<p>6-Phosphogluconate dehydrogenase (<db_xref db="EC" dbkey="1.1.1.44"/>) (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) [<cite idref="PUB00002112"/>, <cite idref="PUB00001132"/>]. Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequence are highly conserved [<cite idref="PUB00003806"/>]. The protein is a homodimer in which the monomers act independently [<cite idref="PUB00001132"/>]: 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 [<cite idref="PUB00001132"/>]. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket [<cite idref="PUB00001132"/>]. </p> <p> This family represents the NADP binding domain of 6-phosphogluconate dehydrogenase which adopts a Rossman fold. The C-terminal domain is described in <db_xref db="INTERPRO" dbkey="IPR006114"/>.</p>