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PUA domain-containing protein
The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was detected also in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in the regulation of the expression of other genes [1]. It is predicted that the PUA domain is an RNA binding domain. [1]. 10093218. Novel predicted RNA-binding domains associated with the translation machinery. Aravind L, Koonin EV;. J Mol Evol 1999;48:291-302. (from Pfam)
Amino acid kinase family
This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4, Swiss:P00561. Acetylglutamate kinase EC:2.7.2.8, Swiss:Q07905. Glutamate 5-kinase EC:2.7.2.11, Swiss:P07005. Uridylate kinase EC:2.7.4.-, Swiss:P29464. Carbamate kinase EC:2.7.2.2, Swiss:O96432. [1]. 10860751. The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight in. Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V;. J Mol Biol 2000;299:463-476. (from Pfam)
glutamate 5-kinase
glutamate 5-kinase catalyzes glutamate-dependent ATP cleavage, and transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (or ornithine) biosynthesis
The glutamate 5-kinase ProB has an N-terminal kinase domain and a dispensable C-terminal PUA domain. ProB catalyzes the first step in proline biosynthesis from glutamate, and typically is subject to feedback inhibition by proline.
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