GPR domain (IPR000965)

Short name: GPR_dom

Overlapping homologous superfamilies

Domain relationships


Gamma-glutamyl phosphate reductase (EC: (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 [PMID: 8896266] (gene PRO2), GPR is a monofunctional protein, while in plants and mammals, it is a bifunctional enzyme (P5CS) [PMID: 1384052] that consists of two domains, an N-terminal glutamate 5-kinase domain (EC: 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 [PMID: 10037775]. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1) [PMID: 9765552].

This entry represents the C-terminal GPR domain of the gamma-glutamyl phosphate reductase.

GO terms

Biological Process

GO:0055114 oxidation-reduction process
GO:0006561 proline biosynthetic process

Molecular Function

GO:0004350 glutamate-5-semialdehyde dehydrogenase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.