EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   6.3.5.10 | ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O |
cobalamin biosynthetic pathway, involved in coenzyme B12 synthesis |
Pseudomonas denitrificans (nom. rej.) |
ADP + phosphate + adenosylcobyric acid + L-glutamate |
- |
? |
| 6.3.5.10 | ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O |
cobinamide biosynthesis |
Halobacterium sp. |
ADP + phosphate + adenosylcobyric acid + L-glutamate |
- |
? |
| 6.3.5.10 | ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O |
CobQ is involved in the biosynthesis of adenosylcobalamin, i.e. vitamin B12, aerobic pathway |
Pseudomonas denitrificans (nom. rej.) |
ADP + phosphate + adenosylcobyric acid + 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 |
involved in the de novo cobinamide biosynthesis pathway |
Salmonella enterica |
ADP + phosphate + adenosylcobyric acid + L-glutamate |
- |
? |
| 6.3.5.10 | ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O |
CbiP catalyzes b, d, e, and g amidation |
Salmonella enterica |
ADP + phosphate + adenosylcobyric acid + L-glutamate |
- |
? |
| 6.3.5.10 | ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O |
CobQ amidates the side chains b, d, e, and g generating adenosylcobyric acid, requires glutamine as the amide donor |
Pseudomonas denitrificans (nom. rej.) |
ADP + phosphate + adenosylcobyric acid + L-glutamate |
- |
? |
| 6.3.5.10 | ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O |
CobQ catalyzes amidations at positions b, d, e and g |
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 |
- |
? |
| 6.3.5.10 | ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O |
enzyme catalyzes the stepwise amidation of carboxyl groups b, d, e, and g of cobyrinic acid a,c-diamide, four-step amidation sequence from cobyrinic acid a,c-diamide to cobyric acid via the formation of corbyrinic acid triamide, tetraamide, and pentaamide intermediates, the amidations are carried out in a specific order, enzyme is specific to coenzyme forms of substrates, no amidation of the carboxyl group at position f, L-glutamine is the preferred amide group donor |
Pseudomonas denitrificans (nom. rej.) |
ADP + phosphate + adenosylcobyric acid + L-glutamate |
- |
? |
