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Q9ZAG3

- LIMA_RHOER

UniProt

Q9ZAG3 - LIMA_RHOER

Protein

Limonene-1,2-epoxide hydrolase

Gene

limA

Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalyzes the conversion of limonene-1,2-epoxide to limonene-1,2-diol. Can use both the (-) and (+) isomers of limonene-1,2-epoxide as substrates and also has some activity with 1-methylcyclohexene oxide, cyclohexene oxide and indene oxide as substrates.

    Catalytic activityi

    1,2-epoxymenth-8-ene + H2O = menth-8-ene-1,2-diol.1 Publication

    pH dependencei

    Optimum pH is 7.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei101 – 1011Proton donorCurated
    Active sitei132 – 1321Proton acceptorCurated

    GO - Molecular functioni

    1. limonene-1,2-epoxide hydrolase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13975.
    BRENDAi3.3.2.8. 5389.
    UniPathwayiUPA00987; UER00865.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Limonene-1,2-epoxide hydrolase (EC:3.3.2.8)
    Gene namesi
    Name:limA
    OrganismiRhodococcus erythropolis (Arthrobacter picolinophilus)
    Taxonomic identifieri1833 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi53 – 531Y → F: 15% of wild-type catalytic efficiency. 1 Publication
    Mutagenesisi55 – 551N → A: Almost no activity. 1 Publication
    Mutagenesisi55 – 551N → D: No activity. 1 Publication
    Mutagenesisi99 – 991R → A, H, K or Q: Impaired protein folding and no activity. 1 Publication
    Mutagenesisi101 – 1011D → A or N: No activity. 1 Publication
    Mutagenesisi132 – 1321D → A or N: No activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 149148Limonene-1,2-epoxide hydrolasePRO_0000084422Add
    BLAST

    Expressioni

    Inductioni

    By growth on monoterpenes.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1
    149
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni15 – 184
    Helixi23 – 3412
    Helixi35 – 373
    Helixi40 – 445
    Beta strandi52 – 554
    Beta strandi61 – 633
    Helixi64 – 7714
    Beta strandi78 – 9114
    Beta strandi94 – 10512
    Turni106 – 1083
    Beta strandi111 – 12313
    Beta strandi126 – 1338
    Helixi136 – 1438

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NU3X-ray1.75A/B1-149[»]
    1NWWX-ray1.20A/B1-149[»]
    ProteinModelPortaliQ9ZAG3.
    SMRiQ9ZAG3. Positions 3-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ZAG3.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR013100. LEH.
    [Graphical view]
    PfamiPF07858. LEH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9ZAG3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSKIEQPRW ASKDSAAGAA STPDEKIVLE FMDALTSNDA AKLIEYFAED    50
    TMYQNMPLPP AYGRDAVEQT LAGLFTVMSI DAVETFHIGS SNGLVYTERV 100
    DVLRALPTGK SYNLSILGVF QLTEGKITGW RDYFDLREFE EAVDLPLRG 149
    Length:149
    Mass (Da):16,521
    Last modified:January 23, 2007 - v3
    Checksum:i1A8602D20793A1B9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y18005 Genomic DNA. Translation: CAA77012.1.
    AJ272366 Genomic DNA. Translation: CAC20854.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y18005 Genomic DNA. Translation: CAA77012.1 .
    AJ272366 Genomic DNA. Translation: CAC20854.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NU3 X-ray 1.75 A/B 1-149 [» ]
    1NWW X-ray 1.20 A/B 1-149 [» ]
    ProteinModelPortali Q9ZAG3.
    SMRi Q9ZAG3. Positions 3-149.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00987 ; UER00865 .
    BioCyci MetaCyc:MONOMER-13975.
    BRENDAi 3.3.2.8. 5389.

    Miscellaneous databases

    EvolutionaryTracei Q9ZAG3.

    Family and domain databases

    InterProi IPR013100. LEH.
    [Graphical view ]
    Pfami PF07858. LEH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Rhodococcus erythropolis DCL14 limonene-1,2-epoxide hydrolase gene encodes an enzyme belonging to a novel class of epoxide hydrolases."
      Barbirato F., Verdoes J.C., de Bont J.A.M., van der Werf M.J.
      FEBS Lett. 438:293-296(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DCL 14.
    2. "Genetic analysis of the lim operon of Rhodococcus erythropolis DCL14."
      Van der Vlugt-Bergmans C.J.B., van der Werf M.J.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DCL 14.
    3. "Limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14 belongs to a novel class of epoxide hydrolases."
      van der Werf M.J., Overkamp K.M., de Bont J.A.M.
      J. Bacteriol. 180:5052-5057(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-51, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    4. "Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site."
      Arand M., Hallberg B.M., Zou J., Bergfors T., Oesch F., van der Werf M.J., de Bont J.A., Jones T.A., Mowbray S.L.
      EMBO J. 22:2583-2592(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH INHIBITOR, MUTAGENESIS OF TYR-53; ASN-55; ARG-99; ASP-101 AND ASP-132, PUTATIVE REACTION MECHANISM.

    Entry informationi

    Entry nameiLIMA_RHOER
    AccessioniPrimary (citable) accession number: Q9ZAG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 61 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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