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Glutamine amidotransferase domain
This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase. (from Pfam)
This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase. (from Pfam)
asparagine synthase-related protein
Most members of this family are asparagine synthase, which catalyzes conversion of aspartate to asparagine. Exceptions that score well against the HMM include isopeptide bond formation proteins for lasso peptide biosynthesis. But note that many additional proteins, such as the 7-cyano-7-deazaguanine synthase QueC, hit with scores barely above the model's cutoff scores to N-terminal regions about 60 amino acids long, whereas the full length of the model is 355.
asparagine synthase (glutamine-hydrolyzing)
This HMM describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff.
asparagine synthetase B family protein
asparagine synthetase B (glutamine-hydrolyzing) family protein may catalyze the ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen
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