P0A434 (OPD_BREDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Parathion hydrolase
EC=3.1.8.1

Alternative name(s):
Phosphotriesterase
Short name=PTE

Gene names

Name:

opd

Encoded on

Plasmid pCMS1

Organism

Brevundimonas diminuta (Pseudomonas diminuta)

Taxonomic identifier

293 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Brevundimonas

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cell membrane Membrane
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aryldialkylphosphatase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Tat-type signal Ref.1

Chain

30 – 365

336

Parathion hydrolase

PRO_0000029860

Sites

Metal binding

55

1

Zinc 1

Metal binding

57

1

Zinc 1

Metal binding

169

1

Zinc 1; via carbamate group

Metal binding

169

1

Zinc 2; via carbamate group

Metal binding

201

1

Zinc 2

Metal binding

230

1

Zinc 2

Metal binding

301

1

Zinc 1

Amino acid modifications

Modified residue

169

1

N6-carboxylysine

Secondary structure

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365

Helix Strand Turn

Details...

Beta strand

36 – 39

4

Beta strand

42 – 45

4

Helix

46 – 48

3

Beta strand

51 – 56

6

Beta strand

58 – 60

3

Helix

65 – 68

4

Helix

70 – 73

4

Helix

76 – 92

17

Beta strand

97 – 100

4

Helix

104 – 106

3

Helix

110 – 120

11

Beta strand

123 – 125

3

Beta strand

127 – 129

3

Helix

136 – 139

4

Helix

143 – 155

13

Turn

159 – 162

4

Beta strand

166 – 171

6

Beta strand

173 – 175

3

Helix

178 – 194

17

Beta strand

198 – 201

4

Helix

204 – 206

3

Helix

208 – 218

11

Helix

223 – 225

3

Beta strand

226 – 228

3

Helix

231 – 233

3

Helix

237 – 245

9

Beta strand

249 – 252

4

Helix

266 – 272

7

Helix

277 – 289

13

Helix

293 – 295

3

Beta strand

296 – 298

3

Beta strand

304 – 306

3

Beta strand

308 – 310

3

Helix

313 – 320

8

Helix

324 – 326

3

Helix

327 – 330

4

Helix

332 – 338

7

Helix

343 – 350

8

Helix

352 – 358

7

Sequences

	Sequence		Length	Mass (Da)
	P0A434 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 41FF8E4B029B46DC	FASTA	365	39,004
	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

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: 2834339] [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: 8155644] [Abstract] Cited for: ACTIVE SITE.
[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: 7999757] [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: 7794910] [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: 8634243] [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.

PIR

A28214.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0A434.

SMR

P0A434. Positions 34-364.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

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Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-3322.

Family and domain databases

InterPro

IPR017947. AryldialkylPase_Zn-BS.
IPR001559. Aryldialkylphosphatase.
IPR006311. TAT_signal.
[Graphical view]

PANTHER

PTHR10819. PTE. 1 hit.

Pfam

PF02126. PTE. 1 hit.
[Graphical view]

PROSITE

PS01322. PHOSPHOTRIESTERASE_1. 1 hit.
PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

OPD_BREDI

Accession

Primary (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:	May 31, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program