ID   GATA_COCP7              Reviewed;         499 AA.
AC   C5P3I5;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=CPC735_061260;
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; ACFW01000015; EER28253.1; -; Genomic_DNA.
DR   RefSeq; XP_003070398.1; XM_003070352.1.
DR   AlphaFoldDB; C5P3I5; -.
DR   SMR; C5P3I5; -.
DR   PRIDE; C5P3I5; -.
DR   EnsemblFungi; EER28253; EER28253; CPC735_061260.
DR   GeneID; 9695893; -.
DR   KEGG; cpw:CPC735_061260; -.
DR   VEuPathDB; FungiDB:CPC735_061260; -.
DR   HOGENOM; CLU_009600_7_6_1; -.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
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.
DR   TIGRFAMs; TIGR00132; gatA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..499
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT                   mitochondrial"
FT                   /id="PRO_0000413351"
FT   ACT_SITE        61
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT   ACT_SITE        139
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT   ACT_SITE        163
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ   SEQUENCE   499 AA;  53643 MW;  0C1766BFB0EE215F CRC64;
     MSLLREAERC LVNRKAFASL NAFVTPLDRV GSWIERVKDA DARRKRGAPK SSLDGKLIAI
     KDNICTRDVR TTCASAILEN FTSPFNATVV ELLEESGAIV AGKTNLDEFG MGSHSTYSHF
     GPVKGVRADD LGYVSAGGSS GGSAIAVATE QCYAALGTDT GGSVRLPAAY TGTVGFKPSY
     GLLSRWGVVA YANSLDTVGI IGANTSTVSE VFGVLNRYDH RDPTSISKAT RSRIDEITGS
     TSKTRSERLR IGVPIEYNIL ELDPFVRETW RKSIQHLKNQ GHTVHPVSLP ATKQALSAYY
     VLAPAEASSN LAKYDGVRYG TRDLDSPDNT GGYLYARSRG SGFGPEVKRR IVLGAFSLSA
     EAIDNYFIQA QKVRRLVQSD FNKVFRLHNP LLQATLTSHP KALESDGDTA EKVDVLVCPT
     APSPPPLLCS LENAAPTEAY TNDVFTVPAS LAGLPALSVP VTPGDREQES PLGIQVIGQF
     GDDQLVLDVG SRLEKMNIQ