The N-terminal of the nucleophile aminohydrolase (Ntn hydrolases) provides two catalytic groups, nucleophile and proton donor. Ntn hydrolases use the side chain of the amino-terminal residue, incorporated in a beta-sheet, as the nucleophile in the catalytic attack at the carbonyl carbon. The nucleophile is cysteine in GAT, serine in penicillin acylase, and threonine in the proteasome. All the enzymes share an unusual fold in which the nucleophile and other catalytic groups occupy equivalent sites. This fold provides both the capacity for nucleophilic attack and the possibility of autocatalytic processing. Proteins containing this domain include: Class II glutamine amidotransferases. Penicillin acylases. Penicillin V acylases. Proteasome subunits. (Glycosyl)asparaginases. Gamma-glutamyltranspeptidase-like proteins. SPO2555-like proteins.