ID   GATA_ORITI              Reviewed;         492 AA.
AC   B3CQQ9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=OTT_0367;
OS   Orientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Orientia.
OX   NCBI_TaxID=334380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ikeda;
RX   PubMed=18508905; DOI=10.1093/dnares/dsn011;
RA   Nakayama K., Yamashita A., Kurokawa K., Morimoto T., Ogawa M., Fukuhara M.,
RA   Urakami H., Ohnishi M., Uchiyama I., Ogura Y., Ooka T., Oshima K.,
RA   Tamura A., Hattori M., Hayashi T.;
RT   "The whole-genome sequencing of the obligate intracellular bacterium
RT   Orientia tsutsugamushi revealed massive gene amplification during reductive
RT   genome evolution.";
RL   DNA Res. 15:185-199(2008).
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; AP008981; BAG39825.1; -; Genomic_DNA.
DR   RefSeq; WP_012461052.1; NC_010793.1.
DR   AlphaFoldDB; B3CQQ9; -.
DR   SMR; B3CQQ9; -.
DR   EnsemblBacteria; BAG39825; BAG39825; OTT_0367.
DR   GeneID; 66652548; -.
DR   KEGG; ott:OTT_0367; -.
DR   HOGENOM; CLU_009600_0_3_5; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000001033; 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.
FT   CHAIN           1..492
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_1000095157"
FT   ACT_SITE        78
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        182
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   492 AA;  53403 MW;  DA12734D771A103B CRC64;
     MNNLVKLTIS QAISGLKNKE FTATDLVTAH INQMDKYRCI NAYITEIPEL ALQAAKKSDF
     LIQTNQARPI EGIPVSIKDL FCTKGILTTA ASKMLQNFTP VYDATVYSKI INAGGIMLGK
     GNMDEFAMGS ANINSYFGNV INPWKAENDD IDLTPGGSSG GSSAAVAAFM AMAALGSDTG
     GSVRQPASYT GTVGIKPSYG RCSRWGMIAF SCSLDQAGII TRTVEDAAIM LETMMGYDEK
     DSTSLNVEVP NLRSAVNQPI KGMKIGIPYD LMENKSLSSE IITMWQNTIN LLKDHGVEIV
     SISLPYINYA LPVYYVLSSA EASSNLARYD GVRYGLRVEG KNSNINEIYE LSRSEGFGAE
     VKRRIMMGTY ALASTNINSY YIKAQQVRRL IVNDFTNSFN KVDCILIPSA PTAAFPLNSN
     QDDPVTMYLN DILTIPASLA GLPCISIPAG FSANKLPLGM QVIGSRLDEY NIIKISSAIE
     KALNLKFIPK GF