ID   GATA_ALKHC              Reviewed;         485 AA.
AC   Q9Z9W9; Q9JPV8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE            Short=Glu-ADT subunit A;
DE            EC=6.3.5.7;
GN   Name=gatA; OrderedLocusNames=BH0666;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=10086842; DOI=10.1007/s007920050096;
RA   Takami H., Nakasone K., Ogasawara N., Hirama C., Nakamura Y., Masui N.,
RA   Fuji F., Takaki Y., Inoue A., Horikoshi K.;
RT   "Sequencing of three lambda clones from the genome of alkaliphilic Bacillus
RT   sp. strain C-125.";
RL   Extremophiles 3:29-34(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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) (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB011836; BAA75313.1; -; Genomic_DNA.
DR   EMBL; BA000004; BAB04385.1; -; Genomic_DNA.
DR   PIR; T44294; T44294.
DR   RefSeq; WP_010896842.1; NC_002570.2.
DR   AlphaFoldDB; Q9Z9W9; -.
DR   SMR; Q9Z9W9; -.
DR   STRING; 272558.10173280; -.
DR   EnsemblBacteria; BAB04385; BAB04385; BAB04385.
DR   KEGG; bha:BH0666; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_9; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000001258; 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..485
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105136"
FT   ACT_SITE        79
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        154
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   485 AA;  52888 MW;  914C7A27D0FB9167 CRC64;
     MSLFDLKLKD VHTKLHEKEI SVSDLVDEAY KRIEQVDGQV EAFLALNEEK ARAYAKELDA
     ALDRSEARGL LFGIPIGVKD NIVTKNLRTT CSSRILGNFD PIYDATVVHK LREAQAVTIG
     KLNMDEFAMG SSTENSAFQK TKNPWNLEYV PGGSSGGSAA AVAAGEVPFT LGSDTGGSIR
     QPAAYCGVVG LKPTYGRVSR YGLVAFASSL DQIGPITRNV EDNAYLLQAI SGHDPMDSTS
     ANLDVPDYLS ALTGDIKGLK IAVPKEYLGE GVKEEVKQSV LDALKVLEGL GATWEEVSLP
     HSKYALATYY LLASSEASAN LARFDGVRYG FRSDNADNLL DMYKQTRAEG FGDEVKRRIM
     LGTFALSSGY YDAYYKKAQQ VRTLIKQDFE KVFEQYDVII GPTTPTPAFK IGEKTDDPLT
     MYANDILTIP VNLAGVPAIS VPCGFDNGLP LGLQIIGKHF DEGSVYRVAH AFEQATDYHT
     KRPTL