ID   GATA_CHLTR              Reviewed;         491 AA.
AC   O84006;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE            Short=Glu-ADT subunit A;
DE            EC=6.3.5.7;
GN   Name=gatA; OrderedLocusNames=CT_003;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC67593.1; -; Genomic_DNA.
DR   PIR; F71568; F71568.
DR   RefSeq; NP_219505.1; NC_000117.1.
DR   RefSeq; WP_009871349.1; NC_000117.1.
DR   AlphaFoldDB; O84006; -.
DR   SMR; O84006; -.
DR   STRING; 813.O172_00020; -.
DR   EnsemblBacteria; AAC67593; AAC67593; CT_003.
DR   GeneID; 884087; -.
DR   KEGG; ctr:CT_003; -.
DR   PATRIC; fig|272561.5.peg.4; -.
DR   HOGENOM; CLU_009600_0_3_0; -.
DR   InParanoid; O84006; -.
DR   OMA; EVSCPHF; -.
DR   Proteomes; UP000000431; 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..491
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105153"
FT   ACT_SITE        77
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        152
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        176
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   491 AA;  53588 MW;  00773EB3B3F6BDF2 CRC64;
     MYRKSALELR DAVVNRELSV TAITEYFYHR IESHDEQIGA FLSLCKERAL LRASRIDDKL
     AKGDPIGLLA GIPIGVKDNI HITGVKTTCA SKMLENFVAP FDSTVVRRIE MEDGILLGKL
     NMDEFAMGST TRYSAFHPTN NPWDLERVPG GSSGGSAAAV SARFCPIALG SDTGGSIRQP
     AAFCGVVGFK PSYGAVSRYG LVAFGSSLDQ IGPLTTVVED VALAMDAFAG RDPKDSTTRD
     FFKGTFSQAL SLEVPKLIGV PRGFLDGLQE DCKENFFEAL AVMEREGSRI IDVDLSVLKH
     AVPVYYIVAS AEAATNLARF DGVRYGHRCA QADNMHEMYA RSRKEGFGKE VTRRILLGNY
     VLSAERQNIF YKKGMAVRAR LIDAFQAAFE RCDVIAMPVC ATPAIRDQDV LDPVSLYLQD
     VYTVAVNLAY LPAISVPSGL SKEGLPLGVQ FIGERGSDQQ ICQVGYSFQE HSQIKQLYPK
     AVNGLFDGGI E