Literature summary for 2.7.7.59 extracted from

Bonatto, A.C.; Souza, E.M.; Oliveira, M.A.; Monteiro, R.A.; Chubatsu, L.S.; Huergo, L.F.; Pedrosa, F.O.
Uridylylation of Herbaspirillum seropedicae GlnB and GlnK proteins is differentially affected by ATP, ADP and 2-oxoglutarate in vitro (2012), Arch. Microbiol., 194, 643-652.

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Activating Compound

Activating Compound	Comment	Organism	Structure
2-oxoglutarate	maximum uridylylation rates for both PII proteins GlnB and GlnK are observed in the presence of about 2 mM 2-oxoglutarate and 200500 microM ATP. Uridylylation of both GlnB and GlnK responds to 2-oxoglutarate levels, but only GlnB responds effectively to variation on ADP/ATP ratio	Herbaspirillum seropedicae
ADP	or ATP, absolutely required for in vitro uridylylation of PII proteins GlnB and GlnK. Maximum uridylylation rates for both proteins are observed in the presence of about 2 mM 2-oxoglutarate and 200-500 microM ATP. Uridylylation of both GlnB and GlnK responds to 2-oxoglutarate levels, but only GlnB responds effectively to variation on ADP/ATP ratio	Herbaspirillum seropedicae
AMP	may partially replace ATP or ADP	Herbaspirillum seropedicae
ATP	or ADP, absolutely required for in vitro uridylylation of PII proteins GlnB and GlnK. Maximum uridylylation rates for both proteins are observed in the presence of about 2 mM 2-oxoglutarate and 200-500 microM ATP. Uridylylation of both GlnB and GlnK responds to 2-oxoglutarate levels, but only GlnB responds effectively to variation on ADP/ATP ratio	Herbaspirillum seropedicae

Organism

Organism	UniProt	Comment	Textmining
Herbaspirillum seropedicae	D8IU13	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UTP + GlnB	-	Herbaspirillum seropedicae	diphosphate + uridylyl-GlnB	-	?
UTP + GlnK	-	Herbaspirillum seropedicae	diphosphate + uridylyl-GlnK	-	?

Synonyms

Synonyms	Comment	Organism
GlnD	-	Herbaspirillum seropedicae

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Release 2023.1 (January 2023)