ID   GATA_MAGO7              Reviewed;         517 AA.
AC   A4QR60; G4N6S6;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
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};
GN   ORFNames=MGG_13483;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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, B and C subunits. {ECO:0000255|HAMAP-
CC       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; CM001234; EHA49893.1; -; Genomic_DNA.
DR   RefSeq; XP_003716212.1; XM_003716164.1.
DR   AlphaFoldDB; A4QR60; -.
DR   SMR; A4QR60; -.
DR   STRING; 318829.MGG_13483T0; -.
DR   EnsemblFungi; MGG_13483T0; MGG_13483T0; MGG_13483.
DR   GeneID; 5051641; -.
DR   KEGG; mgr:MGG_13483; -.
DR   VEuPathDB; FungiDB:MGG_13483; -.
DR   eggNOG; KOG1211; Eukaryota.
DR   HOGENOM; CLU_009600_7_6_1; -.
DR   InParanoid; A4QR60; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1195292at2759; -.
DR   Proteomes; UP000009058; 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; IPR020556; Amidase_CS.
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   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..517
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT                   mitochondrial"
FT                   /id="PRO_0000413354"
FT   REGION          106..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        58
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT   ACT_SITE        131
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT   ACT_SITE        155
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ   SEQUENCE   517 AA;  54881 MW;  80CC48912023071E CRC64;
     MLVHGRRLGL LLGRSHVAAP KHTSHLPRRT VHLNHFVSKG EAASEAEPPQ STFTVAVKDN
     IATQAHPTTC ASNILRDYTS PYEATVVRQL RRRGARVVGT TNLDEFGMGT HSTHSAHGPV
     ASPAGRSAGG SSGGSAVAVA AGEVEVALGT DTGGSVRLPA AYNGVVGFKP SYGMLSRYGV
     VPYANSLDTV GLLARSVERI RDLVVGEGLW AQHDDKDPTS LSAAARLRCA SGRTGYKGEA
     AKVGWEGLTF GIPLEYNIFE LDPLIREAWE EVAALLQSLG ANVVPVSLPT TRQALSAYYV
     LAPAEASSNL AKYDGVRYGN PGPESENEGG VLYSAARGAG FGDEVKRRIL LGAYSLSSEA
     MDNYFVQAQK VRRLVRGDFD RVFLLDNPLV DKEPTEEGFG EEAEQADLAD LHEDVPLLNK
     RGPARVDFIL SPTAPTPAPT LDEALSQTSL DSATNDVFTV PASLAGLPAI SLPVDMKEDV
     HGVGRFAGIQ IIGQYWDDAR LLDVAVALRG VLGRGLV