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IPR004412

Description

IPR004412 is a Glutamyl-tRNA(Gln) amidotransferase A subunit.

<p>In many species, Gln-tRNA ligase is missing. tRNA(Gln) is misacylated with Glu after which a heterotrimeric amidotransferase converts Glu to Gln. This group represents the amidase chain of the heterotrimer, encoded by the gatA gene called glutamyl-tRNA(Gln) amidotransferase, A subunit [ec:6.3.5]. This enzyme functions as an alternative to a direct Gln-tRNA synthetase (Gln-tRNA ligase) in mitochondria, chloroplasts, Gram-positive bacteria, cyanobacteria, and the Archaea.</p> <p>The archaea have an Asp-tRNA(Asn) amidotransferase instead of an Asp-tRNA ligase. In the archaea, a paralog of gatB is found, here designated gatB_rel, that is a candidate B subunit of the Asp-tRNA(Asn) amidotransferase. The gatA-encoded subunit may be shared by gatB and gatB_rel.</p> <p>Amidase signature (AS) enzymes are a large group of hydrolytic enzymes that contain a conserved stretch of approximately 130 amino acids known as the AS sequence. They are widespread, being found in both prokaryotes and eukaryotes. AS enzymes catalyse the hydrolysis of amide bonds (CO-NH2), although the family has diverged widely with regard to substrate specificity and function. Nonetheless, these enzymes maintain a core α/β/α structure, where the topologies of the N-and C-terminal halves are similar. AS enzymes characteristically have a highly conserved C-terminal region rich in serine and glycine residues, but devoid of aspartic acid and histidine residues, therefore they differ from classical serine hydrolases. These enzymes posses a unique, highly conserved Ser-Ser-Lys catalytic triad used for amide hydrolysis, although the catalytic mechanism for acyl-enzyme intermediate formation can differ between enzymes [[cite:PUB00035563]].</p> <p>Examples of AS enzymes include:</p> <ul> <li>Peptide amidase (Pam) [[cite:PUB00035563]], which catalyses the hydrolysis of the C-terminal amide bond of peptides.</li> <li>Fatty acid amide hydrolases [[cite:PUB00035564]], which hydrolyse fatty acid amid substrates (e.g. cannabinoid anandamide and sleep-inducing oleamide), thereby controlling the level and duration of signalling induced by this diverse class of lipid transmitters.</li> <li>Malonamidase E2 [[cite:PUB00035565]], which catalyses the hydrolysis of malonamate into malonate and ammonia, and which is involved in the transport of fixed nitrogen from bacteroids to plant cells in symbiotic nitrogen metabolism.</li> <li>Subunit A of Glu-tRNA(Gln) amidotransferase [[cite:PUB00035566]],a heterotrimeric enzyme that catalyses the formation of Gln-tRNA(Gln) by the transamidation of misacylated Glu-tRNA(Gln) via amidolysis of glutamine.</li> </ul>

This description is obtained from EB-eye REST.

Associated GO terms

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
Biological process Translation The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
Cellular component Glutamyl-tRNA(Gln) amidotransferase complex A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms.
Molecular function Glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP.

Associated Lotus transcripts 2

Transcript Name Description Predicted domains Domain count
PREDICTED: glutamyl-tRNA(Gln) amidotransferase subunit A, chloroplastic/mitochondrial-like isoform X1 [Cicer arietinum] gi|502128559|ref|XP_004500003.1| 12
Glutamyl-tRNA(Gln) amidotransferase subunit A; TAIR: AT3G25660.1 Amidase family protein; Swiss-Prot: sp|Q9LI77|GATA_ARATH Glutamyl-tRNA(Gln) amidotransferase subunit A, chloroplastic/mitochondrial; TrEMBL-Plants: tr|G7IZY8|G7IZY8_MEDTR Glutamyl-tRNA(Gln) amidotransferase subunit A, chloroplastic/mitochondrial; Found in the gene: LotjaGi6g1v0171200 15

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space:

Predicted domain Source Observations Saturation (%)
mobidb-lite MobiDBLite 1 50.00