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29  structures 1270  species 3  interactions 1944  sequences 22  architectures

Family: G6PD_C (PF02781)

Summary: Glucose-6-phosphate dehydrogenase, C-terminal domain

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This is the Wikipedia entry entitled "Glucose-6-phosphate dehydrogenase". More...

Glucose-6-phosphate dehydrogenase Edit Wikipedia article

Glucose-6-phosphate dehydrogenase
EC number
CAS number 9001-40-5
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Glucose-6-phosphate dehydrogenase, NAD binding domain
PDB 1dpg EBI.jpg
glucose 6-phosphate dehydrogenase from leuconostoc mesenteroides
Symbol G6PD_N
Pfam PF00479
Pfam clan CL0063
InterPro IPR022674
SCOP 1dpg
Glucose-6-phosphate dehydrogenase, C-terminal domain
Symbol G6PD_C
Pfam PF02781
SCOP 1dpg
Glucose-6-phosphate dehydrogenase
Protein G6PD PDB 1qki.png
PDB rendering based on 1qki.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols G6PD ; G6PD1
External IDs OMIM305900 MGI105979 HomoloGene37906 ChEMBL: 5347 GeneCards: G6PD Gene
EC number
RNA expression pattern
PBB GE G6PD 202275 at tn.png
More reference expression data
Species Human Mouse
Entrez 2539 14381
Ensembl ENSG00000160211 ENSMUSG00000031400
UniProt P11413 Q00612
RefSeq (mRNA) NM_000402 NM_008062
RefSeq (protein) NP_000393 NP_032088
Location (UCSC) Chr X:
154.53 – 154.55 Mb
Chr X:
74.41 – 74.43 Mb
PubMed search [1] [2]

Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC is a cytosolic enzyme that catalyzes the chemical reaction

D-glucose 6-phosphate + NADP+ \rightleftharpoons 6-phospho-D-glucono-1,5-lactone + NADPH + H+

This enzyme is in the pentose phosphate pathway (see image), a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). The NADPH in turn maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. Of greater quantitative importance is the production of NADPH for tissues actively engaged in biosynthesis of fatty acids and/or isoprenoids, such as the liver, mammary glands, adipose tissue, and the adrenal glands. G6PD reduces nicotinamide adenine dinucleotide phosphate (NADP) to NADPH while oxidizing glucose-6-phosphate.[1]

It is notable in humans when there is a genetic deficiency of G6PD which predisposes to non-immune hemolytic anemia .

Species distribution

G6PD is widely distributed in many species from bacteria to humans. In higher plants, several isoforms of G6PDH have been reported, which are localized in the cytosol, the plastidic stroma, and peroxisomes.[2] Among humans, G6PD is common in certain insular groups, such as Parsis.[3]


Glucose-6-phosphate dehydrogenase is stimulated by its substrate Glucose 6 Phosphate. The usual ratio of NADPH/NADP+ in the cytosol of tissues engaged in biosyntheses is about 100/1. Increased utilization of NADPH for fatty acid biosynthesis will dramatically increase the level of NADP+, thus stimulating G6PD to produce more NADPH.

G6PD converts glucose-6-phosphate into 6-phosphoglucono-δ-lactone and is the rate-limiting enzyme of the pentose phosphate pathway.

G6PD is one of a number of glycolytic enzymes activated by the transcription factor Hypoxia-inducible factor 1 (HIF1).[4]

Clinical significance

G6PD is remarkable for its genetic diversity. Many variants of G6PD, mostly produced from missense mutations, have been described with wide ranging levels of enzyme activity and associated clinical symptoms. Two transcript variants encoding different isoforms have been found for this gene.[5]

Glucose-6-phosphate dehydrogenase deficiency is very common worldwide, and causes acute hemolytic anemia in the presence of simple infection, ingestion of fava beans, or reaction with certain medicines, antibiotics, antipyretics, and antimalarials.[6]

Pathology of G6PD deficiency.png

Cell growth and proliferation are affected by G6PD.[7] G6PD inhibitors are under investigation to treat cancers and other conditions.[4] DHEA is a G6PD inhibitor.[7]

