of beta-D-glucose.
CC -!- TISSUE SPECIFICITY: Leaves.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
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DR EMBL; X56734; CAA40058.1; -; mRNA.
DR PIR; S16581; GLJY31.
DR ProteinModelPortal; P26204; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; -; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR013781; Glyco_hydro_catalytic_dom.
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; Glyco_hydro_cat; 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;
KW Signal.
FT SIGNAL 1 18 Potential.
FT CHAIN 19 493 Non-cyanogenic beta-glucosidase.
FT /FTId=PRO_0000011764.
FT REGION 478 479 Substrate binding (By similarity).
FT ACT_SITE 204 204 Proton donor (Potential).
FT ACT_SITE 422 422 Nucleophile (By similarity).
FT BINDING 54 54 Substrate (By similarity).
FT BINDING 158 158 Substrate (By similarity).
FT BINDING 203 203 Substrate (By similarity).
FT BINDING 346 346 Substrate (By similarity).
FT BINDING 471 471 Substrate (By similarity).
FT CARBOHYD 34 34 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 335 335 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 371 371 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 412 412 N-linked (GlcNAc...) (Potential).
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
//
