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Q9ZAG3

- LIMA_RHOER

UniProt

Q9ZAG3 - LIMA_RHOER

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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

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
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 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 [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:
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