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100  structures 947  species 1  interaction 1183  sequences 6  architectures

Family: PTE (PF02126)

Summary: Phosphotriesterase family

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Aryldialkylphosphatase". More...

Aryldialkylphosphatase Edit Wikipedia article

aryldialkylphosphatase
Identifiers
EC number 3.1.8.1
CAS number 117698-12-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Phosphotriesterase family
Structure of organophosphorus hydrolase.jpg
Structure of organophosphorus hydrolase
Identifiers
Symbol PTE
Pfam PF02126
InterPro IPR001559
PROSITE PDOC01026
SCOP 1dpm
SUPERFAMILY 1dpm

Aryldialkylphosphatase (EC 3.1.8.1) (also known as organophosphorus hydrolase, phosphotriesterase, and paraoxon hydrolase) is an enzyme that hydrolyse organophosphates:

an aryl dialkyl phosphate + H2O \rightleftharpoons dialkyl phosphate + an aryl alcohol

Thus, the two substrates of this enzyme are aryldialkylphosphate and H2O, whereas its two products are dialkylphosphate and aryl alcohol.

An organophosphate is the general name for esters of phosphoric acid and is one of the organophosphorus compounds. They can be found as part of insecticides, herbicides, and nerve gases, amongst others. Some less-toxic organophosphates can be used as solvents, plasticizers, and EP additives.

Function[edit]

Bacteria such as Pseudomonas diminuta harbor a plasmid that carries the gene for aryldialkylphosphatase (EC 3.1.8.1). This enzyme 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. It acts specifically on synthetic organophosphate triesters and phosphorofluoridates. It does not seem to have a natural occurring substrate and may thus have optimally evolved for utilizing paraoxon.

Structure[edit]

Aryldialkylphosphatase belongs to a family[1][2] of enzymes that possess a binuclear zinc metal centre at their active site. The two zinc ions are coordinated by six different residues, six of which being histidines.

References[edit]

  1. ^ Scanlan TS, Reid RC (1995). "Evolution in action". Chem. Biol. 2 (2): 71–75. doi:10.1016/1074-5521(95)90278-3. PMID 9383406. 
  2. ^ Fletterick RJ, Buchbinder JL, Stephenson RC, Dresser MJ, Pitera JW, Scanlan TS (1998). "Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family". Biochemistry 37 (15): 5096–5106. doi:10.1021/bi971707. PMID 9548740. 

Further reading[edit]


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Phosphotriesterase family Provide feedback

No Pfam abstract.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001559

Synonym(s): Paraoxonase, A-esterase, Aryltriphosphatase, Phosphotriesterase, Paraoxon hydrolase

Bacteria such as Brevundimonas diminuta (Pseudomonas diminuta) harbour a plasmid that carries the gene for Aryldialkylphosphatase (EC) (PTE) (also known as parathion hydrolase). This enzyme 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. It acts specifically on synthetic organophosphate triesters and phosphorofluoridates. It does not seem to have a natural occuring substrate and may thus have optimally evolved for utilizing paraoxon.

Aryldialkylphosphatase belongs to a family [PUBMED:9383406, PUBMED:9548740] of enzymes that possess a binuclear zinc metal centre at their active site. The two zinc ions are coordinated by six different residues, six of which being histidines. This family so far includes, in addition to the parathion hydrolase, the following proteins:

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Amidohydrolase (CL0034), which has the following description:

This family includes a large family of metal dependent amidohydrolase enzymes [1].

The clan contains the following 16 members:

A_deaminase Amidohydro_1 Amidohydro_2 Amidohydro_3 Amidohydro_4 Amidohydro_5 DHOase DUF3604 Peptidase_M19 PHP PHP_C PTE RNase_P_p30 TatD_DNase Urease_alpha UxaC

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(4)
Full
(1183)
Representative proteomes NCBI
(791)
Meta
(85)
RP15
(78)
RP35
(132)
RP55
(176)
RP75
(216)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(4)
Full
(1183)
Representative proteomes NCBI
(791)
Meta
(85)
RP15
(78)
RP35
(132)
RP55
(176)
RP75
(216)
Alignment:
Format:
Order:
Sequence:
Gaps:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(4)
Full
(1183)
Representative proteomes NCBI
(791)
Meta
(85)
RP15
(78)
RP35
(132)
RP55
(176)
RP75
(216)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: IPR001559
Previous IDs: none
Type: Domain
Author: Mian N, Bateman A, Griffiths-Jones SR
Number in seed: 4
Number in full: 1183
Average length of the domain: 301.20 aa
Average identity of full alignment: 34 %
Average coverage of the sequence by the domain: 95.71 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.0 20.0
Trusted cut-off 20.0 20.0
Noise cut-off 19.8 19.9
Model length: 308
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

PTE

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PTE domain has been found. There are 100 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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