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IPR011904 is a Acetate-CoA ligase.
<p>Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme) is a ubiquitous enzyme, found in both prokaryotes and eukaryotes, which catalyses the formation of acetyl-CoA from acetate, coenzyme A (CoA) and ATP as shown below [[cite:PUB00028098]]: <reaction>ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA</reaction> The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. It is especially important in eukayotic species as it is the only route for the activation of acetate to acetyl-CoA in these organisms (some prokaryotic species can also activate acetate by either acetate kinase/phosphotransacetylase or by ADP-forming acetyl-CoA synthase). Eukaryotes typically have two isoforms of acetyl-CoA synthase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.</p> <p>The crystal structures of a eukaryotic ([swissprot:Q01574], from yeast) and bacterial ([swissprot:Q8ZKF6], from Salmonella) form of this enzyme have been determined [[cite:PUB00028099], [cite:PUB00028100]]. The yeast enzyme is trimeric, while the bacterial enzyme is monomeric. The trimeric state of the yeast protein may be unique to this organism however, as the residues involved in the trimer interface are poorly conserved in other sequences. Despite differences in the oligomeric state of the two enzyme, the structures of the monomers are almost identical. A large N-terminal domain (~500 residues) containing two parallel β sheets is followed by a small (~110 residues) C-terminal domain containing a three-stranded β sheet with helices. The active site occurs at the domain interface, with its contents determining the orientation of the C-terminal domain.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Acetate-CoA ligase activity | Catalysis of the reaction: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. | ||
| Molecular function | AMP binding | Interacting selectively and non-covalently with AMP, adenosine monophosphate. | ||
| Biological process | Acetyl-CoA biosynthetic process from acetate | The chemical reactions and pathways resulting in the formation of acetyl-CoA from acetate, either directly or via acetylphosphate. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: acetyl-coenzyme A synthetase-like [Glycine max] gi|356570289|ref|XP_003553322.1| | 17 | ||
| – | Acetyl-coenzyme A synthetase; TAIR: AT5G36880.1 acetyl-CoA synthetase; Swiss-Prot: sp|B9DGD6|ACS_ARATH Acetyl-coenzyme A synthetase, chloroplastic/glyoxysomal; TrEMBL-Plants: tr|A0A151QY83|A0A151QY83_CAJCA Acetyl-coenzyme A synthetase; Found in the gene: LotjaGi1g1v0637400 | 18 | ||
| – | Acetyl-coenzyme A synthetase; TAIR: AT5G36880.2 acetyl-CoA synthetase; Swiss-Prot: sp|B9DGD6|ACS_ARATH Acetyl-coenzyme A synthetase, chloroplastic/glyoxysomal; TrEMBL-Plants: tr|I1N846|I1N846_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0637400 | 18 | ||
| – | Acetyl-coenzyme A synthetase; TAIR: AT5G36880.4 acetyl-CoA synthetase; Swiss-Prot: sp|B9DGD6|ACS_ARATH Acetyl-coenzyme A synthetase, chloroplastic/glyoxysomal; TrEMBL-Plants: tr|I1N846|I1N846_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0637400 | 15 | ||
| – | Acetyl-coenzyme A synthetase; TAIR: AT5G36880.1 acetyl-CoA synthetase; Swiss-Prot: sp|B9DGD6|ACS_ARATH Acetyl-coenzyme A synthetase, chloroplastic/glyoxysomal; TrEMBL-Plants: tr|A0A151QY83|A0A151QY83_CAJCA Acetyl-coenzyme A synthetase; Found in the gene: LotjaGi1g1v0637400 | 17 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd05966 | CDD | 1 | 20.00 |