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Protein

Limonene-1,2-epoxide hydrolase

Gene

limA

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

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

Pathway:i(4R)-limonene degradation

This protein is involved in step 2 of the subpathway that synthesizes (1S,4R)-1-hydroxylimonen-2-one from (4R)-limonene.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Limonene 1,2-monooxygenase (limB)
  2. Limonene-1,2-epoxide hydrolase (limA)
  3. no protein annotated in this organism
This subpathway is part of the pathway (4R)-limonene degradation, which is itself part of Terpene metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (1S,4R)-1-hydroxylimonen-2-one from (4R)-limonene, the pathway (4R)-limonene degradation and in Terpene metabolism.

Sites

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

GO - Molecular functioni

Complete GO annotation...

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 lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

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
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni15 – 184Combined sources
Helixi23 – 3412Combined sources
Helixi35 – 373Combined sources
Helixi40 – 445Combined sources
Beta strandi52 – 554Combined sources
Beta strandi61 – 633Combined sources
Helixi64 – 7714Combined sources
Beta strandi78 – 9114Combined sources
Beta strandi94 – 10512Combined sources
Turni106 – 1083Combined sources
Beta strandi111 – 12313Combined sources
Beta strandi126 – 1338Combined sources
Helixi136 – 1438Combined sources
Turni147 – 1493Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NU3X-ray1.75A/B1-149[»]
1NWWX-ray1.20A/B1-149[»]
4R9KX-ray1.50A/B/C3-149[»]
4R9LX-ray1.80A/B/C3-149[»]
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

        10         20         30         40         50
MTSKIEQPRW ASKDSAAGAA STPDEKIVLE FMDALTSNDA AKLIEYFAED
60 70 80 90 100
TMYQNMPLPP AYGRDAVEQT LAGLFTVMSI DAVETFHIGS SNGLVYTERV
110 120 130 140
DVLRALPTGK SYNLSILGVF QLTEGKITGW RDYFDLREFE EAVDLPLRG
Length:149
Mass (Da):16,521
Last modified:January 23, 2007 - v3
Checksum:i1A8602D20793A1B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18005 Genomic DNA. Translation: CAA77012.1.
AJ272366 Genomic DNA. Translation: CAC20854.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18005 Genomic DNA. Translation: CAA77012.1.
AJ272366 Genomic DNA. Translation: CAC20854.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NU3X-ray1.75A/B1-149[»]
1NWWX-ray1.20A/B1-149[»]
4R9KX-ray1.50A/B/C3-149[»]
4R9LX-ray1.80A/B/C3-149[»]
ProteinModelPortaliQ9ZAG3.
SMRiQ9ZAG3. Positions 3-149.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9ZAG3.

Family and domain databases

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

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: June 24, 2015
This is version 66 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.