List of medicines which cause lysis in G6PD

Note that this list doesn't contain all the medicines which cause hemolysis:[citation needed]

See also


  1. ^ Aster J, Kumar V, Robbins SL, Abbas AK, Fausto N, Cotran RS (2010). Robbins and Cotran pathologic basis of disease. Saunders/Elsevier. pp. Kindle Locations 33340–33341. ISBN 1-4160-3121-9. 
  2. ^ Corpas FJ, Barroso JB, Sandalio LM, Distefano S, Palma JM, Lupiáñez JA, Del Río LA (March 1998). "A dehydrogenase-mediated recycling system of NADPH in plant peroxisomes". Biochem. J. 330 (Pt 2): 777–84. PMC 1219205. PMID 9480890. 
  3. ^ "G6PD Enzyme Deficiency". Retrieved October 24, 2014. 
  4. ^ a b de Lartigue J (2012-06-12). "Cancer Research Moves Beyond the Original Hallmarks of Cancer". OncLive. 
  5. ^ "Entrez Gene: G6PD glucose-6-phosphate dehydrogenase". 
  6. ^ Cappellini MD, Fiorelli G (January 2008). "Glucose-6-phosphate dehydrogenase deficiency". Lancet 371 (9606): 64–74. doi:10.1016/S0140-6736(08)60073-2. PMID 18177777. 
  7. ^ a b Tian WN, Braunstein LD, Pang J, Stuhlmeier KM, Xi QC, Tian X, Stanton RC (April 1998). "Importance of glucose-6-phosphate dehydrogenase activity for cell growth". J. Biol. Chem. 273 (17): 10609–17. doi:10.1074/jbc.273.17.10609. PMID 9553122. 

Further reading

  • Vulliamy T, Beutler E, Luzzatto L (1993). "Variants of glucose-6-phosphate dehydrogenase are due to missense mutations spread throughout the coding region of the gene". Hum. Mutat. 2 (3): 159–67. doi:10.1002/humu.1380020302. PMID 8364584. 
  • Mason PJ (1996). "New insights into G6PD deficiency". Br. J. Haematol. 94 (4): 585–91. PMID 8826878. 
  • Wajcman H, Galactéros F (2004). "[Glucose 6-phosphate dehydrogenase deficiency: a protection against malaria and a risk for hemolytic accidents]". C. R. Biol. 327 (8): 711–20. doi:10.1016/j.crvi.2004.07.010. PMID 15506519. 

External links

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Glucose-6-phosphate dehydrogenase, C-terminal domain Provide feedback

No Pfam abstract.

Literature references

  1. Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR; , Biochemistry. 1998;37:2759-2767.: On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. PUBMED:9485426 EPMC:9485426

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR022675

Glucose-6-phosphate dehydrogenase (EC) (G6PDH) is a ubiquitous protein, present in bacteria and all eukaryotic cell types [PUBMED:2838391]. The enzyme catalyses the the first step in the pentose pathway, i.e. the conversion of glucose-6-phosphate to gluconolactone 6-phosphate in the presence of NADP, producing NADPH. The ubiquitous expression of the enzyme gives it a major role in the production of NADPH for the many NADPH-mediated reductive processes in all cells [PUBMED:3393536]. Deficiency of G6PDH is a common genetic abnormality affecting millions of people worldwide. Many sequence variants, most caused by single point mutations, are known, exhibiting a wide variety of phenotypes [PUBMED:3393536].

This entry represents the C-terminal domain of glucose-6-phosphate dehydrogenase.

Gene Ontology

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Domain organisation

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Seed source: Prosite
Previous IDs: none
Type: Domain
Author: Finn RD, Griffiths-Jones SR
Number in seed: 490
Number in full: 1944
Average length of the domain: 282.10 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 56.20 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.5 19.5
Trusted cut-off 22.1 19.8
Noise cut-off 19.1 18.5
Model length: 289
Family (HMM) version: 13
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Species distribution

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Archea Archea Eukaryota Eukaryota
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the G6PD_C domain has been found. There are 29 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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