EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.5.10 | additional information | - |
additional information | - |
Pseudomonas denitrificans (nom. rej.) |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.3.5.10 | Mg2+ | bound | Pseudomonas denitrificans (nom. rej.) |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
6.3.5.9 | 45000 | - |
2 * 45000 | Escherichia coli |
6.3.5.10 | 57000 | - |
2 * 57000 | Escherichia coli |
6.3.5.10 | 57000 | - |
2 * 57000 | Pseudomonas denitrificans (nom. rej.) |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.5.9 | ATP + hydrogenobyrinic acid + L-glutamine + H2O | Escherichia coli | vitamin B12 biosynthesis | ADP + phosphate + hydrogenobyrinic acid a,c-diamide + L-glutamate | - |
? | |
6.3.5.10 | adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O | Escherichia coli | vitamin B12 biosynthesis | adenosylcobyric acid + ADP + phosphate + L-glutamate | - |
? | |
6.3.5.10 | ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O | Pseudomonas denitrificans (nom. rej.) | involved in cobalamin biosynthesis | ADP + phosphate + adenosylcobyric acid + L-glutamate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.5.9 | Escherichia coli | - |
- |
- |
6.3.5.10 | Escherichia coli | - |
- |
- |
6.3.5.10 | Pseudomonas denitrificans (nom. rej.) | - |
- |
- |
6.3.5.11 | Pseudomonas denitrificans (nom. rej.) | P21632 | - |
- |
6.3.5.11 | Salmonella enterica subsp. enterica serovar Typhimurium | P29946 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
6.3.5.10 | 4 ATP + adenosylcobyrinic acid a,c-diamide + 4 L-glutamine + 4 H2O = 4 ADP + 4 phosphate + adenosylcobyric acid + 4 L-glutamate | catalytic mechanism | Pseudomonas denitrificans (nom. rej.) |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.5.9 | ATP + hydrogenobyrinic acid + L-glutamine + H2O | - |
Escherichia coli | ADP + phosphate + hydrogenobyrinic acid a,c-diamide + L-glutamate | - |
? | |
6.3.5.9 | ATP + hydrogenobyrinic acid + L-glutamine + H2O | vitamin B12 biosynthesis | Escherichia coli | ADP + phosphate + hydrogenobyrinic acid a,c-diamide + L-glutamate | - |
? | |
6.3.5.10 | adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O | - |
Escherichia coli | adenosylcobyric acid + ADP + phosphate + L-glutamate | - |
? | |
6.3.5.10 | adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O | vitamin B12 biosynthesis | Escherichia coli | adenosylcobyric acid + ADP + phosphate + L-glutamate | - |
? | |
6.3.5.10 | ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O | involved in cobalamin biosynthesis | Pseudomonas denitrificans (nom. rej.) | ADP + phosphate + adenosylcobyric acid + L-glutamate | - |
? | |
6.3.5.10 | ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O | CobQ contains an unusual Triad family, class I, glutamine amidotransferase domain with conserved Cys and His residues, but lacking the Glu residue of the catalytic triad, domain organization, model of substrate binding, catalytic mechanism, CobQ catalyzes amidation of the carboxyls b, d, e, and g in a strict order, one ATP molecule and one glutamine molecule are consumed for each amidation reaction | Pseudomonas denitrificans (nom. rej.) | ADP + phosphate + adenosylcobyric acid + L-glutamate | - |
? | |
6.3.5.11 | 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.) | ? | - |
? | |
6.3.5.11 | 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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.3.5.9 | dimer | 2 * 45000 | Escherichia coli |
6.3.5.10 | dimer | 2 * 57000 | Escherichia coli |
6.3.5.10 | dimer | 2 * 57000 | Pseudomonas denitrificans (nom. rej.) |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.3.5.9 | cobalamin biosynthesis aminotransferase | - |
Escherichia coli |
6.3.5.9 | CobB | - |
Escherichia coli |
6.3.5.9 | cobyrinic acid a,c-diamide synthase | - |
Escherichia coli |
6.3.5.10 | cobalamin biosynthesis aminotransferase | - |
Escherichia coli |
6.3.5.10 | CobQ | - |
Escherichia coli |
6.3.5.10 | cobyric acid synthase | - |
Escherichia coli |
6.3.5.10 | More | CobQ is a member of the dethiobiotin synthetase superfamily | Pseudomonas denitrificans (nom. rej.) |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.3.5.9 | 7.3 | - |
- |
Escherichia coli |
6.3.5.10 | 7.5 | - |
- |
Escherichia coli |
6.3.5.10 | 7.5 | - |
- |
Pseudomonas denitrificans (nom. rej.) |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.3.5.10 | ATP | ATP-dependent | Pseudomonas denitrificans (nom. rej.) |