P26205 (BGLT_TRIRP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyanogenic beta-glucosidase
EC=3.2.1.21

Alternative name(s):
Linamarase

Gene names

Name:

LI

Organism

Trifolium repens (Creeping white clover)

Taxonomic identifier

3899 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Trifolieae › Trifolium

Protein attributes

Sequence length	425 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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-glucosyl residues with release of beta-D-glucose.
Subunit structure	Homodimer.
Tissue specificity	Leaves.
Sequence similarities	Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	beta-glucosidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

‹1 – 11

›11

Ref.1

Chain

12 – 425

414

Cyanogenic beta-glucosidase

PRO_0000011765

Sites

Active site

194

1

Proton donor

Active site

408

1

Nucleophile

Binding site

44

1

Substrate By similarity

Binding site

148

1

Substrate By similarity

Binding site

193

1

Substrate By similarity

Binding site

337

1

Substrate By similarity

Amino acid modifications

Glycosylation

220

1

N-linked (GlcNAc...) Potential

Glycosylation

412

1

N-linked (GlcNAc...) Potential

Disulfide bond

213 ↔ 221

Experimental info

Non-terminal residue

1

1

Secondary structure

1

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425

Helix Strand Turn

Details...

Helix

22 – 24

3

Helix

27 – 29

3

Beta strand

35 – 39

5

Helix

42 – 45

4

Beta strand

49 – 51

3

Helix

58 – 65

8

Helix

67 – 69

3

Beta strand

76 – 78

3

Helix

82 – 95

14

Beta strand

100 – 104

5

Helix

107 – 110

4

Helix

116 – 118

3

Helix

122 – 137

16

Beta strand

141 – 149

9

Helix

153 – 159

7

Helix

161 – 163

3

Helix

167 – 182

16

Turn

183 – 185

3

Beta strand

188 – 193

6

Helix

195 – 203

9

Helix

215 – 217

3

Turn

226 – 228

3

Helix

229 – 251

23

Helix

253 – 256

4

Beta strand

259 – 265

7

Beta strand

268 – 275

8

Helix

276 – 289

14

Helix

291 – 299

9

Helix

304 – 310

7

Helix

311 – 313

3

Helix

319 – 325

7

Beta strand

330 – 335

6

Beta strand

339 – 344

6

Helix

355 – 358

4

Beta strand

361 – 367

7

Beta strand

370 – 373

4

Helix

386 – 398

13

Beta strand

404 – 408

5

Sequences

	Sequence		Length	Mass (Da)
	P26205 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 20B983B65C47A678	FASTA	425	48,325
	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

References

[1]	"Nucleotide and derived amino acid sequence of the cyanogenic beta-glucosidase (linamarase) from white clover (Trifolium repens L.)." Oxtoby E., Dunn M.A., Pancoro A., Hughes M.A. Plant Mol. Biol. 17:209-219(1991) [PubMed: 1907511] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-25 AND 125-147. Strain: S100 (EG). Tissue: Leaf.
[2]	"The crystal structure of a cyanogenic beta-glucosidase from white clover, a family 1 glycosyl hydrolase." Barrett T., Suresh C.G., Tolley S.P., Dodson E.J., Hughes M.A. Structure 3:951-960(1995) [PubMed: 8535788] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X56733 mRNA. Translation: CAA40057.1.

PIR

GLJY14. S16580.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CBG	X-ray	2.15	A	12-412	[»]

ProteinModelPortal

P26205.

SMR

P26205. Positions 12-412.

ModBase

Search...

Protein family/group databases

CAZy

GH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

PANTHER

PTHR10353. Glyco_hydro_1. 1 hit.

Pfam

PF00232. Glyco_hydro_1. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BGLT_TRIRP

Accession

Primary (citable) accession number: P26205

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 31, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program