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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

Pathwayi: (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)DescriptionActionsGraphical viewLength
Active sitei101Proton donorCurated1
Active sitei132Proton acceptorCurated1

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)DescriptionActionsGraphical viewLength
Mutagenesisi53Y → F: 15% of wild-type catalytic efficiency. 1 Publication1
Mutagenesisi55N → A: Almost no activity. 1 Publication1
Mutagenesisi55N → D: No activity. 1 Publication1
Mutagenesisi99R → A, H, K or Q: Impaired protein folding and no activity. 1 Publication1
Mutagenesisi101D → A or N: No activity. 1 Publication1
Mutagenesisi132D → A or N: No activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000844222 – 149Limonene-1,2-epoxide hydrolaseAdd BLAST148

Expressioni

Inductioni

By growth on monoterpenes.

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 11Combined sources3
Turni15 – 18Combined sources4
Helixi23 – 34Combined sources12
Helixi35 – 37Combined sources3
Helixi40 – 44Combined sources5
Beta strandi52 – 55Combined sources4
Beta strandi61 – 63Combined sources3
Helixi64 – 77Combined sources14
Beta strandi78 – 91Combined sources14
Beta strandi94 – 105Combined sources12
Turni106 – 108Combined sources3
Beta strandi111 – 123Combined sources13
Beta strandi126 – 133Combined sources8
Helixi136 – 143Combined sources8
Turni147 – 149Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XBTX-ray1.70A/B/C/D2-149[»]
4XBXX-ray1.53A/B/C/D2-149[»]
4XBYX-ray2.30A/B/C/D/E/F/G/H5-149[»]
4XDVX-ray2.25A/B/C/D/E/F/G/H5-149[»]
4XDWX-ray2.05A/B/C/D/E/F/G/H5-149[»]
5CF1X-ray2.24A/B/C/D/E/F/G/H2-149[»]
5CF2X-ray3.00A/B/C/D2-149[»]
5CK6X-ray2.50A/B2-149[»]
5CLKX-ray2.70A/B2-149[»]
5JPPX-ray2.50A/B2-149[»]
5JPUX-ray1.50A/B2-149[»]
ProteinModelPortaliQ9ZAG3.
SMRiQ9ZAG3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZAG3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK10533.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR013100. LEH.
IPR032710. NTF2-like_dom.
[Graphical view]
PfamiPF07858. LEH. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.

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.

Genome annotation databases

KEGGiag:CAA77012.

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
PDB 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[»]
4XBTX-ray1.70A/B/C/D2-149[»]
4XBXX-ray1.53A/B/C/D2-149[»]
4XBYX-ray2.30A/B/C/D/E/F/G/H5-149[»]
4XDVX-ray2.25A/B/C/D/E/F/G/H5-149[»]
4XDWX-ray2.05A/B/C/D/E/F/G/H5-149[»]
5CF1X-ray2.24A/B/C/D/E/F/G/H2-149[»]
5CF2X-ray3.00A/B/C/D2-149[»]
5CK6X-ray2.50A/B2-149[»]
5CLKX-ray2.70A/B2-149[»]
5JPPX-ray2.50A/B2-149[»]
5JPUX-ray1.50A/B2-149[»]
ProteinModelPortaliQ9ZAG3.
SMRiQ9ZAG3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA77012.

Phylogenomic databases

KOiK10533.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9ZAG3.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR013100. LEH.
IPR032710. NTF2-like_dom.
[Graphical view]
PfamiPF07858. LEH. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 74 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

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 one 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.