ID   GATA_MORCA              Reviewed;         492 AA.
AC   Q49091;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE            Short=Glu-ADT subunit A;
DE            EC=6.3.5.7;
GN   Name=gatA;
OS   Moraxella catarrhalis (Branhamella catarrhalis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 53879 / E22;
RA   Beaulieu D., Piche L., Parr T.R. Jr., Roeger-Lawry K., Rosteck P.,
RA   Roy P.H.;
RT   "The Moraxella (Branhamella) catarrhalis chromosomal beta-lactamase gene is
RT   flanked by an amidase gene and a conserved gene of unknown function.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
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; U49269; AAA92125.1; -; Genomic_DNA.
DR   RefSeq; WP_003668058.1; NZ_RCJJ01000004.1.
DR   AlphaFoldDB; Q49091; -.
DR   SMR; Q49091; -.
DR   STRING; 857571.EA1_07567; -.
DR   PRIDE; Q49091; -.
DR   eggNOG; COG0154; Bacteria.
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..492
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105176"
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   492 AA;  52936 MW;  8382818A82596CA7 CRC64;
     MTDLHHLSVH ELADGLKNKQ FSSHELVEHF ANRINRLDGQ INSFITKDFD NALAQAKLAD
     KLRAKGDNRP LLGVPMAHKD NLCTKGVLTT AGSKMLYNFV SPYDATVVDS IANSGFVSLG
     KLNMDEFAMG SDNESSYFGA VHNPWDVQRV PGGSSGGSAA AVAAGFVPVA TGSDTGGSIR
     QPASFCGITG IKPTYGRVSR YGMIAYASSL DQAGTFGKSA LDCAYLLAPM AGYDPKDATS
     INRPSEDYVA DILATKTDGK PLAGKKIGVA KAYFGAGLDS EVEKSIRTAL AKYEELGAKI
     VEVDITDPAI TLATYYLLAP AEASSNLSRY DGVRFGYRCE NPKDLHDLYT RSRSEGFGAE
     VQRRIIMGTY ALSAGYFDAY YTKAQKVRRL IVDDFKKAFE KCDIIASPTA PTPAYKLGES
     LDPASIYLLD VYTIGVNLAG LPALSHPVGQ ANGLPVGLQL ISKHWAESEL LKTAHIYQSH
     TDFHQAKADL VK