Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR010159 is a N-acyl-L-amino-acid amidohydrolase.
<p>This entry represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolase ([ec:3.5.1.14]) is a homodimeric zinc-binding mammalian enzyme that catalyzes the hydrolysis of N-alpha-acylated amino acids except L-aspartic acid [[cite:PUB00002356], [cite:PUB00028006]]. These enzymes are listed as non-peptidase homologues in MEROPS peptidase family M20A (clan MH). Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase [[cite:PUB00003579], [cite:PUB00030157]].</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 | Aminoacylase activity | Catalysis of the reaction: an N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid. | ||
| Cellular component | Cytoplasm | All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. | ||
| Biological process | Cellular amino acid metabolic process | The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: aminoacylase-1-like [Glycine max] gi|356550846|ref|XP_003543794.1| | 18 | ||
| – | Aminoacylase; TAIR: AT1G44820.1 Peptidase M20/M25/M40 family protein; Swiss-Prot: sp|Q99JW2|ACY1_MOUSE Aminoacylase-1; TrEMBL-Plants: tr|I1LW56|I1LW56_SOYBN Aminoacylase; Found in the gene: LotjaGi1g1v0155900 | 26 | ||
| – | Succinyl-diaminopimelate desuccinylase; TAIR: AT4G38220.1 Peptidase M20/M25/M40 family protein; Swiss-Prot: sp|Q99JW2|ACY1_MOUSE Aminoacylase-1; TrEMBL-Plants: tr|A0A0S3T0P1|A0A0S3T0P1_PHAAN Aminoacylase; Found in the gene: LotjaGi2g1v0024600 | 23 | ||
| – | Aminoacylase; TAIR: AT4G38220.1 Peptidase M20/M25/M40 family protein; Swiss-Prot: sp|Q55DP8|ACY1_DICDI Aminoacylase-1; TrEMBL-Plants: tr|A0A0S3T0P1|A0A0S3T0P1_PHAAN Aminoacylase; Found in the gene: LotjaGi3g1v0316900_LC | 16 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd05646 | CDD | 1 | 25.00 |