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P0A433 (OPD_SPHSA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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 pPDL2
OrganismSphingobium fuliginis (strain ATCC 27551)
Taxonomic identifier336203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingobium

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 By similarity.

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cell membrane; Peripheral membrane protein By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the phosphotriesterase family.

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

dephosphorylation

Inferred from electronic annotation. Source: GOC

   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_0000029861

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
P0A433 [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 specified by the Flavobacterium opd gene: relationship between the gene and protein."
Mulbry W.W., Karns J.S.
J. Bacteriol. 171:6740-6746(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-53.
[2]"Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site."
Hill C.M., Li W.S., Thoden J.B., Holden H.M., Raushel F.M.
J. Am. Chem. Soc. 125:8990-8991(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-365, CARBAMYLATION AT LYS-169.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29593 Genomic DNA. Translation: AAA24930.1.
PIRA43720.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P6BX-ray1.90A/B30-365[»]
1P6CX-ray2.00A/B30-365[»]
ProteinModelPortalP0A433.
SMRP0A433. Positions 34-364.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3321.

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

EvolutionaryTraceP0A433.

Entry information

Entry nameOPD_SPHSA
AccessionPrimary (citable) accession number: P0A433
Secondary accession number(s): P13739, P16648
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: February 19, 2014
This is version 52 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