ID   GATA1_CLOAB             Reviewed;         485 AA.
AC   Q97FQ7;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A 1;
DE            Short=Glu-ADT subunit A 1;
DE            EC=6.3.5.7;
GN   Name=gatA1; OrderedLocusNames=CA_C2670;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80617.1; -; Genomic_DNA.
DR   PIR; F97228; F97228.
DR   RefSeq; NP_349277.1; NC_003030.1.
DR   RefSeq; WP_010965958.1; NC_003030.1.
DR   AlphaFoldDB; Q97FQ7; -.
DR   SMR; Q97FQ7; -.
DR   STRING; 272562.CA_C2670; -.
DR   EnsemblBacteria; AAK80617; AAK80617; CA_C2670.
DR   GeneID; 44999161; -.
DR   KEGG; cac:CA_C2670; -.
DR   PATRIC; fig|272562.8.peg.2860; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_9; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000000814; 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 1"
FT                   /id="PRO_0000105155"
FT   ACT_SITE        79
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        154
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   485 AA;  53209 MW;  2EF96CE7A8D2D8C6 CRC64;
     MELYKLKAHE LKDMISKKEV KVEEVTNSFL NRIEEVDEKV NALLYVAKEE AVNTAKELDK
     KIESGESLSG LSGVPVAIKD NISVKNMQNT CASKILEGYV SPYDATVIEN LKKNNGVIIG
     KANMDEFAMG SSTENSAFKV SKNPWSLERV PGGSSGGSAV AVASLEAPIS LGTETGGSVR
     QPASFCGLVG LKPTYGRISR YGVVAFGSTL DQVGMFARDV EDCALLTQNI AGLDKMDFTT
     VDTPVQDYSK SLNKDLKGRK IGIPKEFFEE GLDEGVREAV KEAIKVFEEN GAEVKECSLP
     LSDYALAAYY IISSAEASSN LARFDGVRYG YRDAEAENAL DLYVKSRSKG FGEEAKRRIM
     LGTYVLSKGY YDAYYKKALK VRSLIKNDFQ RAFKEFDAII TPTTPTPAFR IGEKTKDVLS
     MYMSDIYTVP VNIAGIPSIS VPCGFVSGLP VGLQIMGNYF KEDTLFNLAY SYEQSTKWHD
     KIANL