LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | This entry represents NAD(+) synthetases, including glutamine-dependent NAD(+) synthetases and NH(3)-dependent NAD(+) synthetases.NAD+ is involved electron transport and redox reactions and in DNA ligation and protein ADP-ribosylation. In yeast and most other organisms, NAD is generated through the de novo pathway and the salvage pathway. In the de novo pathway, quinolinic acid is converted to nicotinic acid mononucleotide (NaMN). In the salvage pathway, NaMN is generated by recycling of nicotinamide. Both pathways converge on NaMN, which is then converted into deamido-NAD+. Subsequently, deamido-NAD+ is converted to NAD+ by NAD+ synthetase [ ].NAD+ synthetase has been extensively studied in bacteria. It is encoded by nadE gene in E. coli and by outB gene in B. subtilis [ ]. These prokaryotic enzymes are ammonia-dependent (containing an ammonia-utilising domain)[]. However, some pokaryotic NAD(+) synthetases, such as that from Mycobacterium tuberculosis, contain a nitrilase-related domain, are glutamine-dependent []. Eukaryotic NAD+ synthetases are glutamine-dependent. In budding yeast, this enzyme is named as Qns1. It contains an N-terminal nitrilase-related domain (contaiing the nitrilase-related active-site residues) and a C-terminal NAD+ synthetase domain [ ]. Both domains are required for its function in vivo. The nitrilase-related domain is the fourth independently evolved glutamine amidotransferase domain to have been identified in nature []. |
| Short Name | NAD_synthase |
