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PylC-like, N-terminal domain
This domain is found in 3-methyl-D-ornithine--L-lysine ligase from Methanosarcina barkeri (PylC) and similar sequences from prokaryotes. PylC is required for the biosynthesis of pyrrolysine. This ATP-grasp enzyme is composed of three domains. This entry represents the N-terminal domain, which is composed of a central four-stranded beta-sheet that is faced on both sides by two helices. It shows an adenine binding pocket that has not been observed in any homologous structure determined before [1]. Paper describing PDB structure 4ffl. [1]. 22985965. Biosynthesis of the 22nd genetically encoded amino acid pyrrolysine: structure and reaction mechanism of PylC at 1.5A resolution. Quitterer F, List A, Beck P, Bacher A, Groll M;. J Mol Biol. 2012;424:270-282. (from Pfam)
ATP-grasp domain-containing protein
This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response [1]. [1]. 23044854. Ter-dependent stress response systems: novel pathways related to metal sensing, production of a nucleoside-like metabolite, and DNA-processing. Anantharaman V, Iyer LM, Aravind L;. Mol Biosyst. 2012;8:3142-3165. (from Pfam)
No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman). (from Pfam)
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