ID   GATA_PSEAE              Reviewed;         484 AA.
AC   Q9HVT8;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=PA4483;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(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). {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; AE004091; AAG07871.1; -; Genomic_DNA.
DR   PIR; H83084; H83084.
DR   RefSeq; NP_253173.1; NC_002516.2.
DR   RefSeq; WP_003112871.1; NZ_QZGE01000004.1.
DR   PDB; 4WJ3; X-ray; 3.70 A; A/D/G/J=1-484.
DR   PDBsum; 4WJ3; -.
DR   AlphaFoldDB; Q9HVT8; -.
DR   SMR; Q9HVT8; -.
DR   STRING; 287.DR97_1662; -.
DR   PaxDb; Q9HVT8; -.
DR   PRIDE; Q9HVT8; -.
DR   EnsemblBacteria; AAG07871; AAG07871; PA4483.
DR   GeneID; 881180; -.
DR   KEGG; pae:PA4483; -.
DR   PATRIC; fig|208964.12.peg.4693; -.
DR   PseudoCAP; PA4483; -.
DR   HOGENOM; CLU_009600_0_3_6; -.
DR   InParanoid; Q9HVT8; -.
DR   OMA; EVSCPHF; -.
DR   PhylomeDB; Q9HVT8; -.
DR   BioCyc; PAER208964:G1FZ6-4572-MON; -.
DR   Proteomes; UP000002438; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..484
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105189"
FT   ACT_SITE        77
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        152
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        176
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   484 AA;  51863 MW;  B94A96E6EB1C3A6E CRC64;
     MLHQLTLAEI ARALADKQFS AEELTRTLLG RIRQLDPQLN SFISITDDLA IAQAKAADER
     RANGENGALL GAPIAHKDLF CTQGVRTSCG SKMLDNFVSP YDATVVEKLT AAGAVTLGKL
     NMDEFAMGSS NQSSHYGAVK NPWSLDRVPG GSSGGSAAAV AARLLPAATG TDTGGSIRQP
     AALTNLTGIK PTYGRVSRWG MIAYASSLDQ GGPLARTAED CALMLGVMAG FDPKDSTSVE
     QPVDDYLAAL QKPLSGLRIG LPREYFGAGL DSRIADAVLA VVEELKTLGA TVKDISLPNM
     QHAIPAYYVI APAEASSNLS RFDGVRYGYR CDAPQNLEDL YKRSRAEGFG SEVKNRIMVG
     TYALSAGYYD AYYLQAQKIR RLIKNDFVSA FAEVDVILGP TTPNPAWKIG EKNDDPVSQY
     LEDIYTITAN LAGLPGLSMP AGFVDGLPVG VQLLAPYFQE GRLLNVAHQY QQVSDWHTRT
     PAGF