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InterPro: IPR006183 6-phosphogluconate dehydrogenase

Protein matchesHelp
UniProtKB
Matches:
3250 proteins
AccessionHelp IPR006183 6-phosphogluconate_DH
SecondaryHelp IPR001744 , IPR006112
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR004849 6-phosphogluconate dehydrogenase related protein
IPR006113 6-phosphogluconate dehydrogenase, decarboxylating
Contains IPR002204 3-hydroxyisobutyrate dehydrogenase-related, conserved site
IPR006114 6-phosphogluconate dehydrogenase, C-terminal
IPR006115 6-phosphogluconate dehydrogenase, NAD-binding
IPR006184 6-phosphogluconate-binding site
IPR015815 3-hydroxyacid dehydrogenase/reductase
GO Term annotationHelp
Process GO:0006098 pentose-phosphate shunt
GO:0055114 oxidation reduction
Function GO:0004616 phosphogluconate dehydrogenase (decarboxylating) activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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) [1, 2]. Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequence are highly conserved [3]. The protein is a homodimer in which the monomers act independently [2]: 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 [2]. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket [2].

Structural linksHelp
SCOP: a.100.1.1 , c.2.1.6
Database linksHelp
Enzyme: EC:1.1.1.44
Blocks: IPB006183

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006183 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial

P38720 6-phosphogluconate dehydrogenase, decarboxylating 1

P41572 6-phosphogluconate dehydrogenase, decarboxylating

Q17761 6-phosphogluconate dehydrogenase, decarboxylating

Q99L13 3-hydroxyisobutyrate dehydrogenase, mitochondrial

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002204 3-hydroxyisobutyrate dehydrogenase-related, conserved site
IPR012284 Fibritin/6-phosphogluconate dehydrogenase, C-terminal extension
IPR008927 6-phosphogluconate dehydrogenase, C-terminal-like
IPR016040 NAD(P)-binding domain
IPR015815 3-hydroxyacid dehydrogenase/reductase
IPR006113 6-phosphogluconate dehydrogenase, decarboxylating
IPR006114 6-phosphogluconate dehydrogenase, C-terminal
IPR006115 6-phosphogluconate dehydrogenase, NAD-binding
IPR006183 6-phosphogluconate dehydrogenase
IPR013328 Dehydrogenase, multihelical
IPR006184 6-phosphogluconate-binding site
IPR011548 3-hydroxyisobutyrate dehydrogenase
PDB Chain
ModBase
CATH Domain
SWISS-MODEL

PublicationsHelp
1. Broedel SE Jr, Wolf RE Jr.
Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase.
J. Bacteriol. 172 4023-31 1990 [PubMed: 2113917]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=2113917&action=stream&blobtype=pdf
2. Adams MJ, Archibald IG, Bugg CE, Carne A, Gover S, Helliwell JR, Pickersgill RW, White SW.
The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution.
EMBO J. 2 1009-14 1983 [PubMed: 6641716]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=6641716
3. Reizer A, Deutscher J, Saier MH Jr, Reizer J.
Analysis of the gluconate (gnt) operon of Bacillus subtilis.
Mol. Microbiol. 5 1081-9 1991 [PubMed: 1659648]
http://dx.doi.org/10.1111/j.1365-2958.1991.tb01880.x

Additional ReadingHelp
He W, Wang Y, Liu W, Zhou CZ.
Crystal structure of Saccharomyces cerevisiae 6-phosphogluconate dehydrogenase Gnd1.
BMC Struct. Biol. 7 2007 38 [PubMed: 17570834]
http://dx.doi.org/10.1186/1472-6807-7-38
Sundaramoorthy R, Iulek J, Barrett MP, Bidet O, Ruda GF, Gilbert IH, Hunter WN.
Crystal structures of a bacterial 6-phosphogluconate dehydrogenase reveal aspects of specificity, mechanism and mode of inhibition by analogues of high-energy reaction intermediates.
FEBS J. 274 2007 275-86 [PubMed: 17222187]
http://dx.doi.org/10.1111/j.1742-4658.2006.05585.x
Adams MJ, Ellis GH, Gover S, Naylor CE, Phillips C.
Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism.
Structure 2 1994 651-68 [PubMed: 7922042]
http://dx.doi.org/10.1016/S0969-2126(00)00066-6
Phillips C, Dohnalek J, Gover S, Barrett MP, Adams MJ.
A 2.8 A resolution structure of 6-phosphogluconate dehydrogenase from the protozoan parasite Trypanosoma brucei: comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues.
J. Mol. Biol. 282 1998 667-81 [PubMed: 9737929]
http://dx.doi.org/10.1006/jmbi.1998.2059
Osipiuk J, Zhou M, Moy S, Collart F, Joachimiak A.
X-Ray crystal structure of GarR-tartronate semialdehyde reductase from Salmonella typhimurium.
J. Struct. Funct. Genomics 2009 [PubMed: 19184529]
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InterPro 23.1