NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 12-25 AND 125-147.
STRAIN=S100 (EG);
TISSUE=Leaf;
DOI=10.1007/BF00039495; PubMed=1907511 [NCBI, ExPASy, EBI, Israel, Japan]
Oxtoby E., Dunn M.A., Pancoro A., Hughes M.A.;
"Nucleotide and derived amino acid sequence of the cyanogenic beta-glucosidase (linamarase) from white clover (Trifolium repens L.).";
Plant Mol. Biol. 17:209-219(1991).

[2]

X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
DOI=10.1016/S0969-2126(01)00229-5; PubMed=8535788 [NCBI, ExPASy, EBI, Israel, Japan]
Barrett T., Suresh C.G., Tolley S.P., Dodson E.J., Hughes M.A.;
"The crystal structure of a cyanogenic beta-glucosidase from white clover, a family 1 glycosyl hydrolase.";
Structure 3:951-960(1995).

Comments

FUNCTION: Hydrolyzes cyanoglucosides, contributing to the release of hydrocyanic acid, which functions as a defense mechanism against small predators, when the leaf tissue is damaged.
CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
SUBUNIT: Homodimer.
TISSUE SPECIFICITY: Leaves.
SIMILARITY: Belongs to the glycosyl hydrolase 1 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X56733; CAA40057.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S16580; GLJY14.

3D structure databases

PDB

1CBG; X-ray; 2.15 A; A=12-425.

[ExPASy / RCSB / EBI]

PDBsum

1CBG; -.

ModBase

P26205.

Ontologies

GO:0008422;	Molecular function: beta-glucosidase activity (inferred from electronic annotation from EC).
GO:0043169;	Molecular function: cation binding (inferred from electronic annotation from InterPro).
GO:0005975;	Biological process: carbohydrate metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001360; Glyco_hydro_1.
IPR013781; Glyco_hydro_sub_cat.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.80; Glyco_hydro_cat; 1.

PANTHER

PTHR10353; Glyco_hydro_1; 1.

Pfam

PF00232; Glyco_hydro_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00131; GLHYDRLASE1.

PROSITE

PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PS00653; GLYCOSYL_HYDROL_F1_2; 1.

Other

P26205; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`<1 11`	`>11`
`CHAIN`	`12 425`	`414`	`Cyanogenic beta-glucosidase.`	`PRO_0000011765`
`ACT_SITE`	`194 194`		`Proton donor.`
`ACT_SITE`	`408 408`		`Nucleophile.`
`CARBOHYD`	`220 220`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`412 412`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`213 221`
`NON_TER`	`1 1`
`HELIX`	`22 24`	`3`
`HELIX`	`27 29`	`3`
`STRAND`	`35 39`	`5`
`HELIX`	`42 45`	`4`
`STRAND`	`49 51`	`3`
`HELIX`	`58 65`	`8`
`HELIX`	`67 69`	`3`
`STRAND`	`76 78`	`3`
`HELIX`	`82 95`	`14`
`STRAND`	`100 104`	`5`
`HELIX`	`107 110`	`4`
`HELIX`	`116 118`	`3`
`HELIX`	`122 137`	`16`
`STRAND`	`141 149`	`9`
`HELIX`	`153 159`	`7`
`HELIX`	`161 163`	`3`
`HELIX`	`167 182`	`16`
`TURN`	`183 185`	`3`
`STRAND`	`188 193`	`6`
`HELIX`	`195 203`	`9`
`HELIX`	`215 217`	`3`
`TURN`	`226 228`	`3`
`HELIX`	`229 251`	`23`
`HELIX`	`253 256`	`4`
`STRAND`	`259 265`	`7`
`STRAND`	`268 275`	`8`
`HELIX`	`276 289`	`14`
`HELIX`	`291 299`	`9`
`HELIX`	`304 310`	`7`
`HELIX`	`311 313`	`3`
`HELIX`	`319 325`	`7`
`STRAND`	`330 335`	`6`
`STRAND`	`339 344`	`6`
`HELIX`	`355 358`	`4`
`STRAND`	`361 367`	`7`
`STRAND`	`370 373`	`4`
`HELIX`	`386 398`	`13`
`STRAND`	`404 408`	`5`

Sequence information

Length: 425 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 48325 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 20B983B65C47A678 [This is a checksum on the sequence]

        10         20         30         40         50         60 
LLSITTTHIH AFKPLPISFD DFSDLNRSCF APGFVFGTAS SAFQYEGAAF EDGKGPSIWD 

        70         80         90        100        110        120 
TFTHKYPEKI KDRTNGDVAI DEYHRYKEDI GIMKDMNLDA YRFSISWPRV LPKGKLSGGV 

       130        140        150        160        170        180 
NREGINYYNN LINEVLANGM QPYVTLFHWD VPQALEDEYR GFLGRNIVDD FRDYAELCFK 

       190        200        210        220        230        240 
EFGDRVKHWI TLNEPWGVSM NAYAYGTFAP GRCSDWLKLN CTGGDSGREP YLAAHYQLLA 

       250        260        270        280        290        300 
HAAAARLYKT KYQASQNGII GITLVSHWFE PASKEKADVD AAKRGLDFML GWFMHPLTKG 

       310        320        330        340        350        360 
RYPESMRYLV RKRLPKFSTE ESKELTGSFD FLGLNYYSSY YAAKAPRIPN ARPAIQTDSL 

       370        380        390        400        410        420 
INATFEHNGK PLGPMAASSW LCIYPQGIRK LLLYVKNHYN NPVIYITENG RNSSTINTVT 


SRIPF

P26205 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools