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Asd/ArgC dimerization domain-containing protein
This Pfam domain model identifies C-terminal domains of N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), aspartate-semialdehyde dehydrogenase (Asd) and a few other, less common enzymes.
Semialdehyde dehydrogenase, NAD binding domain
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)
aspartate-semialdehyde dehydrogenase
Catalyzes the formation of aspartate semialdehyde from aspartyl phosphate
aspartate-semialdehyde dehydrogenase family protein
aspartate-semialdehyde dehydrogenase family protein such as aspartate-semialdehyde dehydrogenase and malonyl-CoA reductase
Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. Separate models are built for the two types in order to exclude the USG-1 protein, found in several species, which is specifically related to the Bacillus subtilis type of aspartate-semialdehyde dehydrogenase. Members of this type are found primarily in organisms that lack peptidoglycan.
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