Reviewed, UniProtKB/Swiss-Prot P0A433 (OPD_FLAS2)

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 pPDL2

Organism

Flavobacterium sp. (strain ATCC 27551)

Taxonomic identifier

74567 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteria › Flavobacteriales › Flavobacteriaceae › Flavobacterium

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 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 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	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aryldialkylphosphatase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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_0000029861

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

Helix

136 – 139

4

Helix

143 – 155

13

Beta strand

167 – 171

5

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 – 337

11

Turn

338 – 340

3

Helix

343 – 350

8

Helix

352 – 358

7

Sequences

	Sequence		Length	Mass (Da)
	P0A433-1 [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 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: 2556372] [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: 15369336] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-365, CARBAMYLATION AT LYS-169.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M29593 Genomic DNA. Translation: AAA24930.1.

PIR

A43720.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P6B	X-ray	1.90	A/B	30-365	[»]
1P6C	X-ray	2.00	A/B	30-365	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3321.

Family and domain databases

InterPro

IPR017947. AryldialkylPase_Zn-BS.
IPR001559. Aryldialkylphosphatase.
IPR017909. Twin_arg_translocation_Tat.
[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_FLAS2

Accession

Primary (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:	October 13, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)