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Literature summary for 2.7.7.59 extracted from

  • Zhang, Y.; Pohlmann, E.L.; Serate, J.; Conrad, M.C.; Roberts, G.P.
    Mutagenesis and functional characterization of the four domains of GlnD, a bifunctional nitrogen sensor protein (2010), J. Bacteriol., 192, 2711-2721.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli
expression in Escherichia coli Rhodospirillum rubrum

Protein Variants

Protein Variants Comment Organism
D107A large decrease in activity Escherichia coli
D107V large decrease in activity Escherichia coli
D107Y large decrease in activity Escherichia coli
G93L large decrease in activity Escherichia coli
G93V large decrease in activity Escherichia coli
G94L large decrease in activity Escherichia coli
G94V large decrease in activity Escherichia coli
H514A/D515A large decrease in activity Escherichia coli
H514Q/D515N large decrease in activity Escherichia coli
additional information the uridylyl-removing activity is a property specifically of the central HD domain, substitutions in this domain eliminated uridylyl-removing activity, and a truncated protein lacking the N-terminal domain display uridylyl-removing activity. The deletion of C-terminal ACT domains has little effect on uridylyl-removing activity itself but eliminates the ability of glutamine to stimulate that activity. The deletion of C-terminal ACT domains also dramatically decreases uridylyltransferase activity under all conditions tested Escherichia coli
additional information the uridylyl-removing activity is a property specifically of the central HD domain, substitutions in this domain eliminated uridylyl-removing activity, and a truncated protein lacking the N-terminal domain display uridylyl-removing activity. The deletion of C-terminal ACT domains has little effect on uridylyl-removing activity itself but eliminates the ability of glutamine to stimulate that activity. The deletion of C-terminal ACT domains also dramatically decreases uridylyltransferase activity under all conditions tested Rhodospirillum rubrum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ or Mn2+, required. Enzyme shows more than 5fold higher uridylyl-removing activity in presence of Mn2+ than with Mg2+ Escherichia coli
Mn2+ or Mn2+, required. Enzyme shows more than 5fold higher uridylyl-removing activity in presence of Mn2+ than with Mg2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
bifunctional uridylyltransferase/uridylyl-removing enzyme
-
Rhodospirillum rubrum Q2RNG2 bifunctional uridylyltransferase/uridylyl-removing enzyme
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UTP + GlnB
-
Escherichia coli diphosphate + uridylyl-GlnB
-
r
UTP + GlnB
-
Rhodospirillum rubrum diphosphate + uridylyl-GlnB
-
r