|Quickview||Gene||Gene Product(s)||Expression||Evolution||On One Page|
ECK0165, b0167, JW0162, glnD5
Bifunctional uridylyltransferase/uridylyl-removing enzyme; (UTase/UR); controls uridylylation state and activity of PII(GlnB)
|Function from GO|
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GlnD has both a uridylyltransferase and a uridylyl-removing activity. The only known substrates for GlnD are the two PII proteins GlnB and GlnK. In both cases GlnD covalently modifies residue Tyr51 in the T-loop of the substrate thereby controlling the ability of GlnB and GlnK to interact with their specific targets. The activity of GlnD is controlled by the intracellular glutamine availability. Glutamine inhibits the transferase action of GlnD and as a consequence GlnB and GlnK are deuridylylated in N-sufficient conditions. [Comment provided by EcoTeam member Mike Merrick, 11.16.06]
- Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.