AC   PRU00886;
DC   Domain;
TR   PROSITE; PS51553; GMPS_ATP_PPASE; 1; level=0
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Names: GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain
Function: The GMP synthetase ATP-PPase ATP-binding domain is a twisted, five-
 stranded parallel beta-sheet sandwiched between helical layers. It contains a
 glycine rich ATP-binding motif called the "P-loop motif" located after the
 first beta-strand
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GO   GO:0005524; F:ATP binding
GO   GO:0006177; P:GMP biosynthetic process
GO   GO:0000166; F:nucleotide binding
GO   GO:0006164; P:purine nucleotide biosynthetic process
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KW   ATP-binding
KW   GMP biosynthesis
KW   Nucleotide-binding
KW   Purine biosynthesis
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FT   From: PS51553
FT   DOMAIN          from..to
FT                   /note="GMPS ATP-PPase #"
FT   BINDING         28..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="#"
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Chop: Nter=0; Cter=0;
Size: 172-208;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8TYD7;
Scope:
 Bacteria
 Archaea
 Eukaryota
Comments: None;
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# Revision 1.6 2022/11/19
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