General rule information
[?]
Accession |
PRU00679 |
Dates |
18-DEC-2007 (Created) 21-NOV-2019 (Last updated, Version 7) |
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
[?]
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. |
case <FTGroup:1>
PROSITE |
PS01322; PHOSPHOTRIESTERASE_1; 1; |
end case
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.
end case
From: PS51347 |
Key
|
|
From
|
|
To
|
|
Description
|
|
Tag
|
|
Condition
|
|
FTGroup
|
METAL
|
|
21
|
|
21
|
|
Zinc #1
|
|
|
|
H
|
|
1
|
METAL
|
|
23
|
|
23
|
|
Zinc #1
|
|
|
|
H
|
|
1
|
METAL
|
|
142
|
|
142
|
|
Zinc #1; via carbamate group
|
|
|
|
[KE]
|
|
1
|
METAL
|
|
142
|
|
142
|
|
Zinc #2; via carbamate group
|
|
|
|
[KE]
|
|
2
|
METAL
|
|
175
|
|
175
|
|
Zinc #2
|
|
|
|
H
|
|
2
|
METAL
|
|
204
|
|
204
|
|
Zinc #2
|
|
|
|
H
|
|
2
|
METAL
|
|
263
|
|
263
|
|
Zinc #1
|
|
|
|
D
|
|
1
|
MOD_RES
|
|
142
|
|
142
|
|
N6-carboxylysine
|
|
|
|
K
|
|
|
Additional information
[?]
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
[?]