6PGD

6-phosphogluconate dehydrogenase, C-terminal domain
6PGD
SMART accession number:SM01350
Description: This family represents the C-terminal all-alpha domain of 6-phosphogluconate dehydrogenase. The domain contains two structural repeats of 5 helices each.
Interpro abstract (IPR006114):

6-Phosphogluconate dehydrogenase (EC 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) [(PUBMED:2113917), (PUBMED:6641716)]. Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequences 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 entry represents the C-terminal all-alpha domain of 6-phosphogluconate dehydrogenase. The domain contains two structural repeats of 5 helices each. The NAD-binding domain is described in IPR006115.

GO process:oxidation-reduction process (GO:0055114), pentose-phosphate shunt (GO:0006098)
GO function:phosphogluconate dehydrogenase (decarboxylating) activity (GO:0004616)
Family alignment:
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There are 19935 6PGD domains in 19931 proteins in SMART's nrdb database.

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