AsnA

• PFAM accession number: PF03590
• Interpro abstract (IPR004618):

  Aspartate--ammonia ligase (asparagine synthetase) EC 6.3.1.1 catalyses the conversion of L-aspartate to L-asparagine in the presence of ATP and ammonia. This family represents one of the two non-homologous forms of aspartate--ammonia ligase found in Escherichia coli. This type is also found in Haemophilus influenzae, Treponema pallidum and Lactobacillus delbrueckii, but appears to have a very limited distribution. The fact that the protein from the H. influenzae is more than 70% identical to that from the spirochete T. pallidum, but less than 65% identical to that from the closely related E. coli, strongly suggests lateral transfer.

  AsnA is a homodimeric enzyme which is structurally similiar to the catalytic core domain of class II aminoacyl-tRNA synthetases. Ammonia-dependent AsnA is not homologous to the glutamine-dependent asparagine synthetase AsnB [ (PUBMED:1346128) ].

• GO process: asparagine biosynthetic process (GO:0006529)
• GO component: cytoplasm (GO:0005737)
• GO function: aspartate-ammonia ligase activity (GO:0004071)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry AsnA