Binding Site

6-phosphogluconate-binding site (IPR006184)

Short name: 6PGdom_BS

Description

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) [PMID: 2113917, PMID: 6641716]. Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequences are highly conserved [PMID: 1659648]. The protein is a homodimer in which the monomers act independently [PMID: 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 [PMID: 6641716]. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket [PMID: 6641716].

This signature, found in the C-terminal all-alpha domain of 6-phosphogluconate dehydrogenase, contains the 6-phosphogluconate binding site. The NAD-binding domain is described in IPR006115.

GO terms

Biological Process

GO:0055114 oxidation-reduction process
GO:0006098 pentose-phosphate shunt

Molecular Function

GO:0004616 phosphogluconate dehydrogenase (decarboxylating) activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns