6-Phosphogluconate dehydrogenase
| 6PGD | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Crystallographic structure of sheep 6-phosphogluconate dehydrogenase complexed with adenosine 2'-monophosphate | |||||||||
| Identifiers | |||||||||
| Symbol | 6PGD | ||||||||
| Pfam | PF00393 | ||||||||
| Pfam clan | CL0106 | ||||||||
| InterPro | IPR006114 | ||||||||
| PROSITE | PDOC00390 | ||||||||
| SCOP2 | 2pgd / SCOPe / SUPFAM | ||||||||
| |||||||||
| Phosphogluconate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
6-phosphogluconate dehydrogenase dimer, Ovis aries | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.1.44 | ||||||||
| CAS no. | 9001-82-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| phosphogluconate dehydrogenase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | PGD | ||||||
| NCBI gene | 5226 | ||||||
| HGNC | 8891 | ||||||
| OMIM | 172200 | ||||||
| RefSeq | NM_002631 | ||||||
| UniProt | P52209 | ||||||
| Other data | |||||||
| EC number | 1.1.1.44 | ||||||
| Locus | Chr. 1 p36.3-36.13 | ||||||
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6-Phosphogluconate dehydrogenase (6PGD) is an enzyme in the pentose phosphate pathway. It forms ribulose 5-phosphate from 6-phosphogluconate:
- 6-phospho-D-gluconate + NAD(P)+ D-Ribulose 5-phosphate + CO2 + NAD(P)H + H+
It is an oxidative carboxylase that catalyses the oxidative decarboxylation 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). Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequences are highly conserved. The protein is a homodimer in which the monomers act independently: 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. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket.