ID   GATA_XENLA              Reviewed;         524 AA.
AC   Q8AVG9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) 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; BC042285; AAH42285.1; -; mRNA.
DR   RefSeq; NP_001080891.1; NM_001087422.1.
DR   AlphaFoldDB; Q8AVG9; -.
DR   SMR; Q8AVG9; -.
DR   DNASU; 380585; -.
DR   GeneID; 380585; -.
DR   KEGG; xla:380585; -.
DR   CTD; 380585; -.
DR   Xenbase; XB-GENE-5787983; qrsl1.L.
DR   OrthoDB; 1195292at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 380585; Expressed in testis and 19 other tissues.
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..524
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT                   mitochondrial"
FT                   /id="PRO_0000316771"
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   524 AA;  56786 MW;  CB56D6E354D5F953 CRC64;
     MLGMSLREAA AVLRLGQVKP TELCQKCLSL IKETSFLNAY ITITEDIALK QAAEADKRFA
     QGKPLGELDG IPIAIKDNFS TAGIETTCAS RMLKGYVAPY NATVVQKLFD QGAVLMGKTN
     LDEFGMGSGS TDSIFGPVRN PWSYSRSYIE KRPISHHAAK DDSDWVIAGG SSGGSACAVS
     AGTCYLAIGS DTGGSTRNPA SHCGVVGLKP TYGLVSRHGL IPLVNSMDIP GILTRCVDDA
     ATVLGMLAGH DLYDSTTVQD PFQPFSLPET IDLSNLCIGI PKEYHAPGLS TEILSLWSKT
     ADLLEKAGAK VMEVSLPHTP YSIVCYHVLC TAEVASNMAR FDGLEYGHRS DIDDSTEAMY
     AATRREGFND VVRGRILSGN YFLLKQNYEK YFVKAQKVRR LIADDFVKVF NSGVHVLLTP
     TTLGDAAPYL EFIQEDNRTR SAEEDVFTQC TNMAGLPAVT VPAGLSSRGL PLGLQFIGRA
     FCERQLLTVA KWCEKQMDFS PLQFNRDLGN GSIVLQYSKS ASFV