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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

Zn2+Note: Binds 2 Zn(2+) 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-KW
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 PublicationPROSITE-ProRule annotationAdd
BLAST
Chaini30 – 365336Parathion hydrolasePRO_0000029860Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei169 – 1691N6-carboxylysine1 PublicationPROSITE-ProRule annotation

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A434.

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphotriesterase family.PROSITE-ProRule annotation

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

        10         20         30         40         50
MQTRRVVLKS AAAAGTLLGG LAGCASVAGS IGTGDRINTV RGPITISEAG
60 70 80 90 100
FTLTHEHICG SSAGFLRAWP EFFGSRKALA EKAVRGLRRA RAAGVRTIVD
110 120 130 140 150
VSTFDIGRDV SLLAEVSRAA DVHIVAATGL WFDPPLSMRL RSVEELTQFF
160 170 180 190 200
LREIQYGIED TGIRAGIIKV ATTGKATPFQ ELVLKAAARA SLATGVPVTT
210 220 230 240 250
HTAASQRDGE QQAAIFESEG LSPSRVCIGH SDDTDDLSYL TALAARGYLI
260 270 280 290 300
GLDHIPHSAI GLEDNASASA LLGIRSWQTR ALLIKALIDQ GYMKQILVSN
310 320 330 340 350
DWLFGFSSYV TNIMDVMDRV NPDGMAFIPL RVIPFLREKG VPQETLAGIT
360
VTNPARFLSP TLRAS
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20392 Genomic DNA. Translation: AAA98299.1. Frameshift.
PIRiA28214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20392 Genomic DNA. Translation: AAA98299.1 . Frameshift.
PIRi A28214.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 66 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