Literature summary for 2.7.7.59 extracted from

Yurgel, S.N.; Rice, J.; Kahn, M.L.
Nitrogen metabolism in Sinorhizobium meliloti-alfalfa symbiosis: dissecting the role of GlnD and PII proteins (2012), Mol. Plant Microbe Interact., 25, 355-362.

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Organism

Organism	UniProt	Comment	Textmining
Sinorhizobium meliloti	P56884	-	-

General Information

General Information	Comment	Organism
physiological function	the uridylyltransferase/uridylyl-cleavage enzyme GlnD has a role in free-living growth and in symbiotic nitrogen exchange that does not depend on its substrates, the PII proteins. An in-frame deletion mutationglnDsm2 mutation has severe defects in regulating free-living and symbiotic nitrogen metabolismcompared to the glnBglnK double-deletion strain lacking the substrates of GlnD. Data indicate that the GlnD uridylyltransferase is required for proper regulation of nitrogen exchange in symbiosis with the host plant but that the PII substrate proteins are not involved in this regulation or that the glnD-sm2 mutation disrupts some additional activity of GlnD	Sinorhizobium meliloti

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Release 2023.1 (January 2023)