6-phosphogluconate dehydrogenase, decarboxylating (PGD)

The protein contains 483 amino acids for an estimated molecular weight of 53140 Da.

 

Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. (updated: April 1, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 100%
Model score: 100
No model available.

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VariantDescription
dbSNP:rs11547610

The reference OMIM entry for this protein is 172200

6-@phosphogluconate dehydrogenase, erythrocyte; pgd
Pgd, erythrocyte; 6pgd

Brewer and Dern (1964) reported deficiency of 6-phosphogluconate dehydrogenase (6PGD), the second dehydrogenase in the pentose phosphate shunt, in 10 members of 4 generations of an American black family. They concluded that the inheritance is autosomal dominant, all 6PGD-deficient persons observed being heterozygotes. However, no male-to-male transmission was observed; indeed, no offspring of affected males were tested. Against X-linkage is the fact that the average enzyme level in 3 6PGD-deficient males was somewhat higher than that in seven 6PGD-deficient females. The opposite would be expected of an X-linked trait. The authors commented on the autosomal control of an enzyme that is closely related metabolically to G6PD, an enzyme determined by an X-linked gene. In a survey of unrelated persons, Dern et al. (1966) found in 3 of 873 American blacks and 2 of 275 Caucasians a reduction in erythrocyte 6-phosphogluconate dehydrogenase to the range of 42 to 65% of normal. Leukocyte enzyme was also reduced. No correlation was found between electrophoretic phenotype and the quantitative variation. The inheritance was clearly autosomal dominant. Using starch-gel electrophoresis, Fildes and Parr (1963) detected 2 distinct types of human red cell 6-phosphogluconate dehydrogenase. Ten of 150 random blood samples showed 2 broad, less distinct bands in contrast to the single narrow, sharp band in the remainder. Inheritance appears to be autosomal, a point of particular note. Since the G6PD locus is X-linked, these 2 functionally related genes do not show clustering. Heterozygotes and homozygotes showed no quantitative difference in red blood cell 6PGD activity. Deficiency of this enzyme, with or without electrophoretic abnormality, has been observed (Parr, 1966). Nevo (1989) identified a rare PGD variant called PGD Mediterranean. Severe deficiency of 6PGD, although well-documented (Brewer and Dern, 1964; Dern et al., 1966; Parr and Fitch, 1967), has never been incriminated as the cause of hemolytic anemia. In fact, persons with less than 5% of normal activity in red cell enzymes, who were found in population surveys by Parr and Fitch (1967), were entirely asymptomatic. A possibility of linkage between the Rhesus and 6PGD loci was found by Weitkamp et al. (1970). This has since been fully confirmed (Weitkamp et al., 1971). Weitkamp (1972) gave valid criticism of the conclusions of linkage studies of 2 groups. It is clear, however, that the Rhesus and 6PGD loci are on chromosome 1. Douglas et al. (1973) demonstrated that the PGM1 and 6PGD loci are on the distal end of the short arm of chromosome 1. Assuming that each arm of chromosome 1 is 140 male cM long, Cook et al. (1974) concluded that, measured from the centromere, map positions are as follows: PGD, 1p124; RH, 1p109; PGM1, 1p079; FY, 1p010; PEPC, 1q030. At HGM8, Povey et al. (1985) concluded that the smallest region of overlap for PGD is 1p36.2-p36.13. Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988). ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 15, 2016: Protein entry updated
Automatic update: OMIM entry 172200 was added.

Jan. 27, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed