PROSITE documentation PDOC51553GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain profile
Guanosine 5'-monophosphate synthetase (GMPS) is a widespread enzyme seen in all domains of life. GMPS is required for the final step of the de novo synthesis of guanine nucleotides, converting xanthosine 5'-monophosphate (XMP) into guanosine 5'-monophosphate (GMP), a precursor of DNA and RNA. GMPS consists of two catalytic units, glutamine amidotransferase (GATase) (see <PDOC00405>) and ATP pyrophosphatase (ATP-PPase). GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATP-PPase utilizes ammonia to convert adenyl xanthosine 5'-monophosphate (adenyl-XMP) into GMP. The two catalytic units are either encoded by a single gene (two-domain type) in eucaryotes, bacteria, and some archaea, or encoded by two separate genes (two-subunit type) in other archaea. In two-domain-type GMPS, the GATase domain is located in the N-terminal half, and the ATP-PPase domain is located in the C-terminal half; in two-subunit-type GMPS, these two units exist as separate polypeptides. ATP-PPase consists of two domains (N-domain and C-domain). The N-domain contains an ATP-binding platform called P-loop (see <PDOC00017>), whereas the C-domain contains the XMP-binding site and also contributes to homodimerization [1,2,3].
The GMP synthetase ATP-PPase ATP-binding domain is a twisted, five-stranded parallel β-sheet sandwiched between helical layers (see <PDB:1GPM>). It contains a glycine rich ATP-binding motif called the "P-loop motif" located after the first β-strand [1,3].
The profile we developed covers the entire GMPS ATP-PPase domain.
Last update:November 2011 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Tesmer J.J.G. Klem T.J. Deras M.L. Davisson V.J. Smith J.L. |
| Title | The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. | |
| Source | Nat. Struct. Biol. 3:74-86(1996). | |
| PubMed ID | 8548458 |
| 2 | Authors | Grimaldi C. Dutertre M. Simonet J.-M. |
| Title | Genetic organization and polymorphism of the guaA gene encoding the GMP synthetase in Lactobacillus rhamnosus. | |
| Source | Curr. Microbiol. 40:245-249(2000). | |
| PubMed ID | 10688693 | |
| DOI | 10.1007/s002849910049 |
| 3 | Authors | Maruoka S. Horita S. Lee W.C. Nagata K. Tanokura M. |
| Title | 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. | |
| Source | J. Mol. Biol. 395:417-429(2010). | |
| PubMed ID | 19900465 | |
| DOI | 10.1016/j.jmb.2009.10.053 |
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