PRU00679
General rule information
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Accession | PRU00679 |
Dates | 18-DEC-2007 (Created) 19-NOV-2022 (Last updated, Version 9) |
Data class | Domain |
Predictors | PROSITE; PS51347; PHOSPHOTRIESTERASE_2 |
Name | Phosphotriesterase family |
Function | The enzyme phosphotriesterase (EC 3.1.8.1) (PTE) (also known as parathion hydrolase) belongs to a family of enzymes that possess a binuclear zinc metal center at their active site. The two zinc ions are coordinated by six different residues, four of which being histidines. |
Propagated annotation
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Comments
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case <FTGroup:1> and <FTGroup:2>
Cofactor | Zn(2+) Note: Binds 2 Zn(2+) ions per subunit. |
end case
Similarity | Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family. |
Cross-references
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case <FTGroup:1>
PROSITE | PS01322; PHOSPHOTRIESTERASE_1; 1; |
end case
Gene Ontology
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case <FTGroup:1> or <FTGroup:2>
GO:0016787; Molecular function: hydrolase activity.
GO:0046872; Molecular function: metal ion binding.
GO:0008270; Molecular function: zinc ion binding.
GO:0046872; Molecular function: metal ion binding.
GO:0008270; Molecular function: zinc ion binding.
Keywords
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end case
Features
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From: PS51347 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 21 | 21 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1 | H | 1 | |||||||
BINDING | 23 | 23 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1 | H | 1 | |||||||
BINDING | 142 | 142 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /note="via carbamate group | [KE] | 1 | |||||||
BINDING | 142 | 142 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /note="via carbamate group | [KE] | 2 | |||||||
BINDING | 175 | 175 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2 | H | 2 | |||||||
BINDING | 204 | 204 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2 | H | 2 | |||||||
BINDING | 263 | 263 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1 | D | 1 | |||||||
MOD_RES | 142 | 142 | N6-carboxylysine | K |
Additional information
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Size range | 280-360 amino acids |
Related rules | None |
Repeats | 1 |
Topology | Undefined |
Example | P0A433 (OPD_SPHSA) |
Scope | Eukaryota
Bacteria |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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UniProtKB/Swiss-Prot sets
Archaea [1] Bacteria [8] Eukaryota [24] All [ 33 ]
- Retrieve set of proteins with 3D structure for this domain