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pyrimidine/purine nucleosidase domain-containing protein
This is an N-terminal domain found in pyrimidine/purine nucleotide 5'-monophosphate nucleosidases (PpnN) in bacteria. PpnN catalyzes 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 [1]. It is found in association with Pfam:PF03641 and Pfam:PF11892. [1]. 27941785. Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli. Sevin DC, Fuhrer T, Zamboni N, Sauer U;. Nat Methods. 2017;14:187-194. (from Pfam)
pyrimidine/purine nucleotide monophosphate nucleosidase domain-containing protein
This domain is found at the C-terminal end of Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase from Escherichia coli (PpnN, also known as YgdH) and similar proteins mainly found in gammaproteobacteria. PpnN is a nucleosidase that catalyses the hydrolysis of the N-glycosidic bond of diverse pyrimidine and purine nucleotide 5'-monophosphates. The binding of (p)ppGpp, an alarmone molecule that plays a role in the bacterial stringent response, gives rise to a large conformational change in the terminal region that leads to the exposure of the catalytic pocket. This domain shows a completely alpha-helical fold with an extension that wraps around the central domain [1, 2]. [1]. 31023582. (p)ppGpp Regulates a Bacterial Nucleosidase by an Allosteric Two-Domain Switch. Zhang YE, Baerentsen RL, Fuhrer T, Sauer U, Gerdes K, Brodersen DE;. Mol Cell. 2019;74:1239-1249. [2]. 27941785. Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli. Sevin DC, Fuhrer T, Zamboni N, Sauer U;. Nat Methods. 2017;14:187-194. (from Pfam)
LOG family protein
The members of this family share a highly conserved motif PGGXGTXXE that is probably functionally important. This family includes proteins annotated as lysine decarboxylases, although the evidence for this is not clear. (from Pfam)
nucleotide 5'-monophosphate nucleosidase PpnN
nucleotide 5'-monophosphate nucleosidase PpnN catalyzes 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
PpnN (pyrimidine/purine nucleotide 5'-monophosphate nucleosidase), widely conserved in gamma proteobacteria, plays a role in purine homeostasis. It can bind the the stringent response alarmones ppGpp and pppGpp and then, because of allosteric changes, have a much higher rate of cleavage of preferred substrate GMP. PpnN was previously known in E. coli as YgdH.
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