Protein Family Models

This entry represents the dimerisation domain found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) and related sequences not included in Pfam:PF02774 [1-3]. Paper describing PDB structure 2cvo. [1]. 16240442. Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa). Nonaka T, Kita A, Miura-Ohnuma J, Katoh E, Inagaki N, Yamazaki T, Miki K;. Proteins. 2005;61:1137-1140. Paper describing PDB structure 2i3a. [2]. 17316682. Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase from Mycobacterium tuberculosis in complex with NADP(+). Cherney LT, Cherney MM, Garen CR, Niu C, Moradian F, James MN;. J Mol Biol. 2007;367:1357-1369. Paper describing PDB structure 5ein. [3]. 26966182. Crystal Structure of the LysY.LysW Complex from Thermus thermophilus. Shimizu T, Tomita T, Kuzuyama T, Nishiyama M;. J Biol Chem. 2016;291:9948-9959. (from Pfam)

Date:

2024-10-16

This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase [1]. 10369777. Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R;. J Mol Biol 1999;289:991-1002. (from Pfam)

Date:

2024-10-16

This HMM represents the less common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step of Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment.

Gene:

argC

Date:

2024-05-30