InterPro domain: IPR016119

This superfamily represents an alpha helical domain is found in bromoperoxidases and at the C-terminal of chloroperoxidases, both being haloperoxidases [ 1 ]. The structure of chloroperoxidase from the fungus Curvularia inaequalis consists of a duplication containing two core alpha-helical bundles arranged as in other family dimers [ 2 ]. Chloroperoxidases ( 1.11.1.10 ) use a haem cofactor to bring about the chlorination of a range of organic molecules, forming stable C-Cl bonds.

The vanadium-dependent haloperoxidases exclusively catalyse the oxidation of halides. Vanadium-dependent haloperoxidase has an almost all-helical structure, with two four-helix bundles and only three small beta-sheets. The holoenzyme contains trigonal-bipyramidal coordinated vanadium atoms at its two active centres.

1. Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis. J. Mol. Biol. 299, 1035-49
2. X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis. J. Biol. Inorg. Chem. 4, 209-19