ID   GATA_PSE14              Reviewed;         483 AA.
AC   Q48E92;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=PSPPH_4174;
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6;
RX   PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA   Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA   Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA   Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA   Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ36055.1; -; Genomic_DNA.
DR   RefSeq; WP_004666201.1; NC_005773.3.
DR   AlphaFoldDB; Q48E92; -.
DR   SMR; Q48E92; -.
DR   STRING; 264730.PSPPH_4174; -.
DR   EnsemblBacteria; AAZ36055; AAZ36055; PSPPH_4174.
DR   KEGG; psp:PSPPH_4174; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_6; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000000551; 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.
FT   CHAIN           1..483
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000241134"
FT   ACT_SITE        76
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        151
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        175
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   483 AA;  51866 MW;  8B68CBB7B647FC36 CRC64;
     MHQMTLAEIA RGLAEKKFSS EELTRVLLSR IATLDPQLNS FISLTEDLAI TQAQAADARR
     AAGENGPLLG APLAHKDLFC TQGIRTSCGS RMLDNFKAPY DATVVSKLAS AGTVTLGKTN
     MDEFAMGSAN ESSHYGAVKN PWNLQCVPGG SSGGSAAAVA ARLLPAATGT DTGGSIRQPA
     ALTNLTGLKP TYGRVSRWGM IAYASSLDQA GPMARTAEDC ALLLQGMAGF DPQDSTSIDE
     PVPDYSASLN TSLKGLRIGV PKEYFSAGLD PRIAQLVHES VKELEKLGAV VKEVSLPNLQ
     HAIPAYYVIA PAEASSNLSR FDGVRFGYRC EDPKDLTDLY KRSRAEGFGP EVQRRIMVGA
     YALSAGYYDA YYLQAQKIRR LIKNDFMSAF AEVDVILGPT TPNPAWKIGA KTNDPIAEYL
     EDFYTITANL AGLPGLSMPA GFVDGLPVGV QLLAPYFQEG RLLNVAHQYQ QVTDWHTRAP
     EGF