InterPro : IPR022310

Name  NAD/GMP synthase Short Name  NAD/GMP_synthase
Type  Domain Description  NAD+ synthase () catalyzes the last step in the biosynthesis of nicotinamide adenine dinucleotide and is induced by stress factors such as heat shock and glucose limitation. The three-dimensional structure of NH3-dependent NAD+ synthetase from Bacillus subtilis, in its free form and in complex with ATP shows that the enzyme consists of a tight homodimer with alpha/beta subunit topology [].This domain is also found in guanosine 5'-monophosphate (GMP) synthetase. GMP synthase catalyses the synthesis of GMP from XMP. The protein is a homodimer, but in some archaea it is a heterodimer composed of a glutamine amidotransferase subunit and a ATP pyrophosphatase subunit. In eucaryotes, bacteria, and some archaea the two catalytic units are encoded by a single gene, producing a two-domain-type GMP, with a GATase domain in the N-terminal half and a ATP-PPase domain in the C-terminal half. This entry represents the ATP pyrophosphatase domain.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



1 Child Features

Id Name Short Name Type
IPR025777 GMP synthetase ATP pyrophosphatase domain GMPS_ATP_PPase_dom Domain

0 Contains

3 Found In

Id Name Short Name Type
IPR001674 GMP synthase, C-terminal GMP_synth_C Domain
IPR014445 Glutamine-dependent NAD(+) synthetase Gln-dep_NAD_synthase Family
IPR005232 Conserved hypothetical protein CHP00268 CHP00268 Family

1 Parent Features

Id Name Short Name Type
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold Rossmann-like_a/b/a_fold Domain

1 Publications

First Author Title Year Journal Volume Pages
Rizzi M Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis. 1996 EMBO J 15 5125-34

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)