Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas denitrificans (nom. rej.) | P21632 | - |
- |
Salmonella enterica subsp. enterica serovar Typhimurium | P29946 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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additional information | enzyme catalyzes ATP-dependent formation of the amide group using the ammonia nitrogen produced by the glutaminase domains. The reaction proceeds through a phosphoacyl intermediate, which is then subjected to the nucleophilic attack of the amino nitrogen, which leads to the formation of the amide bond and liberation of phosphate. Enzyme belongs to a family of ATP-dependent enzymes that also includes dethiobiotin synthetase and cobyric acid synthase CobQ. This enzyme family is also related to the MinD family of ATPases involved in regulation of cell division in bacteria and archaea. CobB and CobQ also contain unusual Triad family class I glutamine amidotransferase domains with conserved Cys and His residues, but lacking the Glu residue of the catalytic triad | Pseudomonas denitrificans (nom. rej.) | ? | - |
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additional information | enzyme catalyzes ATP-dependent formation of the amide group using the ammonia nitrogen produced by the glutaminase domains. The reaction proceeds through a phosphoacyl intermediate, which is then subjected to the nucleophilic attack of the amino nitrogen, which leads to the formation of the amide bond and liberation of phosphate. Enzyme belongs to a family of ATP-dependent enzymes that also includes dethiobiotin synthetase and cobyric acid synthase CobQ. This enzyme family is also related to the MinD family of ATPases involved in regulation of cell division in bacteria and archaea. CobB and CobQ also contain unusual Triad family class I glutamine amidotransferase domains with conserved Cys and His residues, but lacking the Glu residue of the catalytic triad | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
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