ID   GATA_FRATF              Reviewed;         481 AA.
AC   A7NEM1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            Short=Glu-ADT subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00120};
GN   Name=gatA {ECO:0000255|HAMAP-Rule:MF_00120}; OrderedLocusNames=FTA_1949;
OS   Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=458234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FTNF002-00 / FTA;
RX   PubMed=19756146; DOI=10.1371/journal.pone.0007041;
RA   Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J.,
RA   Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W.,
RA   Lion C., Dempsey M.P.;
RT   "Complete genome sequence of Francisella tularensis subspecies holarctica
RT   FTNF002-00.";
RL   PLoS ONE 4:E7041-E7041(2009).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in organisms
CC       which lack glutaminyl-tRNA synthetase. The reaction takes place in the
CC       presence of glutamine and ATP through an activated gamma-phospho-Glu-
CC       tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_00120}.
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_00120};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00120}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00120}.
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DR   EMBL; CP000803; ABU62424.1; -; Genomic_DNA.
DR   RefSeq; WP_003017412.1; NC_009749.1.
DR   AlphaFoldDB; A7NEM1; -.
DR   SMR; A7NEM1; -.
DR   KEGG; fta:FTA_1949; -.
DR   HOGENOM; CLU_009600_0_3_6; -.
DR   OMA; EVSCPHF; -.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro.
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:0006412; P: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   TIGRFAMs; TIGR00132; gatA; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..481
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_1000015831"
FT   ACT_SITE        74
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        173
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   481 AA;  52396 MW;  CDA715EBE4E4D709 CRC64;
     MSYIKKLRAR LDSGEISAVE LTKEYLAKIK EQDKRINSII TLCEAEALKE AEDADAIISA
     GKQGLLTGIP ILHKDLFCTK GIRTTAASKM LDNFVAPYDS TVTKNCKDQG MVTLGKLNMD
     EFAMGSTNEY SYYGAVSNPW DLERVPGGSS GGSAAAVAAG FAPISTGSDT GGSVRQPASF
     CGLTAMKPSY GSTSRFGMVA FASSFDQAGI FGHYAEDVAI MLDAIAGECE FDSTCVGVKQ
     NHFTQDLEKD ISSKVIGVDE SLIKDLPAQI QEAVSKTLDN FKKLGAEIKS VKVPDLKEAL
     STYYIITPAE AAANLARYDG IRYGYRNPEA RDLDELYRKS RTDGFGAEVK RRIMIGNYVL
     ASSQYDSYYN KAQQLRKVMT DQINQIFTQV DAIFMPASPS EAFKKGDKLD PVSAYLSDIY
     TIPANISGLP AIAFPIGFAN NLPVGGQLMA KAFNDNILTQ MVVQYQKHYG IEEFILQQAR
     I