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PMID:17951375
Citation |
Jonsson, A, Teixeira, PF and Nordlund, S (2008) A novel peroxiredoxin activity is located within the C-terminal end of Rhodospirillum rubrum adenylyltransferase. J. Bacteriol. 190:434-7 |
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Abstract |
Adenylyltransferase (GlnE) catalyzes the reversible adenylylation of glutamine synthetase. In this report we present, for the first time, evidence for a peroxiredoxin activity of Rhodospirillum rubrum GlnE, through the carboxyl-terminal AhpC/thiol-specific antioxidant (TSA) domain. The combination of GlnE and AhpC/TSA domains within the same polypeptide constitutes a unique domain architecture that has not previously been identified among proteobacteria. |
Links |
PubMed PMC2223739 Online version:10.1128/JB.01058-07 |
Keywords |
Catalytic Domain; Escherichia coli/enzymology; Escherichia coli/metabolism; Glutamate-Ammonia Ligase/metabolism; Hydrogen Peroxide/metabolism; Kinetics; Nicotinamide-Nucleotide Adenylyltransferase/chemistry; Nicotinamide-Nucleotide Adenylyltransferase/metabolism; Peroxidases/metabolism; Peroxiredoxins/metabolism; Photosynthesis; Reactive Oxygen Species/metabolism; Rhodospirillum rubrum/enzymology |
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Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|
enables |
GO:0051920: peroxiredoxin activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
GO:0051920: peroxiredoxin activity |
ECO:0000314: |
F |
Figure 3 shows peroxidase activities of the GlnE. |
complete | ||||
See also
References
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