SMART: Pfam domain ATP-grasp

The domain within your query sequence starts at position 40 and ends at position 248; the E-value for the ATP-grasp_2 domain shown below is 2.4e-79.

AGGRGKGVFNSGLKGGVHLTKDPKVVGELAQQMIGYNLATKQTPKEGVKVNKVMVAEALD
ISRETYLAILMDRSHNGPVIVGSPQGGVDIEEVAASSPELIFKEQIDIFEGIKDSQAQRM
AENLGFLGSLKNQAADQITKLYHLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAE
FRQKDIFAMDDKSENEPIENEAARYDLKY

ATP-grasp_2

PFAM accession number:	PF08442
Interpro abstract (IPR013650):	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 [ (PUBMED:9416615) ]. 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 [ (PUBMED:7939684) ]. The ATP-grasp domain contains three conserved motifs, corresponding to the phosphate binding loop and the Mg(2+) binding site [ (PUBMED:8804825) ]. The fold is characterised by two alpha-beta subdomains that grasp the ATP molecule between them. 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 [ (PUBMED:7862655) ]. The ATP-grasp domain represented by this entry is found primarily in succinyl-CoA synthetases ( EC 6.2.1.5 ).

PFAM accession number:

PF08442

Interpro abstract (IPR013650):

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 [ (PUBMED:9416615) ]. 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 [ (PUBMED:7939684) ].

The ATP-grasp domain contains three conserved motifs, corresponding to the phosphate binding loop and the Mg(2+) binding site [ (PUBMED:8804825) ]. The fold is characterised by two alpha-beta subdomains that grasp the ATP molecule between them. 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 [ (PUBMED:7862655) ].

The ATP-grasp domain represented by this entry is found primarily in succinyl-CoA synthetases ( EC 6.2.1.5 ).

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ATP-grasp_2