We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU00679
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00679
General rule information
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| Accession | PRU00679 |
| Dates | 18-DEC-2007 (Created)
19-NOV-2022 (Last updated, Version 10) |
| 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. |
| Scope(s) |
Eukaryota Bacteria |
| Example(s) | P0A433; |
Propagated annotation
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Comments
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| case <FTGroup:1> and <FTGroup:2> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; |
| end case | |
| SIMILARITY | Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family. |
Keywords
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| Hydrolase | |
| Metal-binding | |
| Zinc | |
| 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 | |
Cross-references
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| PROSITE | PS01322; PHOSPHOTRIESTERASE_1; 1; |
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 | /note="N6-carboxylysine" | K | ||||||||
Additional information
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| Size range | 280-360 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
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