InterPro : IPR025777

Name  GMP synthetase ATP pyrophosphatase domain Short Name  GMPS_ATP_PPase_dom
Type  Domain Description  Guanosine 5'-monophosphate synthetase (GMPS) is a widespread enzyme seen inall domains of life. GMPS is required for the final step of the de novosynthesis of guanine nucleotides, converting xanthosine 5'-monophosphate (XMP)into guanosine 5'-monophosphate (GMP), a precursor of DNA and RNA. GMPSconsists of two catalytic units, glutamine amidotransferase (GATase) and ATP pyrophosphatase (ATP-PPase). GATase hydrolyzes glutamineto yield glutamate and ammonia, while ATP-PPase utilises ammonia to convertadenyl xanthosine 5'-monophosphate (adenyl-XMP) into GMP. The two catalyticunits are either encoded by a single gene (two-domain type) in eucaryotes,bacteria, and some archaea, or encoded by two separate genes (two-subunittype) in other archaea. In two-domain-type GMPS, the GATase domain is locatedin the N-terminal half, and the ATP-PPase domain is located in the C-terminalhalf; in two-subunit-type GMPS, these two units exist as separatepolypeptides. ATP-PPase consists of two domains (N-domain and C-domain). TheN-domain contains an ATP-binding platform called P-loop,whereas the C-domain contains the XMP-binding site and also contributes tohomodimerisation [, , ].The GMP synthetase ATP-PPase ATP-binding domain is a twisted, five-strandedparallel beta-sheet sandwiched between helical layers. Itcontains a glycine rich ATP-binding motif called the "P-loop motif" locatedafter the first beta-strand [, ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

1 Parent Features

Id Name Short Name Type
IPR022310 NAD/GMP synthase NAD/GMP_synthase Domain

3 Publications

First Author Title Year Journal Volume Pages
Tesmer JJ The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. 1996 Nat Struct Biol 3 74-86
Maruoka S Crystal structure of the ATPPase subunit and its substrate-dependent association with the GATase subunit: a novel regulatory mechanism for a two-subunit-type GMP synthetase from Pyrococcus horikoshii OT3. 2010 J Mol Biol 395 417-29
Grimaldi C Genetic organization and polymorphism of the guaA gene encoding the GMP synthetase in Lactobacillus rhamnosus. 2000 Curr Microbiol 40 245-9

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)