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P0A434 (OPD_BREDI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Parathion hydrolase

EC=3.1.8.1
Alternative name(s):
Phosphotriesterase
Short name=PTE
Gene names
Name:opd
Encoded onPlasmid pCMS1
OrganismBrevundimonas diminuta (Pseudomonas diminuta)
Taxonomic identifier293 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeBrevundimonas

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate.

Catalytic activity

An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homodimer.

Subcellular location

Cell membrane; Peripheral membrane protein.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Biotechnological use

Has attracted interest because of its potential use in the detoxification of chemical waste and warfare agents and its ability to degrade agricultural pesticides such as parathion.

Sequence similarities

Belongs to the phosphotriesterase family.

Sequence caution

The sequence AAA98299.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical term3D-structure
Direct protein sequencing
Plasmid
Gene Ontology (GO)
   Biological_processcatabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaryldialkylphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929Tat-type signal Ref.1
Chain30 – 365336Parathion hydrolase
PRO_0000029860

Sites

Metal binding551Zinc 1
Metal binding571Zinc 1
Metal binding1691Zinc 1; via carbamate group
Metal binding1691Zinc 2; via carbamate group
Metal binding2011Zinc 2
Metal binding2301Zinc 2
Metal binding3011Zinc 1

Amino acid modifications

Modified residue1691N6-carboxylysine

Secondary structure

.............................................................................. 365
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A434 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 41FF8E4B029B46DC

FASTA36539,004
        10         20         30         40         50         60 
MQTRRVVLKS AAAAGTLLGG LAGCASVAGS IGTGDRINTV RGPITISEAG FTLTHEHICG 

        70         80         90        100        110        120 
SSAGFLRAWP EFFGSRKALA EKAVRGLRRA RAAGVRTIVD VSTFDIGRDV SLLAEVSRAA 

       130        140        150        160        170        180 
DVHIVAATGL WFDPPLSMRL RSVEELTQFF LREIQYGIED TGIRAGIIKV ATTGKATPFQ 

       190        200        210        220        230        240 
ELVLKAAARA SLATGVPVTT HTAASQRDGE QQAAIFESEG LSPSRVCIGH SDDTDDLSYL 

       250        260        270        280        290        300 
TALAARGYLI GLDHIPHSAI GLEDNASASA LLGIRSWQTR ALLIKALIDQ GYMKQILVSN 

       310        320        330        340        350        360 
DWLFGFSSYV TNIMDVMDRV NPDGMAFIPL RVIPFLREKG VPQETLAGIT VTNPARFLSP 


TLRAS 

« Hide

References

[1]"Parathion hydrolase gene from Pseudomonas diminuta MG: subcloning, complete nucleotide sequence, and expression of the mature portion of the enzyme in Escherichia coli."
Serdar C.M., Murdock D.C., Rohde M.F.
Biotechnology (N.Y.) 7:1151-1155(1989)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-44.
Strain: MG.
[2]"Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase."
McDaniel C.S., Harper L.L., Wild J.R.
J. Bacteriol. 170:2306-2311(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MG.
[3]"Identification of the histidine ligands to the binuclear metal center of phosphotriesterase by site-directed mutagenesis."
Kuo J.M., Raushel F.M.
Biochemistry 33:4265-4272(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: METAL BINDING SITES.
[4]"Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents."
Benning M.M., Kuo J.M., Raushel F.M., Holden H.M.
Biochemistry 33:15001-15007(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]"Three-dimensional structure of the binuclear metal center of phosphotriesterase."
Benning M.M., Kuo J.M., Raushel F.M., Holden H.M.
Biochemistry 34:7973-7978(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), CARBAMYLATION AT LYS-169.
[6]"Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate."
Vanhooke J.L., Benning M.M., Raushel F.M., Holden H.M.
Biochemistry 35:6020-6025(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20392 Genomic DNA. Translation: AAA98299.1. Frameshift.
PIRA28214.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPMX-ray2.10A/B36-363[»]
1EYWX-ray1.90A35-365[»]
1EZ2X-ray1.90A/B35-365[»]
1HZYX-ray1.30A/B34-365[»]
1I0BX-ray1.30A/B34-365[»]
1I0DX-ray1.30A/B34-365[»]
1JGMX-ray1.30A/B30-365[»]
1PSCX-ray2.00A/B1-365[»]
1PTAX-ray2.10A36-362[»]
1QW7X-ray1.90A/B30-365[»]
2O4MX-ray1.64A/B/C/P34-364[»]
2O4QX-ray1.95A/B/K/P34-364[»]
2OB3X-ray1.04A/B35-364[»]
2OQLX-ray1.80A/B35-365[»]
3CAKX-ray1.83A/B35-365[»]
3CS2X-ray1.95A/B/K/P34-364[»]
3E3HX-ray2.15A/B30-365[»]
3UPMX-ray1.95A/B35-361[»]
3UR2X-ray2.00A/B35-363[»]
3UR5X-ray1.60A/B35-361[»]
3URAX-ray1.88A/B35-361[»]
3URBX-ray1.77A/B35-361[»]
3URNX-ray1.95A/B35-361[»]
3URQX-ray2.10A/B35-361[»]
4E3TX-ray1.65A/B34-365[»]
4GY0X-ray1.85A/B34-365[»]
4GY1X-ray1.50A/B34-365[»]
ProteinModelPortalP0A434.
SMRP0A434. Positions 34-364.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3322.
SABIO-RKP0A434.

Family and domain databases

InterProIPR017947. AryldialkylPase_Zn-BS.
IPR001559. Aryldialkylphosphatase.
IPR006311. TAT_signal.
[Graphical view]
PANTHERPTHR10819. PTHR10819. 1 hit.
PfamPF02126. PTE. 1 hit.
[Graphical view]
PROSITEPS01322. PHOSPHOTRIESTERASE_1. 1 hit.
PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A434.

Entry information

Entry nameOPD_BREDI
AccessionPrimary (citable) accession number: P0A434
Secondary accession number(s): P13739, P16648
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: July 9, 2014
This is version 63 of the entry and version 1 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