ID   GATA_GRABC              Reviewed;         499 AA.
AC   Q0BTK2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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};
GN   OrderedLocusNames=GbCGDNIH1_0952;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI61850.1; -; Genomic_DNA.
DR   RefSeq; WP_011631659.1; NC_008343.2.
DR   AlphaFoldDB; Q0BTK2; -.
DR   SMR; Q0BTK2; -.
DR   STRING; 391165.GbCGDNIH1_0952; -.
DR   EnsemblBacteria; ABI61850; ABI61850; GbCGDNIH1_0952.
DR   KEGG; gbe:GbCGDNIH1_0952; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_5; -.
DR   OMA; EVSCPHF; -.
DR   Proteomes; UP000001963; 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..499
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_1000015836"
FT   ACT_SITE        79
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        159
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        183
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   499 AA;  52761 MW;  B395EF0C41831EAF CRC64;
     MSALTDLTIA EARDGLRAKR FSARELTDAH LGAIEALNPR LNAYITVTPD QARAQAAAAD
     RVLASGEAGA LTGIPVASKD MFCSEGIRTT AGSRILENFV PPYESAVTER MLRDGAVILG
     KANLDEFAMG SANLTSAYGP VENPWKRHDD DAVLVPGGSS GGSAAAVAAH LALGATGTDT
     GGSIRQPASY CGIAGIKPTY GRCSRWGIVA YASSLDQAGP FARTVRDNAI LLRSMAGHDP
     RDSTSAMREV PDFEAACQRG VKGLRIGLPR EYVADGMSEE IRTLWQNGAA MLRAAGAEVV
     DVSLPHTKHA LASYYIIAPA EASSNLARYD GVRFGHRSSD NRDLNDLYER SRAEGFGAEV
     KRRIMVGTYV LSAGYYDAYY LKAQKVRALI ARDFAEAFRS VDALLTPTAP SAAFAQGETI
     DDPVAMYLND VFTVPINLAG LPAMSIPAGL STTGLPLGLQ IIGRAFDEET VFAVSAALEQ
     AAAFTHRPAL RADTLNAGA