Family

6-phosphogluconate dehydrogenase (IPR006183)

Short name: Pgluconate_DH

Family relationships

Description

This entry represents prokaryotic and eukaryotic 6PGD and a truncated prokaryotic 6PGD that lacks of a central region of about 140 residues, such as yqeC from Bacillus subtilis [PMID: 15231785]. Bacillus subtilis contains three classes of 6-phosphogluconate dehydrogenases (6PGD), including Gnd (YqjI), GntZ and YqeC. All of them are included in this entry. YgjiI is NADP+ dependent, while GntZ and YqeC are NAD+-dependent [PMID: 15231785].

6-Phosphogluconate dehydrogenase (EC:1.1.1.44) (6PGD) is a key enzyme that produces NADPH by converting 6-phospho D-gluconolactone to D-ribulose 5-phosphate in the pentose phosphate pathways (PPP) [PMID: 2113917, PMID: 6641716]. NADPH provides the major reducing power required for lipid production and protecting the cell against oxidative stress. 6PGD has been extensively studied with respect to kinetics, regulation, role in pentose-shunt production of NADPH and lipogenesis, and population genetics [PMID: 24726622]. 6PGD is associated with several human disorders including cancer and Alzheimer's disease. The structure of the budding yeast 6PGD (also known as Gnd1) has been revealed [PMID: 17570834].

Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequence 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: 17570834, PMID: 6641716]. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket [PMID: 6641716].

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

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