ID   GATA_AROAE              Reviewed;         490 AA.
AC   Q5P4D0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, 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}; OrderedLocusNames=AZOSEA17080;
GN   ORFNames=ebA3030;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR555306; CAI07833.1; -; Genomic_DNA.
DR   RefSeq; WP_011237547.1; NC_006513.1.
DR   AlphaFoldDB; Q5P4D0; -.
DR   SMR; Q5P4D0; -.
DR   STRING; 76114.ebA3030; -.
DR   PRIDE; Q5P4D0; -.
DR   EnsemblBacteria; CAI07833; CAI07833; ebA3030.
DR   KEGG; eba:ebA3030; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_4; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000006552; 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..490
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000241067"
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   490 AA;  51379 MW;  B3899CFCDE606DE3 CRC64;
     MINASLTELR AALDARKISS VELATLFLDR IERLDASLNA FITVDRDGAL EAARAADARI
     AAGDAGPLTG IPLAHKDVFC TEGVLTTCGS KMLANFVSPY DAHVVSLLKT AGAVSLGKTN
     MDEFAMGSSN ENSHFGPAKN PWDTTRIPGG SSGGSAAAVA ARLVPIATGT DTGGSVRQPA
     ALTGVTGIKP TYGVVSRYGM IAYASSLDQG GAFGASAADC AQLLTAMAGF DPRDSTSLER
     PAEDYSRELA APAAARPLAG LRIGLPKEFF GAGMADDVRA AVEAALDGYR ALGATTVDVS
     LPNAQLAIPA YYVIAPAEAS SNLSRFDGVR YGHRAAEYRD LAEMYSKSRA EGFGAEVKRR
     ILVGTYVLSH GYYDAYYLQA QKLRRLIAQD FQAALAGCDV IAGPTSPTTA WTIGEKSDDP
     VQMYLSDIYT IAVNLAGLPG LSHPCGFGAG ELPVGLQLVG DYFSEARLLN AAHRFQQASD
     WHLRRPAIAA