ID   GATA_AJECG              Reviewed;         521 AA.
AC   C0NYZ7;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 52.
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=HCBG_08377;
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) 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, 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; GG663377; EEH03437.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NYZ7; -.
DR   SMR; C0NYZ7; -.
DR   STRING; 447093.C0NYZ7; -.
DR   EnsemblFungi; EEH03437; EEH03437; HCBG_08377.
DR   VEuPathDB; FungiDB:HCBG_08377; -.
DR   HOGENOM; CLU_009600_7_6_1; -.
DR   InParanoid; C0NYZ7; -.
DR   OrthoDB; 1195292at2759; -.
DR   Proteomes; UP000001631; 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; 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..521
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT                   mitochondrial"
FT                   /id="PRO_0000413346"
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   521 AA;  55651 MW;  4E9265368BB1ACE1 CRC64;
     MSLLREAEKC LANQKTYASL NAFITPLQRA GPWRDRVRDS DTRRERGVTK SPLDGKLVAI
     KDNICTRDMP TTCASRILDT YTSPFNATVV ESLEKSGAII AGKTNLDEFG MGSHSMHSHF
     GPVKNVTESR REPISPGGSS GGSAVAVATG QCYAALGTDT GGSVRLPAAY TGTVGFKPSY
     GHVSRWGVVA YANSLDTVGV LGSSISTIRE VYKTINHPDL HDPTNLPPAT RTRLTAAVHN
     SSTTRSSPSP YLRIGIPTEY NIHELSPTVR TAWQRSIVHL QRMGHTILPV SLPATKHALA
     AYYVLAPAEA SSNLARYDGV RYGTRDTDAP DDAEPGGYLY ASSRGKGLGS EVKRRILLGA
     FSLSADAIDN YFLQAQRVRR LVQADFERVF RVKNPLLPAV DVDADVDGRD KKQIAGDNAG
     VDVLVVPTAP TLPPTVESLK RASTVETYMN DIFTVPASLA GLPALSVPVQ MRGLSTVGDG
     DESKGDGADA AFGSVGIQAI GQFGDDEMVL HVGEMLEGMH G