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PROSITE documentation PDOC51553 [for PROSITE entry PS51553]

GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain profile





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

GMPS_ATP_PPASE, PS51553; GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain profile  (MATRIX)


References

1AuthorsTesmer J.J.G. Klem T.J. Deras M.L. Davisson V.J. Smith J.L.
TitleThe crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
SourceNat. Struct. Biol. 3:74-86(1996).
PubMed ID8548458

2AuthorsGrimaldi C. Dutertre M. Simonet J.-M.
TitleGenetic organization and polymorphism of the guaA gene encoding the GMP synthetase in Lactobacillus rhamnosus.
SourceCurr. Microbiol. 40:245-249(2000).
PubMed ID10688693
DOI10.1007/s002849910049

3AuthorsMaruoka S. Horita S. Lee W.C. Nagata K. Tanokura M.
TitleCrystal 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.
SourceJ. Mol. Biol. 395:417-429(2010).
PubMed ID19900465
DOI10.1016/j.jmb.2009.10.053



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