InterPro domain: IPR007803

Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase (P3H) hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. PH3 folds into two domains, anN-terminal domain containing 10 beta strands and a C-terminal helical domain. The N-terminal domain contains the distorted jelly roll beta sheet core [ 1 ]. A similar domain is also found in aspartyl/asparaginyl beta-hydroxylase, which hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins [ 2 ].

1. Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases. Eur. J. Biochem. 268, 6625-36
2. A fully active catalytic domain of bovine aspartyl (asparaginyl) beta-hydroxylase expressed in Escherichia coli: characterization and evidence for the identification of an active-site region in vertebrate alpha-ketoglutarate-dependent dioxygenases. Proc. Natl. Acad. Sci. U.S.A. 91, 7227-31