InterPro domain: IPR006148

This domain is characteristic of the enzymes 6-phosphogluconolactonase ( 3.1.1.31 ), Glucosamine-6-phosphate isomerase ( 3.5.99.6 ), and Galactosamine-6-phosphate isomerase. 6-Phosphogluconolactonase is the enzyme responsible for the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate, the second step in the pentose phosphate pathway. Glucosamine-6-phosphate isomerase (or Glucosamine 6-phosphate deaminase) is the enzyme responsible for the conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate [ 1 ]. It is the last specific step in the pathway for N-acetylglucosamine (GlcNAC) utilization in bacteria such as Escherichia coli (gene nagB) or in fungi such as Candida albicans (gene NAG1).

1. Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution. Structure 3, 1323-32