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P52704

- HNL_HEVBR

UniProt

P52704 - HNL_HEVBR

Protein

(S)-hydroxynitrile lyase

Gene

HNL

Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Involved in cyanogenesis, the release of HCN from injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and the corresponding aldehydes and ketones. The natural substrate of this enzyme is (S)-acetone cyanohydrin.

    Catalytic activityi

    An aliphatic (S)-hydroxynitrile = cyanide + an aliphatic aldehyde or ketone.
    An aromatic (S)-hydroxynitrile = cyanide + an aromatic aldehyde.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei80 – 801
    Active sitei207 – 2071
    Active sitei235 – 2351

    GO - Molecular functioni

    1. aliphatic (S)-hydroxynitrile lyase activity Source: UniProtKB-EC
    2. aromatic (S)-hydroxynitrile lyase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Lyase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    (S)-hydroxynitrile lyase (EC:4.1.2.47)
    Alternative name(s):
    (S)-acetone-cyanohydrin lyase
    Oxynitrilase
    Gene namesi
    Name:HNL
    OrganismiHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
    Taxonomic identifieri3981 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801S → A: Loss of activity. 1 Publication
    Mutagenesisi81 – 811C → S: Loss of activity. 1 Publication
    Mutagenesisi235 – 2351H → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 257257(S)-hydroxynitrile lyasePRO_0000084017Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    PRIDEiP52704.

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    257
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Helixi16 – 194
    Helixi22 – 287
    Beta strandi32 – 365
    Helixi48 – 503
    Helixi54 – 574
    Helixi59 – 668
    Beta strandi74 – 807
    Helixi82 – 9312
    Helixi94 – 963
    Beta strandi97 – 1059
    Beta strandi110 – 1123
    Helixi116 – 1249
    Beta strandi132 – 1387
    Beta strandi141 – 1477
    Helixi150 – 1567
    Helixi163 – 17210
    Helixi180 – 1856
    Turni191 – 1933
    Helixi194 – 1963
    Beta strandi199 – 2035
    Beta strandi208 – 2103
    Helixi212 – 22110
    Beta strandi225 – 2295
    Helixi237 – 2404
    Helixi242 – 25514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QJ4X-ray1.10A1-257[»]
    1SC9X-ray1.80A1-257[»]
    1SCIX-ray2.18A1-257[»]
    1SCKX-ray1.70A1-257[»]
    1SCQX-ray2.90A1-257[»]
    1YASX-ray1.90A1-257[»]
    1YB6X-ray1.54A2-257[»]
    1YB7X-ray1.76A2-257[»]
    2G4LX-ray1.84A1-257[»]
    2YASX-ray1.72A1-257[»]
    3C6XX-ray1.05A1-257[»]
    3C6YX-ray1.25A1-257[»]
    3C6ZX-ray1.05A1-257[»]
    3C70X-ray1.05A1-257[»]
    3YASX-ray1.85A1-257[»]
    4YASX-ray2.00A1-257[»]
    5YASX-ray2.20A1-257[»]
    6YASX-ray2.20A1-257[»]
    7YASX-ray1.75A1-257[»]
    ProteinModelPortaliP52704.
    SMRiP52704. Positions 2-257.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52704.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P52704-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFAHFVLIH TICHGAWIWH KLKPLLEALG HKVTALDLAA SGVDPRQIEE    50
    IGSFDEYSEP LLTFLEALPP GEKVILVGES CGGLNIAIAA DKYCEKIAAA 100
    VFHNSVLPDT EHCPSYVVDK LMEVFPDWKD TTYFTYTKDG KEITGLKLGF 150
    TLLRENLYTL CGPEEYELAK MLTRKGSLFQ NILAKRPFFT KEGYGSIKKI 200
    YVWTDQDEIF LPEFQLWQIE NYKPDKVYKV EGGDHKLQLT KTKEIAEILQ 250
    EVADTYN 257
    Length:257
    Mass (Da):29,228
    Last modified:October 1, 1996 - v1
    Checksum:iEF4AE88717279CEB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40402 mRNA. Translation: AAC49184.1.
    PIRiT10758.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40402 mRNA. Translation: AAC49184.1 .
    PIRi T10758.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QJ4 X-ray 1.10 A 1-257 [» ]
    1SC9 X-ray 1.80 A 1-257 [» ]
    1SCI X-ray 2.18 A 1-257 [» ]
    1SCK X-ray 1.70 A 1-257 [» ]
    1SCQ X-ray 2.90 A 1-257 [» ]
    1YAS X-ray 1.90 A 1-257 [» ]
    1YB6 X-ray 1.54 A 2-257 [» ]
    1YB7 X-ray 1.76 A 2-257 [» ]
    2G4L X-ray 1.84 A 1-257 [» ]
    2YAS X-ray 1.72 A 1-257 [» ]
    3C6X X-ray 1.05 A 1-257 [» ]
    3C6Y X-ray 1.25 A 1-257 [» ]
    3C6Z X-ray 1.05 A 1-257 [» ]
    3C70 X-ray 1.05 A 1-257 [» ]
    3YAS X-ray 1.85 A 1-257 [» ]
    4YAS X-ray 2.00 A 1-257 [» ]
    5YAS X-ray 2.20 A 1-257 [» ]
    6YAS X-ray 2.20 A 1-257 [» ]
    7YAS X-ray 1.75 A 1-257 [» ]
    ProteinModelPortali P52704.
    SMRi P52704. Positions 2-257.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P52704.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P52704.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis. Functional expression in Escherichia coli and Saccharomyces cerevisiae and identification of an active site residue."
      Hasslacher M., Schall M., Hayn M., Griengl H., Kohlwein S.D., Schwab H.
      J. Biol. Chem. 271:5884-5891(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 121-126; 176-181; 200-204 AND 244-253, MUTAGENESIS OF CYS-81.
      Tissue: Leaf.
    2. "Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis."
      Wagner U.G., Hasslacher M., Griengl H., Schwab H., Kratky C.
      Structure 4:811-822(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF SER-80 AND HIS-235.
    3. "Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis."
      Gruber K., Gugganig M., Wagner U.G., Kratky C.
      Biol. Chem. 380:993-1000(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
    4. "Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis."
      Zuegg J., Gruber K., Gugganig M., Wagner U.G., Kratky C.
      Protein Sci. 8:1990-2000(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).

    Entry informationi

    Entry nameiHNL_HEVBR
    AccessioniPrimary (citable) accession number: P52704
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 77 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3