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Human activating signal cointegrator homology (ASCH) domain-containing proteins are widespread and diverse but, at present, the vast majority of those proteins have no function assigned to them. This study demonstrates that the 103-amino acid  Escherichia coli  protein YqfB, previously identified as hypothetical, is a unique ASCH domain-containing amidohydrolase responsible for the catabolism of  N  4 -acetylcytidine (ac4C). YqfB has several interesting and unique features: i) it is the smallest monomeric amidohydrolase described to date, ii) it is active towards structurally different  N  4 -acylated cytosines/cytidines, and iii) it has a high specificity for these substrates (k cat /K m  up to 2.8 × 10 6  M −1  s −1 ). Moreover, our results suggest that YqfB contains a unique Thr-Lys-Glu catalytic triad, and Arg acting as an oxyanion hole. The mutant lacking the  yqfB  gene retains the ability to grow, albeit poorly, on  N  4 -acetylcytosine as a source of uracil, suggesting that an alternative route for the utilization of this compound exists in  E. coli . Overall, YqfB ability to hydrolyse various  N  4 -acylated cytosines and cytidines not only sheds light on the long-standing mystery of how ac4C is catabolized in bacteria, but also expands our knowledge of the structural diversity within the active sites of amidohydrolases.

YqfB protein from Escherichia coli: an atypical amidohydrolase active towards N4-acylcytosine derivatives