{PDOC50975}
{PS50975; ATP_GRASP}
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* ATP-grasp domain profile *
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The  ATP-grasp superfamily currently includes 17 groups of enzymes, catalyzing
ATP-dependent  ligation  of  a  carboxylate containing molecule to an amino or
thiol   group-containing   molecule  [1].  They  contribute  predominantly  to
macromolecular  synthesis. ATP-hydrolysis is used to activate a substrate. For
example, DD-ligase transfers phosphate from ATP to D-alanine on the first step
of  catalysis. On the second step the resulting acylphosphate is attacked by a
second  D-alanine  to  produce  a DD dipeptide following phosphate elimination
[2].

The  ATP-grasp  domain  contains  three conserved motifs, corresponding to the
phosphate  binding  loop  and  the  Mg(2+)  binding  site  [3].  The  fold  is
characterized by two alpha-beta subdomains that grasp the ATP molecule between
them  (see  <PDB:1IOW>).  Each subdomain provides a variable loop that forms a
part  of  the  active site, completed by region of other domains not conserved
between the various ATP-grasp enzymes[4].

Proteins known to contain an ATP-grasp domain are listed below:

 - Biotin carboxylase (EC 6.3.4.14).
 - Carbamoyl-phosphate synthase (EC 6.3.5.5).
 - Cyanophycin synthetase (EC 6.-.-.-).
 - D-alanine--D-alanine ligase (EC 6.3.2.4).
 - Urea amidolyase (Urea carboxylase) (EC 6.3.4.6).
 - Glutathione synthetase  (EC 6.3.2.3).
 - Lysine biosynthesis protein.
 - Methylcrotonyl-CoA carboxylase (EC 6.4.1.4).
 - MurC/ddl bifunctional enzyme (EC 6.3.2.8).
 - Propionyl-CoA carboxylase (EC 6.4.1.3).
 - Phosphoribosylamine--glycine ligase (EC 6.3.4.13).
 - Phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21).
 - Pyruvate carboxylase 1 (EC 6.4.1.1).
 - CAD protein, includes carbamoyl-phosphate synthase activity.
 - Ribosomal protein S6 modification protein.
 - Succinyl-CoA synthetase (EC 6.2.1.5).
 - Vancomycin/teicoplanin resistance protein (EC 6.3.2.-).
 - 5-(carboxyamino)imidazole ribonucleotide synthase (EC 6.3.4.18).
 - Inositol-tetrakisphosphate 1-kinase (EC 2.7.1.134).
 - Inositol-1,3,4-trisphosphate 5/6-kinase (EC 2.7.1.159).

The profile we developed covers the entire ATP-grasp domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2004 / First entry.

[ 1] Galperin M.Y., Koonin E.V.
     "A diverse superfamily of enzymes with ATP-dependent
     carboxylate-amine/thiol ligase activity."
     Protein Sci. 6:2639-2643(1997).
     PubMed=9416615
[ 2] Fan C., Moews P.C., Walsh C.T., Knox J.R.
     "Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3
     A resolution."
     Science 266:439-443(1994).
     PubMed=7939684
[ 3] Murzin A.G.
     "Structural classification of proteins: new superfamilies."
     Curr. Opin. Struct. Biol. 6:386-394(1996).
     PubMed=8804825
[ 4] Fan C., Moews P.C., Shi Y., Walsh C.T., Knox J.R.
     "A common fold for peptide synthetases cleaving ATP to ADP:
     glutathione synthetase and D-alanine:d-alanine ligase of Escherichia
     coli."
     Proc. Natl. Acad. Sci. U.S.A. 92:1172-1176(1995).
     PubMed=7862655

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