PRU00520
General rule information
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Accession | PRU00520 |
Dates | 13-DEC-2005 (Created) 21-NOV-2019 (Last updated, Version 11) |
Data class | Domain |
Predictors | PROSITE; PS51160; ACYLPHOSPHATASE_3 |
Name | Acylphosphatase-like domain |
Function | Acylphosphatase (EC 3.6.1.7) [1,2] catalyzes the hydrolysis of various acyl phosphate carboxyl-phosphate bonds such as carbamyl phosphate, succinyl phosphate, 1,3-diphosphoglycerate, etc. |
Propagated annotation
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Description
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case <FTGroup:1>
+ RecName: EC 3.6.1.7; |
Comments
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Catalytic activity | RHEA:14965: an acyl phosphate + H2O = a carboxylate + H(+) + phosphate
EC 3.6.1.7 |
end case
Cross-references
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Gene Ontology
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case <FTGroup:1>
GO:0016787; Molecular function: hydrolase activity.
Keywords
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end case
Features
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From: PS51160 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DOMAIN | from | to | Acylphosphatase-like # | |||||||||
ACT_SITE | 16 | 16 | R | 1 | ||||||||
ACT_SITE | 34 | 34 | N | 1 |
Additional information
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Size range | 65-100 amino acids |
Related rules | None |
Repeats | 1 |
Topology | Undefined |
Example | P0AB65 (ACYP_ECOLI) |
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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-
UniProtKB/Swiss-Prot sets
Archaea [30] Bacteria [232] Eukaryota [21] All [ 283 ]
- Retrieve set of proteins with 3D structure for this domain