Protein Family Models

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 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. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins [1]. [1]. 8041771. 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. Jia S, McGinnis K, VanDusen WJ, Burke CJ, Kuo A, Griffin PR, Sardana MK, Elliston KO, Stern AM, Friedman PA;. Proc Natl Acad Sci U S A 1994;91:7227-7231. (from Pfam)

Date:

2024-10-16

aspartyl/asparaginyl beta-hydroxylase domain-containing protein similar to Pseudomonas aeruginosa lipopolysaccharide biosynthetic protein LpxO, a Fe2+/alpha-ketoglutarate-dependent dioxygenase homolog

Date:

2020-02-14

Members of this family are LpxO, an enzyme that modifies one of the lipid chains in lipid A by hydroxylation, with resulting changes in resistance to the host immune response and to the antibiotic colistin. This family, as built, includes LpxO1 from Pseudomonas aeruginosa, but not its paralog LpxO2.

Gene:

lpxO

Date:

2021-09-22