Member database | Pfam |
Pfam type | domain |
Short name | Pro_3_hydrox_C |
Author | Finn RD;0000-0001-8626-2148 |
Sequence Ontology | 0000417 |
Description
Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure contains 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. The structure differs significantly from many other 2-OG oxygenases in possessing a discrete C-terminal helical domain.
References
1. Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases. Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ. Eur. J. Biochem. 268, 6625-36, (2001). View articlePMID: 11737217