ID   GATA_BRADU              Reviewed;         491 AA.
AC   Q89K29;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=bll5089;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC50354.1; -; Genomic_DNA.
DR   RefSeq; NP_771729.1; NC_004463.1.
DR   RefSeq; WP_011087849.1; NC_004463.1.
DR   AlphaFoldDB; Q89K29; -.
DR   SMR; Q89K29; -.
DR   STRING; 224911.27353354; -.
DR   EnsemblBacteria; BAC50354; BAC50354; BAC50354.
DR   KEGG; bja:bll5089; -.
DR   PATRIC; fig|224911.5.peg.5166; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_5; -.
DR   InParanoid; Q89K29; -.
DR   OMA; EVSCPHF; -.
DR   PhylomeDB; Q89K29; -.
DR   Proteomes; UP000002526; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..491
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105144"
FT   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        182
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   491 AA;  52173 MW;  ECB5CB7E6B24DB42 CRC64;
     MTDLTSLTLA EARKGLAAKT FTSLELTDAH LSAIEAARVL NAFVMETPDR ARDMAREADG
     KIAKGDAGPL AGIPLGMTDL FATKGVRTTA CSKILGNFVP TYESTVTSQL WRDGAVMLGK
     LNNDEFAMGS ANETSCFGPV GNPWRREGSN TTLVPGGSSG GSASAVAALL CMGATATDTG
     GSIRQPAAFT ATVGIKPTYG RCSRWGIVAF ASSLDQAGPI ARSVRDSAML LRSMAGHDPK
     DTTSVDIPVP DYEAAIGKSV KGIRIGIPKE YRLDGMPAEI EKLWSEGAAW LKAAGAELVE
     VSLPHTKYAL PAYYIVAPAE ASSNLARYDG VRYGLREQGK NIIELYENTR AEGFGAEVRR
     RVMIGTYVLS AGYYDAYYLR AQKVRTLIKK DFEDCFAKGV NAILTPATPS AAFGIGEKGG
     ADPVEMYLND IFTVTVNMAG LPGIAVPAGK DAQGLPLGLQ LIGRPFDEET LFSLGEVIEQ
     AAGRFTPARW W