ID   GATA_LAWIP              Reviewed;         485 AA.
AC   Q1MPY8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-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=LI0885;
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00;
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) 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). {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; AM180252; CAJ54939.1; -; Genomic_DNA.
DR   RefSeq; WP_011526968.1; NC_008011.1.
DR   AlphaFoldDB; Q1MPY8; -.
DR   SMR; Q1MPY8; -.
DR   STRING; 363253.LI0885; -.
DR   PRIDE; Q1MPY8; -.
DR   KEGG; lip:LI0885; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_7; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000002430; 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..485
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_1000015851"
FT   ACT_SITE        78
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        153
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        177
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   485 AA;  52760 MW;  2DD52713E4ABCEFA CRC64;
     MTSDIHLSLA QIHNLLISRE KSVEEVTQAC LDRIIATEPT INAFITICAE EALSEAKKLD
     QSTPDPKKPL WGIPIAVKDN ILTKNIPTTA ASCMLKHFIP QYDAFIIQQL KNAGAIIIGK
     TNLDEFAMGS STETSFFGPT YNPWNTKCVP GGSSGGSAAS VAAFQCFSAI GTDTGGSIRQ
     PAALCGCIGL KPTYGRVSRY GIIAYASSLD QAGPITRTVE DAAIMLSVLA KHDPQDTTSS
     FKATDNYYIN LKKQDLTGIT IGIPKEFISE HIDPPILDIY QQAIEQAKEL GAKTIDLSLP
     HATDHAIATY YIIATAEASS NLARFDGVRY GYRAKNSHTL EELYINSRTK GFGEEVKRRI
     LLGTHVLSTD YYENYYHKAA QVRYLILQDF LSVFKKCDIL LTPVSPITAW EIGSTIKKPI
     TIYHKDIFTV SLNLAGLPGL SIPAGLVKGL PVGIQLIGQA FDESTLLSIG NILHKYLGPT
     SQPNL