IPR006184
6-phosphogluconate-binding site
InterPro entry
Short name | 6PGdom_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
biological process
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- PROSITE patterns:PS00461