Aspartyl/asparaginy/proline hydroxylase (IPR007803)

Short name: Asp/Arg/Pro-Hydrxlase

Overlapping homologous superfamilies

Domain relationships



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, an N-terminal domain containing 10 beta strands and a C-terminal helical domain. The N-terminal domain contains the distorted jelly roll beta sheet core [PMID: 11737217]. 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 [PMID: 8041771].

GO terms

Biological Process

GO:0018193 peptidyl-amino acid modification

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

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