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NAD synthase
NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation. [1]. 8895556. Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis. Rizzi M, Nessi C, Mattevi A, Coda A, Bolognesi M, Galizzi A;. EMBO J 1996;15:5125-5134. (from Pfam)
nitrilase-related carbon-nitrogen hydrolase
This family contains hydrolases that break carbon-nitrogen bonds [1]. The family includes: Nitrilase EC:3.5.5.1 Swiss:Q42965, Aliphatic amidase EC:3.5.1.4 Swiss:Q01360, Biotidinase EC:3.5.1.12 Swiss:P43251, Beta-ureidopropionase EC:3.5.1.6 Swiss:Q03248. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins [2]. [1]. 7987228. A new family of carbon-nitrogen hydrolases. Bork P, Koonin EV;. Protein Sci 1994;3:1344-1346. [2]. 11380987. The nitrilase superfamily: classification, structure and function. Pace HC, Brenner C;. Genome Biol 2001;2:REVIEWS0001. (from Pfam)
glutamine-dependent NAD(+) synthetase
glutamine-dependent NAD(+) synthetase catalyzes the ATP-dependent amidation of deamido-NAD to form NAD; uses L-glutamine as a nitrogen source
NAD(+) synthase
Catalyzes the formation of nicotinamide adenine dinucleotide (NAD) from nicotinic acid adenine dinucleotide (NAAD) using either ammonia or glutamine as the amide donor and ATP
NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity.
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