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maleylpyruvate isomerase N-terminal domain-containing protein
maleylpyruvate isomerase family mycothiol-dependent enzyme
maleylpyruvate isomerase family protein may be a mycothiol-dependent enzyme similar to the N-terminal domain of Corynebacterium glutamicum mycothiol-dependent maleylpyruvate isomerase (MDMPI), which catalyzes the conversion of maleylpyruvate to fumarylpyruvate
This protein family pulls together several groups of proteins, each very different from the others. They share in common three conserved regions. The first is a region of about 38 amino acids, nearly always at the N-terminus of a protein. This region has a bulky hydrophobic residue, usually Trp, at position 29, and a His residue at position 37 that is invariant, so far, in over 150 instances. The second conserved region has a motif [DE]xxxHxxD. The third conserved region contains a hydrophobic patch and a well-conserved Arg residue. Most examples are found in the Actinobacteria, including the genera Mycobacterium, Corynebacterium, Streptomyces, Nocardia, Frankia, etc. The pattern of near-invariant residues against a backdrop of extreme sequence divergence suggests enzymatic activity and conservation of active site residues.
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