|PROSITE documentation PDOC50975
ATP-grasp domain profile
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 . 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
The ATP-grasp domain contains three conserved motifs, corresponding to the
phosphate binding loop and the Mg(2+) binding site . The fold is
characterized by two α-β 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.
Proteins known to contain an ATP-grasp domain are listed below:
- Biotin carboxylase (EC 184.108.40.206).
- Carbamoyl-phosphate synthase (EC 220.127.116.11).
- Cyanophycin synthetase (EC 6.-.-.-).
- D-alanine--D-alanine ligase (EC 18.104.22.168).
- Urea amidolyase (Urea carboxylase) (EC 22.214.171.124).
- Glutathione synthetase (EC 126.96.36.199).
- Lysine biosynthesis protein.
- Methylcrotonyl-CoA carboxylase (EC 188.8.131.52).
- MurC/ddl bifunctional enzyme (EC 184.108.40.206).
- Propionyl-CoA carboxylase (EC 220.127.116.11).
- Phosphoribosylamine--glycine ligase (EC 18.104.22.168).
- Phosphoribosylaminoimidazole carboxylase (EC 22.214.171.124).
- Pyruvate carboxylase 1 (EC 126.96.36.199).
- CAD protein, includes carbamoyl-phosphate synthase activity.
- Ribosomal protein S6 modification protein.
- Succinyl-CoA synthetase (EC 188.8.131.52).
- Vancomycin/teicoplanin resistance protein (EC 6.3.2.-).
- 5-(carboxyamino)imidazole ribonucleotide synthase (EC 184.108.40.206).
- Inositol-tetrakisphosphate 1-kinase (EC 220.127.116.11).
- Inositol-1,3,4-trisphosphate 5/6-kinase (EC 18.104.22.168).
The profile we developed covers the entire ATP-grasp domain.
April 2004 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|ATP_GRASP, PS50975; ATP-grasp fold profile (MATRIX)
|Sequences known to belong to this class detected by the profile:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1A9X 1B6R 1B6S 1BNC ... [ALL]
||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).
||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.
||Structural classification of proteins: new superfamilies.
||Curr. Opin. Struct. Biol. 6:386-394(1996).
||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).
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