ID   GATA_MACFA              Reviewed;         528 AA.
AC   Q4R7R9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
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 {ECO:0000255|HAMAP-Rule:MF_03150};
GN   ORFNames=QtsA-10264, QtsA-14543;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB168163; BAE00288.1; -; mRNA.
DR   EMBL; AB168744; BAE00853.1; -; mRNA.
DR   RefSeq; NP_001271511.1; NM_001284582.1.
DR   AlphaFoldDB; Q4R7R9; -.
DR   SMR; Q4R7R9; -.
DR   STRING; 9541.XP_005552298.1; -.
DR   GeneID; 101926039; -.
DR   CTD; 55278; -.
DR   VEuPathDB; HostDB:ENSMFAG00000032880; -.
DR   eggNOG; KOG1211; Eukaryota.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1195292at2759; -.
DR   Proteomes; UP000233100; Chromosome 4.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule.
DR   GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
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.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..528
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT                   mitochondrial"
FT                   /id="PRO_0000316768"
FT   REGION          147..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        76
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT   ACT_SITE        171
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT   ACT_SITE        195
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ   SEQUENCE   528 AA;  57467 MW;  865AFEF725F96419 CRC64;
     MLGRTLQEVS AALKQGQITP TELCQKCLSL IKKTKFLNAY ITVSEEVALK QAEESEKRYK
     NGQSLGDLDG IPVAVKDNFS TSGIETTCAS NMLKGYIPPY NATVVQKLLD QGALLMGKTN
     LDEFAMGSGS TDGIFGPVKN PWSYSKQYRE KRKQNPHSKN EDSDWLITGG SSGGSAAAVS
     AFTCYAALGS DTGGSTRNPA AHCGLVGFKP SYGLVSRHGL IPLVNSMDVP GILTRCVDDA
     AIVLGALAGP DPKDSTTVHD PINKPFMLPS LADVSKLCIG IPKEYLIPEL SSEVRSLWSK
     AADLFESEGA KVLEVSLPHT SYSIVCYHVL CTSEVASNMA RFDGLQYGHR CDINVSTEAM
     YAATRREGFN DVVRGRILSG NFFLLKENYE NYFVKAQKVR RLIANDFVNA FNSGVDVLLT
     PTTLSEAVPY LEFIKEDNRT RSAQDDIFTQ AVNMAGLPAV SIPVALSNQG LPIGLQFIGR
     AFCDQQLLTV AKWFEKQVQF PFIQLQELMD DCSAVLENEK SASVSLKQ