S
IPR006184

6-phosphogluconate-binding site

InterPro entry
Short name6PGdom_BS

Description

6-Phosphogluconate dehydrogenase (
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)
[1, 2]
. Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequences are highly conserved
[3]
. The protein is a homodimer in which the monomers act independently
[2]
: each contains a large, mainly α-helical domain and a smaller β-α-β domain, containing a mixed parallel and anti-parallel 6-stranded β sheet
[2]
. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket
[2]
.

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
.

References

1.Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase. Broedel SE Jr, Wolf RE Jr. J. Bacteriol. 172, 4023-31, (1990). View articlePMID: 2113917

2.The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution. Adams MJ, Archibald IG, Bugg CE, Carne A, Gover S, Helliwell JR, Pickersgill RW, White SW. EMBO J. 2, 1009-14, (1983). View articlePMID: 6641716

3.Analysis of the gluconate (gnt) operon of Bacillus subtilis. Reizer A, Deutscher J, Saier MH Jr, Reizer J. Mol. Microbiol. 5, 1081-9, (1991). View articlePMID: 1659648

GO terms

Cross References

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