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NADP(+)-dependent, decarboxylating phosphogluconate dehydrogenase
NADP(+)-dependent decarboxylating phosphogluconate dehydrogenase catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate, as part of the oxidative branch of the pentose phosphate pathway
NAD(P)-binding domain-containing protein
The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold. (from Pfam)
6-phosphogluconate dehydrogenase, C-terminal domain
This family represents the C-terminal all-alpha domain of 6-phosphogluconate dehydrogenase. The domain contains two structural repeats of 5 helices each. (from Pfam)
phosphogluconate dehydrogenase (NAD(+)-dependent, decarboxylating)
This family resembles the larger family (gnd) of bacterial and eukaryotic NADP+-dependent 6-phosphogluconate dehydrogenase (EC 1.1.1.44), but differs from it by a deep split in a UPGMA similarity clustering tree and the lack of a central region of about 140 residues. It differs also in being NAD+-dependent, making this family EC 1.1.1.343. Among complete genomes, it is found is found in Bacillus subtilis and Mycobacterium tuberculosis, both of which also contain gnd, and in Aquifex aeolicus. The protein from Methylobacillus flagellatus KT has been characterized as a decarboxylating 6-phosphogluconate dehydrogenase as part of an unusual formaldehyde oxidation cycle In some sequenced organisms members of this family are the sole 6-phosphogluconate dehydrogenase present and are probably active in the pentose phosphate cycle.
NADP-dependent phosphogluconate dehydrogenase
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