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kelch repeat protein
kelch repeat-containing protein
The kelch motif was initially discovered in Kelch (Swiss:Q04652). In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase [1] for which a structure has been solved [2]. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in Pfam:PF00064, Pfam:PF00400 and Pfam:PF00415. [1]. 8126718. Drosophila kelch motif is derived from a common enzyme fold. Bork P, Doolittle RF;. J Mol Biol 1994;236:1277-1282. [2]. 2002850. Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF;. Nature 1991;350:87-90. [3]. 15475350. Crystal structure of the Kelch domain of human Keap1. Li X, Zhang D, Hannink M, Beamer LJ;. J Biol Chem 2004;279:54750-54758. (from Pfam)
N-acetylneuraminate epimerase
N-acetylneuraminate epimerase converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers
YjhT family mutarotase
Members of this protein family contain multiple copies of the beta-propeller-forming Kelch repeat. All are full-length homologs to YjhT of Escherichia coli, which has been identified as a mutarotase for sialic acid. This protein improves bacterial ability to obtain host sialic acid, and thus serves as a virulence factor. Some bacteria carry what appears to be a cyclically permuted homolog of this protein.
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