Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Escherichia coli |
expression in Escherichia coli | Rhodospirillum rubrum |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
bifunctional uridylyltransferase/uridylyl-removing enzyme | - |
Rhodospirillum rubrum | Q2RNG2 | bifunctional uridylyltransferase/uridylyl-removing enzyme | - |
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 |