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P26205

- BGLT_TRIRP

UniProt

P26205 - BGLT_TRIRP

Protein

Cyanogenic beta-glucosidase

Gene

LI

Organism
Trifolium repens (Creeping white clover)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    Functioni

    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 activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei44 – 441SubstrateBy similarity
    Binding sitei148 – 1481SubstrateBy similarity
    Binding sitei193 – 1931SubstrateBy similarity
    Active sitei194 – 1941Proton donor
    Binding sitei337 – 3371SubstrateBy similarity
    Active sitei408 – 4081Nucleophile

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyanogenic beta-glucosidase (EC:3.2.1.21)
    Alternative name(s):
    Linamarase
    Gene namesi
    Name:LI
    OrganismiTrifolium repens (Creeping white clover)
    Taxonomic identifieri3899 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeTrifolium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei‹1 – 11›111 PublicationAdd
    BLAST
    Chaini12 – 425414Cyanogenic beta-glucosidasePRO_0000011765Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi213 ↔ 221
    Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Leaves.

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    425
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 243
    Helixi27 – 293
    Beta strandi35 – 395
    Helixi42 – 454
    Beta strandi49 – 513
    Helixi58 – 658
    Helixi67 – 693
    Beta strandi76 – 783
    Helixi82 – 9514
    Beta strandi100 – 1045
    Helixi107 – 1104
    Helixi116 – 1183
    Helixi122 – 13716
    Beta strandi141 – 1499
    Helixi153 – 1597
    Helixi161 – 1633
    Helixi167 – 18216
    Turni183 – 1853
    Beta strandi188 – 1936
    Helixi195 – 2039
    Helixi215 – 2173
    Turni226 – 2283
    Helixi229 – 25123
    Helixi253 – 2564
    Beta strandi259 – 2657
    Beta strandi268 – 2758
    Helixi276 – 28914
    Helixi291 – 2999
    Helixi304 – 3107
    Helixi311 – 3133
    Helixi319 – 3257
    Beta strandi330 – 3356
    Beta strandi339 – 3446
    Helixi355 – 3584
    Beta strandi361 – 3677
    Beta strandi370 – 3734
    Helixi386 – 39813
    Beta strandi404 – 4085

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CBGX-ray2.15A12-412[»]
    ProteinModelPortaliP26205.
    SMRiP26205. Positions 12-412.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26205.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P26205-1 [UniParc]FASTAAdd to Basket

    « Hide

    LLSITTTHIH AFKPLPISFD DFSDLNRSCF APGFVFGTAS SAFQYEGAAF    50
    EDGKGPSIWD TFTHKYPEKI KDRTNGDVAI DEYHRYKEDI GIMKDMNLDA 100
    YRFSISWPRV LPKGKLSGGV NREGINYYNN LINEVLANGM QPYVTLFHWD 150
    VPQALEDEYR GFLGRNIVDD FRDYAELCFK EFGDRVKHWI TLNEPWGVSM 200
    NAYAYGTFAP GRCSDWLKLN CTGGDSGREP YLAAHYQLLA HAAAARLYKT 250
    KYQASQNGII GITLVSHWFE PASKEKADVD AAKRGLDFML GWFMHPLTKG 300
    RYPESMRYLV RKRLPKFSTE ESKELTGSFD FLGLNYYSSY YAAKAPRIPN 350
    ARPAIQTDSL INATFEHNGK PLGPMAASSW LCIYPQGIRK LLLYVKNHYN 400
    NPVIYITENG RNSSTINTVT SRIPF 425
    Length:425
    Mass (Da):48,325
    Last modified:May 1, 1992 - v1
    Checksum:i20B983B65C47A678
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56733 mRNA. Translation: CAA40057.1.
    PIRiS16580. GLJY14.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56733 mRNA. Translation: CAA40057.1 .
    PIRi S16580. GLJY14.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CBG X-ray 2.15 A 12-412 [» ]
    ProteinModelPortali P26205.
    SMRi P26205. Positions 12-412.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P26205.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).

    Entry informationi

    Entry nameiBGLT_TRIRP
    AccessioniPrimary (citable) accession number: P26205
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3