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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: 5 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei101 – 1011Proton donor Inferred
Active sitei132 – 1321Proton acceptor Inferred

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.1 Publication

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.

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: July 9, 2014
This is version 60 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

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