| Description | This domain can be found at the N terminus of pyrimidine/purine nucleotide 5'-monophosphate nucleosidase (PpnN, also known as YgdH) from bacteria. PpnN catalyses the hydrolysis of the N-glycosidic bond of diverse pyrimidine and purine nucleotide 5'-monophosphates, to form ribose 5-phosphate and the corresponding free base. It can use AMP, GMP, IMP, CMP, dTMP and UMP as substrates. This enzyme adopts a tetrameric configuration with allosteric (p)ppGpp binding sites located between subunits. The binding of this alarmone molecule, which play a role in the bacterial stringent response, gives rise to a large conformational change involving the terminal region that leads to the exposure of the catalytic pocket. The N-terminal domain consists of a three-stranded anti-parallel β-sheet surrounded by α-helices [, ]. | Name | Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase, N-terminal |
| Short Name | PpnN_N | Type | Domain |
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