ID   GATA_RAT                Reviewed;         525 AA.
AC   Q5FWT5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03150};
DE            Short=Glu-AdT subunit A {ECO:0000255|HAMAP-Rule:MF_03150};
DE            EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_03150};
DE   AltName: Full=Glutaminyl-tRNA synthase-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03150};
GN   Name=Qrsl1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in the
CC       mitochondria. The reaction takes place in the presence of glutamine and
CC       ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC       {ECO:0000255|HAMAP-Rule:MF_03150}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC         L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; EC=6.3.5.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03150};
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC       complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_03150}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03150}.
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DR   EMBL; BC089213; AAH89213.1; -; mRNA.
DR   RefSeq; NP_001014056.1; NM_001014034.1.
DR   RefSeq; XP_006256650.1; XM_006256588.3.
DR   AlphaFoldDB; Q5FWT5; -.
DR   SMR; Q5FWT5; -.
DR   STRING; 10116.ENSRNOP00000018891; -.
DR   PaxDb; Q5FWT5; -.
DR   Ensembl; ENSRNOT00000018892; ENSRNOP00000018891; ENSRNOG00000026049.
DR   GeneID; 309911; -.
DR   KEGG; rno:309911; -.
DR   CTD; 55278; -.
DR   RGD; 1359490; Qrsl1.
DR   eggNOG; KOG1211; Eukaryota.
DR   GeneTree; ENSGT00550000074866; -.
DR   HOGENOM; CLU_009600_7_6_1; -.
DR   InParanoid; Q5FWT5; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1195292at2759; -.
DR   PhylomeDB; Q5FWT5; -.
DR   TreeFam; TF313766; -.
DR   PRO; PR:Q5FWT5; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000026049; Expressed in heart and 19 other tissues.
DR   Genevisible; Q5FWT5; RN.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; ISO:RGD.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; ISO:RGD.
DR   GO; GO:0032543; P:mitochondrial translation; ISO:RGD.
DR   GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   HAMAP; MF_00120; GatA; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR004412; GatA.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   TIGRFAMs; TIGR00132; gatA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..525
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT                   mitochondrial"
FT                   /id="PRO_0000316770"
FT   ACT_SITE        76
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT   ACT_SITE        168
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT   ACT_SITE        192
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ   SEQUENCE   525 AA;  56838 MW;  CF281FD359C8F741 CRC64;
     MLGRTLREVS SALKQGHITP TELCKKCLSL IKKTKYLNAY ITVSEEVALK QAEESEKRYK
     QGQSLGDLDG IPVAVKDNFS TSGIETTCAS NMLKGYLPPY NATVVQRLLD QGALLMGKTN
     LDEFAMGSGS TDGVFGPVKN PWTYSKQYRE RSRQDAQEDS HWLITGGSSG GSAAAVAAFT
     CFAALGSDTG GSTRNPAAHC GTVGFKPSYG LVSRHGLIPL VNSMDVPGIF TRCVDDTAIV
     LGVLAGHDPK DSTTVNDPVK PTTLPSVPDV SGLCIGIPKE YLVPELSSEI RSLWSQAADL
     FEAEGARVIE VCLPHTCYSI VCYHVLCTSE VASNMARFDG LQYGHRSAVD MSSTEALYAA
     TRQEGFNDVV KGRILSGNFF LLKENYENYF VKAQKVRRLI VNDFVNVFGS GVDVLLTPTT
     LTQAVPYLEF IKEDNRTRSA QDDIFTQAVN MAGLPAVNVP VALSSQGLPI GLQLIGRAFC
     DQQLLTVAKW FEKQVQFPVI QLQDLMDDGS LVPENGKLTS GSLTQ