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PMID:17951375

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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

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

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

RHORT:Q2RSQ7

enables

GO:0051920: peroxiredoxin activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

RHORT:Q2RSQ7

GO:0051920: peroxiredoxin activity

ECO:0000314:

F

Figure 3 shows peroxidase activities of the GlnE.

complete
CACAO 3380


See also

References

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