GatA Glutamyl-tRNA amidotransferase, subunit A [Drosophila melanogaster (fruit fly)] - Gene

Summary

Official Symbol: GatAprovided by FlyBase
Official Full Name: Glutamyl-tRNA amidotransferase, subunit Aprovided by FlyBase
Primary source: FLYBASE:FBgn0260779
Locus tag: Dmel_CG6007
See related: AllianceGenome:FB:FBgn0260779
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Drosophila melanogaster
Lineage: Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora
Also known as: 0929/02; bene; benedict; CG6007; Dmel\CG6007; gatA; GATA; l(3)S092902
Summary: Enables serine hydrolase activity. Predicted to be involved in glutaminyl-tRNAGln biosynthesis via transamidation and mitochondrial translation. Located in mitochondrion. Human ortholog(s) of this gene implicated in combined oxidative phosphorylation deficiency 40. Orthologous to human QRSL1 (glutaminyl-tRNA amidotransferase subunit QRSL1). [provided by Alliance of Genome Resources, Dec 2024]
Orthologs: all
NEW: Try the new Gene table
Try the new Transcript table

Annotation release	Status	Assembly	Chr	Location
Release 6.54	current	Release 6 plus ISO1 MT (GCF_000001215.4)	3R	NT_033777.3 (19026174..19028857, complement)
Release 5.57	previous assembly	Release 5 (GCF_000001215.2)	3R	NT_033777.2 (14851896..14854579, complement)

Chromosome 3R - NT_033777.3 Genomic Context describing neighboring genes

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

gatA expression is required cell autonomously for normal growth. The gatA gene is widely expressed in mitotic and endoreplicating tissues.
Title: Mutations in the Drosophila mitochondrial tRNA amidotransferase, bene/gatA, cause growth defects in mitotic and endoreplicating tissues.

Submit: New GeneRIF Correction

Function	Evidence Code	Pubs
enables catalytic activity	IEA Inferred from Electronic Annotation more info
enables glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity	IBA Inferred from Biological aspect of Ancestor more info
enables glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity	IEA Inferred from Electronic Annotation more info
contributes_to glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables serine hydrolase activity	HDA more info	PubMed

Process	Evidence Code	Pubs
involved_in glutaminyl-tRNAGln biosynthesis via transamidation	IBA Inferred from Biological aspect of Ancestor more info
involved_in glutaminyl-tRNAGln biosynthesis via transamidation	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in mitochondrial translation	IBA Inferred from Biological aspect of Ancestor more info
involved_in mitochondrial translation	ISS Inferred from Sequence or Structural Similarity more info
involved_in translation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of glutamyl-tRNA(Gln) amidotransferase complex	IBA Inferred from Biological aspect of Ancestor more info
part_of glutamyl-tRNA(Gln) amidotransferase complex	IEA Inferred from Electronic Annotation more info
part_of glutamyl-tRNA(Gln) amidotransferase complex	ISS Inferred from Sequence or Structural Similarity more info
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed

Names: CG6007-PA; GatA-PA; Glutamyl-tRNA(Gln) amidotransferase, subunit A; benedict; gatA; glutamyl-tRNA amidotransferase A; glutamyl-tRNA amidotransferase subunit A; lethal (3) S092902

NP_650775.2

NEW Try the new Transcript table

The following sections contain reference sequences that belong to a specific genome build. Explain