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GATA_BRUME
ID   GATA_BRUME              Reviewed;         493 AA.
AC   Q8YC57;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   03-AUG-2022, entry version 99.
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=BMEII0675;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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=AAL53917.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008918; AAL53917.1; ALT_INIT; Genomic_DNA.
DR   PIR; AB3594; AB3594.
DR   RefSeq; WP_004681901.1; NZ_GG703779.1.
DR   AlphaFoldDB; Q8YC57; -.
DR   SMR; Q8YC57; -.
DR   STRING; 224914.BMEII0675; -.
DR   EnsemblBacteria; AAL53917; AAL53917; BMEII0675.
DR   GeneID; 29595292; -.
DR   KEGG; bme:BMEII0675; -.
DR   PATRIC; fig|224914.52.peg.2692; -.
DR   eggNOG; COG0154; Bacteria.
DR   OMA; EVSCPHF; -.
DR   PhylomeDB; Q8YC57; -.
DR   Proteomes; UP000000419; Chromosome II.
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..493
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105145"
FT   ACT_SITE        79
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        159
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        183
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   493 AA;  52477 MW;  D987B33D8DFCC25D CRC64;
     MSELTALTIA EARDKLKAKA ITATELTDAY LSAIDAANDA INAYVAVTHD QARSMAKASD
     ERIAKGEAGA LEGIPLGVKD LFATKGVHTQ ACSHILDGFK PEYESTVTAN LWADGAVMLG
     KLNMDEFAMG SSNETSYYGP VKNPWRAKGS NADLVPGGSS GGSAAAVAAH LCAGATATDT
     GGSIRQPAAF TGTVGIKPTY GRVSRWGTVA FASSLDQAGP IARDVRDAAI LMKSMASLDL
     KDTTSVDLPV PDYEAALGRS VKGMKIGIPR EYRVDGMPGE IEELWQKGIQ YLKDAGAEIV
     DISLPHTKYA LPAYYIVAPA EASSNLARYD GVRYGLRVPG KDIADMYEQT RAAGFGKEVK
     RRIMIGTYVL SAGYYDAYYL RAQKVRTLIK KDFEDVFAKG VDAILTPATP SAAFSLADEV
     LANDPVKMYL NDIFTVTVNM AGLPGIAVPA GLNGQGLPLG LQLIGRPFEE ETLFQAAHVI
     EQAAGRFTPA KWW
 
 
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