General rule information
[?]
Accession |
PRU00700 |
Dates |
27-MAR-2008 (Created) 21-NOV-2019 (Last updated, Version 17) |
Predictors |
PROSITE; PS51368; UREASE_3
|
Function |
Urease (EC 3.5.1.5) is a nickel-binding enzyme that catalyzes the hydrolysis of urea to carbon dioxide and ammonia. The urease domain forms an (alpha beta)(8) barrel structure that binds two nickel ions and with a histidine that is catalytically involved. |
Propagated annotation
[?]
case <FT:2> and <FTGroup:1> and <FTGroup:2> and not <OC:Bacteria> and not <OC:Archaea>
+ AltName: Full=Urease;
EC 3.5.1.5;
AltName: Full=Urea amidohydrolase; |
end case
case <FT:2> and <FTGroup:1> and <FTGroup:2>
end case
case <FTGroup:1> or <FTGroup:2>
Cofactor |
Ni(2+) Note: Binds #(nickel,ion) per subunit. |
end case
case <OC:Bacteria>
Subcellular location |
Cytoplasm. |
end case
case <OC:Eukaryota> and <AnyFeature:Nter~350,~PS51368>
Similarity |
In the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family. |
else
Similarity |
Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family. |
end case
case <FT:3> and <FT:4>
end case
case <FT:2>
end case
case <FT:2>
GO:0016787; Molecular function: hydrolase activity.
end case
case <FTGroup:1> or <FTGroup:2>
GO:0046872; Molecular function: metal ion binding.
GO:0016151; Molecular function: nickel cation binding.
end case
case <OC:Bacteria>
end case
case <OC:Bacteria>
end case
case <FT:2>
end case
case <FTGroup:1> or <FTGroup:2>
end case
From: PS51368 |
Key
|
|
From
|
|
To
|
|
Description
|
|
Tag
|
|
Condition
|
|
FTGroup
|
DOMAIN
|
|
from
|
|
to
|
|
Urease #
|
|
|
|
|
|
|
ACT_SITE
|
|
192
|
|
192
|
|
Proton donor
|
|
|
|
H
|
|
|
METAL
|
|
6
|
|
6
|
|
Nickel #2
|
|
|
|
H
|
|
2
|
METAL
|
|
8
|
|
8
|
|
Nickel #2
|
|
|
|
H
|
|
2
|
METAL
|
|
89
|
|
89
|
|
Nickel #1; via carbamate group
|
|
|
|
K
|
|
1
|
METAL
|
|
89
|
|
89
|
|
Nickel #2; via carbamate group
|
|
|
|
K
|
|
2
|
METAL
|
|
118
|
|
118
|
|
Nickel #1
|
|
|
|
H
|
|
1
|
METAL
|
|
144
|
|
144
|
|
Nickel #1
|
|
|
|
H
|
|
1
|
METAL
|
|
232
|
|
232
|
|
Nickel #2
|
|
|
|
D
|
|
2
|
BINDING
|
|
91
|
|
91
|
|
Substrate
|
|
|
|
H
|
|
|
Additional information
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Size range |
420-470 amino acids |
Related rules |
None |
Repeats |
1 |
Topology |
Undefined |
Example |
Q5KCQ6 (UREA_CRYNE) |
Scope |
Eukaryota
Bacteria
Archaea |
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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