ID   GATA_WOLTR              Reviewed;         489 AA.
AC   Q5GRM3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   25-MAY-2022, entry version 97.
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=Wbm0763;
OS   Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=292805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRS;
RX   PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA   Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA   Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA   Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA   Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA   Koonin E., Slatko B.;
RT   "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT   human pathogenic nematode.";
RL   PLoS Biol. 3:599-614(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   -!- SEQUENCE CAUTION:
CC       Sequence=AAW71351.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017321; AAW71351.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041571512.1; NC_006833.1.
DR   AlphaFoldDB; Q5GRM3; -.
DR   SMR; Q5GRM3; -.
DR   STRING; 292805.Wbm0763; -.
DR   EnsemblBacteria; AAW71351; AAW71351; Wbm0763.
DR   KEGG; wbm:Wbm0763; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_5; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000000534; 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..489
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000241177"
FT   ACT_SITE        80
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        160
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        184
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   489 AA;  53031 MW;  49BA39BE9A308599 CRC64;
     MNELRKLSIA QMHNGLKQRS FSAVELIEVH INAVENEKLN AFITKTPEIA IKAAKTADER
     FSQQKDSTIS PLMGIPVGVK DLFCTKGVKT TACSKMLENF IPTYESTVSD LLLKSGAAML
     GKLNMDEFAM GSANINSYFG PVENVWVRKS DGEKVVPGGS SGGSAASVAG FLCAGALGSD
     TGGSVRQPAA YCGVVGAKPT YGRCSRFGMI AFASSLDQAG VITRSVSDSA LMLETICGYD
     NKDSTSSERP VPRFSNFING DIKGRRIGIP KEYRMDGISE EIIYHWEKVS SDLKENGAEV
     VDITLPHTKY AIPVYYLICS AEASSNLARY DGVRYGLRVN ADILEEMYSL TRAEGFGKEV
     KRRILIGAYA LSSGHYNEYY EKAQCIRALI RNDFIKAFEK IDYILVPSAP TEAFGLNEKP
     DPLIMCINDV FTVPASLAGL PAISVPVGLS NEGLPLALQV IGNYYDEAGM LNVASVIEQN
     CSRIIKLNS