Homologous Superfamily

Galactose oxidase/kelch, beta-propeller (IPR011043)

Short name: Gal_Oxase/kelch_b-propeller

Overlapping entries


This entry represents a beta-propeller domain found in galactose oxidase and in Kelch repeat-containing proteins.

The known functions of kelch-containing proteins are diverse: scruin is an actin cross-linking protein; galactose oxidase catalyses the oxidation of the hydroxyl group at the C6 position in D-galactose; neuraminidase hydrolyses sialic acid residues from glycoproteins; and kelch may have a cytoskeletal function, as it is localised to the actin-rich ring canals that connect the 15 nurse cells to the developing oocyte in Drosophila [PMID: 7593276]. Nevertheless, based on the location of the kelch pattern in the catalytic unit in galactose oxidase, functionally important residues have been predicted in glyoxal oxidase [PMID: 8126718].

Galactose oxidase (EC: is a monomeric enzyme that contains a single copper ion and catalyses the stereospecific oxidation of primary alcohols to their corresponding aldehyde [PMID: 11698678]. The protein contains an unusual covalent thioether bond between a tyrosine and a cysteine that forms during its maturation [PMID: 12418174]. Galactose oxidase is a three-domain protein: the N-terminal domain forms a jelly-roll sandwich, the central domain forms a seven 4-bladed beta-propeller, and the C-terminal domain has an immunoglobulin-like fold.

Contributing signatures

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