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P0A434

- OPD_BREDI

UniProt

P0A434 - OPD_BREDI

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Protein

Parathion hydrolase

Gene
opd
Organism
Brevundimonas diminuta (Pseudomonas diminuta)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551Zinc 1
Metal bindingi57 – 571Zinc 1
Metal bindingi169 – 1691Zinc 1; via carbamate group
Metal bindingi169 – 1691Zinc 2; via carbamate group
Metal bindingi201 – 2011Zinc 2
Metal bindingi230 – 2301Zinc 2
Metal bindingi301 – 3011Zinc 1

GO - Molecular functioni

  1. aryldialkylphosphatase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3322.
SABIO-RKP0A434.

Names & Taxonomyi

Protein namesi
Recommended name:
Parathion hydrolase (EC:3.1.8.1)
Alternative name(s):
Phosphotriesterase
Short name:
PTE
Gene namesi
Name:opd
Encoded oniPlasmid pCMS10 Publication
OrganismiBrevundimonas diminuta (Pseudomonas diminuta)
Taxonomic identifieri293 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeBrevundimonas

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Biotechnological usei

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Tat-type signal1 PublicationAdd
BLAST
Chaini30 – 365336Parathion hydrolasePRO_0000029860Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei169 – 1691N6-carboxylysine

Post-translational modificationi

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

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 393
Beta strandi42 – 443
Helixi46 – 494
Beta strandi51 – 566
Beta strandi58 – 603
Turni61 – 644
Helixi65 – 684
Helixi70 – 734
Helixi76 – 9217
Beta strandi97 – 1004
Helixi104 – 1063
Helixi110 – 12011
Beta strandi123 – 1253
Beta strandi127 – 1293
Helixi136 – 1394
Helixi143 – 15513
Turni159 – 1624
Beta strandi166 – 1716
Beta strandi173 – 1753
Helixi178 – 19417
Beta strandi198 – 2014
Helixi204 – 2063
Helixi208 – 21811
Helixi223 – 2253
Beta strandi226 – 2283
Helixi231 – 2333
Helixi237 – 2459
Beta strandi249 – 2524
Helixi255 – 2584
Helixi266 – 2727
Helixi277 – 28913
Turni290 – 2923
Helixi293 – 2953
Beta strandi296 – 2983
Beta strandi304 – 3063
Beta strandi308 – 3103
Helixi313 – 3208
Helixi324 – 3263
Helixi327 – 3304
Helixi332 – 3387
Helixi343 – 3508
Helixi352 – 3587

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0A434.
SMRiP0A434. Positions 34-364.

Miscellaneous databases

EvolutionaryTraceiP0A434.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR017947. AryldialkylPase_Zn-BS.
IPR001559. Aryldialkylphosphatase.
IPR006311. TAT_signal.
[Graphical view]
PANTHERiPTHR10819. PTHR10819. 1 hit.
PfamiPF02126. PTE. 1 hit.
[Graphical view]
PROSITEiPS01322. PHOSPHOTRIESTERASE_1. 1 hit.
PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A434-1 [UniParc]FASTAAdd to Basket

« Hide

MQTRRVVLKS AAAAGTLLGG LAGCASVAGS IGTGDRINTV RGPITISEAG    50
FTLTHEHICG SSAGFLRAWP EFFGSRKALA EKAVRGLRRA RAAGVRTIVD 100
VSTFDIGRDV SLLAEVSRAA DVHIVAATGL WFDPPLSMRL RSVEELTQFF 150
LREIQYGIED TGIRAGIIKV ATTGKATPFQ ELVLKAAARA SLATGVPVTT 200
HTAASQRDGE QQAAIFESEG LSPSRVCIGH SDDTDDLSYL TALAARGYLI 250
GLDHIPHSAI GLEDNASASA LLGIRSWQTR ALLIKALIDQ GYMKQILVSN 300
DWLFGFSSYV TNIMDVMDRV NPDGMAFIPL RVIPFLREKG VPQETLAGIT 350
VTNPARFLSP TLRAS 365
Length:365
Mass (Da):39,004
Last modified:March 15, 2005 - v1
Checksum:i41FF8E4B029B46DC
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M20392 Genomic DNA. Translation: AAA98299.1. Frameshift.
PIRiA28214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M20392 Genomic DNA. Translation: AAA98299.1 . Frameshift.
PIRi A28214.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DPM X-ray 2.10 A/B 36-363 [» ]
1EYW X-ray 1.90 A 35-365 [» ]
1EZ2 X-ray 1.90 A/B 35-365 [» ]
1HZY X-ray 1.30 A/B 34-365 [» ]
1I0B X-ray 1.30 A/B 34-365 [» ]
1I0D X-ray 1.30 A/B 34-365 [» ]
1JGM X-ray 1.30 A/B 30-365 [» ]
1PSC X-ray 2.00 A/B 1-365 [» ]
1PTA X-ray 2.10 A 36-362 [» ]
1QW7 X-ray 1.90 A/B 30-365 [» ]
2O4M X-ray 1.64 A/B/C/P 34-364 [» ]
2O4Q X-ray 1.95 A/B/K/P 34-364 [» ]
2OB3 X-ray 1.04 A/B 35-364 [» ]
2OQL X-ray 1.80 A/B 35-365 [» ]
3CAK X-ray 1.83 A/B 35-365 [» ]
3CS2 X-ray 1.95 A/B/K/P 34-364 [» ]
3E3H X-ray 2.15 A/B 30-365 [» ]
3UPM X-ray 1.95 A/B 35-361 [» ]
3UR2 X-ray 2.00 A/B 35-363 [» ]
3UR5 X-ray 1.60 A/B 35-361 [» ]
3URA X-ray 1.88 A/B 35-361 [» ]
3URB X-ray 1.77 A/B 35-361 [» ]
3URN X-ray 1.95 A/B 35-361 [» ]
3URQ X-ray 2.10 A/B 35-361 [» ]
4E3T X-ray 1.65 A/B 34-365 [» ]
4GY0 X-ray 1.85 A/B 34-365 [» ]
4GY1 X-ray 1.50 A/B 34-365 [» ]
ProteinModelPortali P0A434.
SMRi P0A434. Positions 34-364.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-3322.
SABIO-RK P0A434.

Miscellaneous databases

EvolutionaryTracei P0A434.

Family and domain databases

InterProi IPR017947. AryldialkylPase_Zn-BS.
IPR001559. Aryldialkylphosphatase.
IPR006311. TAT_signal.
[Graphical view ]
PANTHERi PTHR10819. PTHR10819. 1 hit.
Pfami PF02126. PTE. 1 hit.
[Graphical view ]
PROSITEi PS01322. PHOSPHOTRIESTERASE_1. 1 hit.
PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiOPD_BREDI
AccessioniPrimary (citable) accession number: P0A434
Secondary accession number(s): P13739, P16648
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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