| Primary Identifier | IPR000965 | Type | Domain |
| Short Name | GPR_dom |
| description | Gamma-glutamyl phosphate reductase () (GPR) is the enzyme that catalyses the second step in the biosynthesis of proline from glutamate, the NADP-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. In bacteria (gene proA) and yeast [](gene PRO2), GPR is a monofunctional protein, while in plants and mammals, it is a bifunctional enzyme (P5CS) []that consists of two domains, an N-terminal glutamate 5-kinase domain () and a C-terminal GPR domain. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine []. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1) [].This entry represents the C-terminal GPR domain of the gamma-glutamyl phosphate reductase. |
