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P52705

- HNL_MANES

UniProt

P52705 - HNL_MANES

Protein

(S)-hydroxynitrile lyase

Gene

HNL

Organism
Manihot esculenta (Cassava) (Jatropha manihot)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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 – 801By similarity
    Active sitei208 – 2081By similarity
    Active sitei236 – 2361By similarity

    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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-6902.

    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
    OrganismiManihot esculenta (Cassava) (Jatropha manihot)
    Taxonomic identifieri3983 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeManihoteaeManihot

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801S → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 258257(S)-hydroxynitrile lyasePRO_0000084018Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.

    Structurei

    Secondary structure

    1
    258
    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 – 679
    Beta strandi74 – 807
    Helixi83 – 9311
    Helixi94 – 963
    Beta strandi97 – 1059
    Beta strandi110 – 1123
    Helixi116 – 1249
    Beta strandi132 – 1376
    Beta strandi143 – 1486
    Helixi151 – 1577
    Helixi164 – 17310
    Helixi181 – 1855
    Turni192 – 1943
    Helixi195 – 1973
    Beta strandi200 – 2045
    Beta strandi209 – 2113
    Helixi213 – 22210
    Beta strandi226 – 2305
    Helixi238 – 2414
    Helixi243 – 25715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DWOX-ray2.20A/B2-258[»]
    1DWPX-ray2.20A/B2-258[»]
    1DWQX-ray2.20A/B2-258[»]
    1E89X-ray2.10A/B2-258[»]
    1E8DX-ray2.20A/B2-258[»]
    1EB8X-ray2.10A/B2-258[»]
    1EB9X-ray2.10A/B2-258[»]
    3RKSX-ray2.50A/B/C/D1-258[»]
    3RKTX-ray2.91A/B/C/D/E/F/G/H1-258[»]
    ProteinModelPortaliP52705.
    SMRiP52705. Positions 1-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52705.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P52705-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVTAHFVLIH TICHGAWIWH KLKPALERAG HKVTALDMAA SGIDPRQIEQ    50
    INSFDEYSEP LLTFLEKLPQ GEKVIIVGES CAGLNIAIAA DRYVDKIAAG 100
    VFHNSLLPDT VHSPSYTVEK LLESFPDWRD TEYFTFTNIT GETITTMKLG 150
    FVLLRENLFT KCTDGEYELA KMVMRKGSLF QNVLAQRPKF TEKGYGSIKK 200
    VYIWTDQDKI FLPDFQRWQI ANYKPDKVYQ VQGGDHKLQL TKTEEVAHIL 250
    QEVADAYA 258
    Length:258
    Mass (Da):29,372
    Last modified:January 23, 2007 - v3
    Checksum:i98ABA050AC8AF1C5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29091 mRNA. Translation: CAA82334.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29091 mRNA. Translation: CAA82334.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DWO X-ray 2.20 A/B 2-258 [» ]
    1DWP X-ray 2.20 A/B 2-258 [» ]
    1DWQ X-ray 2.20 A/B 2-258 [» ]
    1E89 X-ray 2.10 A/B 2-258 [» ]
    1E8D X-ray 2.20 A/B 2-258 [» ]
    1EB8 X-ray 2.10 A/B 2-258 [» ]
    1EB9 X-ray 2.10 A/B 2-258 [» ]
    3RKS X-ray 2.50 A/B/C/D 1-258 [» ]
    3RKT X-ray 2.91 A/B/C/D/E/F/G/H 1-258 [» ]
    ProteinModelPortali P52705.
    SMRi P52705. Positions 1-258.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-6902.

    Miscellaneous databases

    EvolutionaryTracei P52705.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view ]
    Pfami PF00561. Abhydrolase_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Purification, characterization, and cloning of alpha-hydroxynitrile lyase from cassava (Manihot esculenta Crantz)."
      Hughes J., Carvalho F.J.P.D.C., Hughes M.A.
      Arch. Biochem. Biophys. 311:496-502(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-37 AND 169-192.
      Tissue: Cotyledon.
    2. "Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis."
      Lauble H., Foerster S., Miehlich B., Wajant H., Effenberger F.
      Acta Crystallogr. D 57:194-200(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    3. "Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin."
      Lauble H., Miehlich B., Foerster S., Wajant H., Effenberger F.
      Protein Sci. 10:1015-1022(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), MUTAGENESIS OF SER-80.
    4. "Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta."
      Lauble H., Miehlich B., Foerster S., Kobler C., Wajant H., Effenberger F.
      Protein Sci. 11:65-71(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

    Entry informationi

    Entry nameiHNL_MANES
    AccessioniPrimary (citable) accession number: P52705
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 75 of the entry and version 3 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