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YheC/YheD family protein
A member of the ATP-grasp fold predicted to be involved in the modification/biosynthesis of spore-wall and capsular proteins [1]. [1]. 20023723. Amidoligases with ATP-grasp, glutamine synthetase-like and acetyltransferase-like domains: synthesis of novel metabolites and peptide modifications of proteins. Iyer LM, Abhiman S, Maxwell Burroughs A, Aravind L;. Mol Biosyst. 2009;5:1636-1660. (from Pfam)
RimK-like ATP-grasp domain
This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK [1]. [1]. 9416615. A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Galperin MY, Koonin EV;. Protein Sci 1997;6:2639-2643. (from Pfam)
Prokaryotic glutathione synthetase, N-terminal domain
Prokaryotic glutathione synthetase, ATP-grasp domain
glutathione synthase
glutathione synthase catalyzes the conversion from ATP, gamma-L-glutamyl-L-cysteine and glycine to ADP, phosphate and glutathione
Catalyzes the second step in the glutathione biosynthesis pathway, where it synthesizes ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
This model was built using glutathione synthetases found in Gram-negative bacteria. This gene does not appear to be present in genomes of Gram-positive bacteria. Glutathione synthetase has an ATP-binding domain in the COOH terminus and catalyzes the second step in the glutathione biosynthesis pathway: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione. Glutathione is a tripeptide that functions as a reductant in many cellular reactions.
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