ID   GATA_XENTR              Reviewed;         524 AA.
AC   Q0VFI5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2006) 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; BC118816; AAI18817.1; -; mRNA.
DR   RefSeq; NP_001072779.1; NM_001079311.1.
DR   AlphaFoldDB; Q0VFI5; -.
DR   SMR; Q0VFI5; -.
DR   STRING; 8364.ENSXETP00000041743; -.
DR   PaxDb; Q0VFI5; -.
DR   Ensembl; ENSXETT00000041743; ENSXETP00000041743; ENSXETG00000027717.
DR   GeneID; 780239; -.
DR   KEGG; xtr:780239; -.
DR   CTD; 55278; -.
DR   Xenbase; XB-GENE-5787967; qrsl1.
DR   eggNOG; KOG1211; Eukaryota.
DR   HOGENOM; CLU_009600_7_6_1; -.
DR   InParanoid; Q0VFI5; -.
DR   OrthoDB; 1195292at2759; -.
DR   PhylomeDB; Q0VFI5; -.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000027717; Expressed in testis and 13 other tissues.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
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_0000316772"
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;  56803 MW;  165B5627CA6F6682 CRC64;
     MLGMSLREAA AALRLGQIKP TELCQKCLSF IKETSFLNAY ITVTEDFALK QAAEADERFI
     QGKPLGDLDG IPIAIKDNFS TAGIETTCAS RMLKGYIAPY NATVVQKLFD QGAVFMGKTN
     LDEFAMGSGS TDSIFGPVKN PWSYSRSYID KTSLSHHAAK DDSDWVITGG SSGGSACAVS
     AGTCYLAIGS DTGGSTRNPA SHCGVVGLKP TYGLVSRHGL IPLVNSMDVP GIVTRCVDDA
     ATVLGVLAGH DPYDSTTIQD PFQPFSLPEK VDVRNVCIGI PKEYHAPGLS AEILSLWSET
     ADLLENAGAK VVEVSLPHTP YSIVCYHVLC TAEVASNMAR FDGLEYGHRS DIDDSTEALY
     AATRREGFNE VVRGRILSGN YFLLKRNYEK YFVKAQKVRR LIADDFVKVF NSGVHVLLTP
     TTLGDAAPYL EFIQEDNRTR SAQEDVFTQC ANMAGLPAVT VPAALSSRGL PLGLQFIGRA
     FCEQQLLTIA KWFEKQIDFS PLQFNRDSEN GNIVQQYSKS ASSV