InterPro domain: IPR027250

This entry includes phosphoglycerate kinase-A/B/C (PGK-A/B/C) from euglenozoa.

Phosphoglycerate kinase ( 2.7.2.3 ) (PGK) is an enzyme that catalyses the formation of ATP to ADP and vice versa. In the second step of the second phase in glycolysis, 1,3-diphosphoglycerate is converted to3-phosphoglycerate, forming one molecule of ATP. If the reverse were to occur, one molecule of ADP would be formed. This reaction is essential in most cells for the generation of ATP in aerobes, for fermentation in anaerobes and for carbon fixation in plants.

Trypanosoma brucei and Crithidia fasciculata both contain three different phosphoglycerate kinase (PGK) genes, A, B and C [ 1 ]. The genes B and C encode the major PGKs: the cytosolic and glycosomal PGKs, respectively. The PGK-A genes of both Trypanosomatid species encode open reading frames related to PGK, which have most active site residues conserved, but contain an insert of 80 amino acids at approximately position 80 of the 420 amino acids average PGK sequence [ 2 ]. PGK-A may be a minor PGK with special function [ 3 ].

1. Evidence for gene conversion between the phosphoglycerate kinase genes of Trypanosoma brucei. J. Mol. Biol. 200, 439-47
2. A phosphoglycerate kinase-related gene conserved between Trypanosoma brucei and Crithidia fasciculata. Mol. Biochem. Parasitol. 50, 69-78