NAD_binding_2

The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossman fold.

6-Phosphogluconate dehydrogenase () (6PGD) is an oxidative carboxylase that catalyses the decarboxylating reduction of 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP. This reaction is a component of the hexose mono-phosphate shunt and pentose phosphate pathways (PPP) PUBMED:2113917, PUBMED:6641716. Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequence are highly conserved PUBMED:1659648. The protein is a homodimer in which the monomers act independently PUBMED:6641716: each contains a large, mainly alpha-helical domain and a smaller beta-alpha-beta domain, containing a mixed parallel and anti-parallel 6-stranded beta sheet PUBMED:6641716. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket PUBMED:6641716.

This family represents the NAD binding domain of 6-phosphogluconate dehydrogenase which adopts a Rossman fold. The C-terminal domain is described in .

Alignment

Visualize domain structures

Species distribution