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Database: UniProt
Entry: P26204
LinkDB: P26204
Original site: P26204 
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   19-FEB-2014, entry version 70.
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; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   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: 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:UniProtKB-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; 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;
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
//
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