{PDOC51553}
{PS51553; GMPS_ATP_PPASE}
{BEGIN}
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* GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain profile *
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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 beta-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 beta-strand [1,3].

The profile we developed covers the entire GMPS ATP-PPase domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: November 2011 / First entry.

[ 1] Tesmer J.J.G., Klem T.J., Deras M.L., Davisson V.J., Smith J.L.
     "The crystal structure of GMP synthetase reveals a novel catalytic
     triad and is a structural paradigm for two enzyme families."
     Nat. Struct. Biol. 3:74-86(1996).
     PubMed=8548458
[ 2] Grimaldi C., Dutertre M., Simonet J.-M.
     "Genetic organization and polymorphism of the guaA gene encoding the
     GMP synthetase in Lactobacillus rhamnosus."
     Curr. Microbiol. 40:245-249(2000).
     PubMed=10688693; DOI=10.1007/s002849910049
[ 3] Maruoka S., Horita S., Lee W.C., Nagata K., Tanokura M.
     "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."
     J. Mol. Biol. 395:417-429(2010).
     PubMed=19900465; DOI=10.1016/j.jmb.2009.10.053

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