ID   GATA_KINRD              Reviewed;         516 AA.
AC   A6W7L7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Krad_1318;
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX   NCBI_TaxID=266940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX   PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA   Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA   Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT   "Survival in nuclear waste, extreme resistance, and potential applications
RT   gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL   PLoS ONE 3:e3878-e3878(2008).
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; CP000750; ABS02806.1; -; Genomic_DNA.
DR   RefSeq; WP_012084338.1; NC_009664.2.
DR   AlphaFoldDB; A6W7L7; -.
DR   SMR; A6W7L7; -.
DR   STRING; 266940.Krad_1318; -.
DR   EnsemblBacteria; ABS02806; ABS02806; Krad_1318.
DR   KEGG; kra:Krad_1318; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_11; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000001116; 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..516
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_1000076132"
FT   ACT_SITE        92
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        167
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        191
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   516 AA;  53251 MW;  0A7BB7AB0729F9FC CRC64;
     MSGSASELVR WDAARLSEAL RAGEVSAEEV TRAHLDRIDA VDGPTSGAGE TGVHAFLHVD
     HEGALARARQ IDADRAAGAE LGPLAGVPIG VKDVLTTKGL PTTAGSRMLQ GWVPPYDATV
     VRELHAAGLV VLGKTNMDEF AMGSTTEHSA YGVTRNPWDP TRIPGGSGGG SAAALAAFEA
     PLTIGSDTGG SIRQPAAVTG TVGVKPTYGA VSRYGLIALA SSLDQAGPCA RTVLDTALLH
     AVIAGHDPYD STSIPAAVPD VVGAARLGAT GDLAGVRVGV VRELSGEGYE PGVLARFEES
     LTELRAAGAE VVELSLPNIV HALAAYYLIL PSEASSNLAK FDGMRYGLRV VPEGEHVTAE
     AVMRATRAAG FGDEAKRRII LGTYALSAGY YDAYYGSAQK VRTLVQRDFD AAFGSVDVLV
     SPTAPTVAYR LGEKLDDPLA MYAGDVATIP ANLAGIPGMS LPCGLSEGLP VGLQVLAPQQ
     ADDRLYRVGA ALEARLNDKW GGPLLAQVPT WQGASA