ProRule 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. |
| Scope(s) |
Eukaryota Bacteria Archaea |
| Example(s) | P0AB65 (ACYP_ECOLI); |
Propagated annotation
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Identifier, protein and gene names
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| case <FTGroup:1> | |
| Protein name | + RecName: EC=3.6.1.7; |
Comments
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| CATALYTIC ACTIVITY | Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate; Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7; |
| end case | |
Keywords
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Gene Ontology
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| GO:0016787; Molecular function:hydrolase activity |
Cross-references
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Features
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| From: PS51160 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="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 |
| 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 [30] Bacteria [232] Eukaryota [21] All [ 283 ]
- Retrieve set of proteins with 3D structure for this domain