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Q9ZAG3 (LIMA_RHOER) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Limonene-1,2-epoxide hydrolase

EC=3.3.2.8
Gene names
Name:limA
OrganismRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifier1833 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

1,2-epoxymenth-8-ene + H2O = menth-8-ene-1,2-diol. Ref.3

Pathway

Terpene metabolism; (4R)-limonene degradation; (1S,4R)-1-hydroxylimonen-2-one from (4R)-limonene: step 2/3.

Subunit structure

Monomer. Ref.3

Induction

By growth on monoterpenes.

Sequence similarities

Belongs to the limonene-1,2-epoxide hydrolase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7. Ref.3

Temperature dependence:

Optimum temperature is 50 degrees Celsius.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functionlimonene-1,2-epoxide hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 149148Limonene-1,2-epoxide hydrolase
PRO_0000084422

Sites

Active site1011Proton donor Probable
Active site1321Proton acceptor Probable

Experimental info

Mutagenesis531Y → F: 15% of wild-type catalytic efficiency. Ref.4
Mutagenesis551N → A: Almost no activity. Ref.4
Mutagenesis551N → D: No activity. Ref.4
Mutagenesis991R → A, H, K or Q: Impaired protein folding and no activity. Ref.4
Mutagenesis1011D → A or N: No activity. Ref.4
Mutagenesis1321D → A or N: No activity. Ref.4

Secondary structure

....................... 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ZAG3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1A8602D20793A1B9

FASTA14916,521
        10         20         30         40         50         60 
MTSKIEQPRW ASKDSAAGAA STPDEKIVLE FMDALTSNDA AKLIEYFAED TMYQNMPLPP 

        70         80         90        100        110        120 
AYGRDAVEQT LAGLFTVMSI DAVETFHIGS SNGLVYTERV DVLRALPTGK SYNLSILGVF 

       130        140 
QLTEGKITGW RDYFDLREFE EAVDLPLRG 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y18005 Genomic DNA. Translation: CAA77012.1.
AJ272366 Genomic DNA. Translation: CAC20854.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NU3X-ray1.75A/B1-149[»]
1NWWX-ray1.20A/B1-149[»]
ProteinModelPortalQ9ZAG3.
SMRQ9ZAG3. Positions 3-149.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13975.
BRENDA3.3.2.8. 5389.
UniPathwayUPA00987; UER00865.

Family and domain databases

InterProIPR013100. LEH.
[Graphical view]
PfamPF07858. LEH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9ZAG3.

Entry information

Entry nameLIMA_RHOER
AccessionPrimary (citable) accession number: Q9ZAG3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 60 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways