ID   GATA2_CLOAB             Reviewed;         478 AA.
AC   Q97EX8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A 2;
DE            Short=Glu-ADT subunit A 2;
DE            EC=6.3.5.7;
GN   Name=gatA2; OrderedLocusNames=CA_C2977;
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; AAK80919.1; -; Genomic_DNA.
DR   PIR; D97266; D97266.
DR   RefSeq; NP_349579.1; NC_003030.1.
DR   RefSeq; WP_010966260.1; NC_003030.1.
DR   AlphaFoldDB; Q97EX8; -.
DR   SMR; Q97EX8; -.
DR   STRING; 272562.CA_C2977; -.
DR   PRIDE; Q97EX8; -.
DR   EnsemblBacteria; AAK80919; AAK80919; CA_C2977.
DR   GeneID; 44999465; -.
DR   KEGG; cac:CA_C2977; -.
DR   PATRIC; fig|272562.8.peg.3162; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_9; -.
DR   OMA; TNPAAYN; -.
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..478
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A 2"
FT                   /id="PRO_0000105156"
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   478 AA;  52481 MW;  0AA0908BCF021707 CRC64;
     MEILDMTVEQ LRNAILDKHL KSEDIVKAYF DNIKRNEPEI NAYITLCEDY ALKEAKDVDK
     KIANGDKVGR LAGIPIAIKD NICTDGIKTT CASKMLYDFV PPYDATVIKK LKAEDAIIIG
     KVNMDEFAMG SSTENSAFKI TKNPRDITRV PGGSSGGSAA VVAAKMAPIS LGSDTGGSIR
     QPAAFCGVVG LKPTYGLVSR FGLIAFASSL DQIGPLGKTV KDCAELLEVI SGEDELDNTS
     SKKHEKEDYL EGIDDGIKGM KIGMPKEFLN DGLDPEIRKC IDDTIEKLKS LGAEVCEMSL
     PITEEGLSAY YIISSAEASS NLARFDGIRY GYRPDDFEDV YDLMETSRSE AFGDEVKRRI
     MLGTYALSSG YYDAYYKRAL KLKKKIKNEF KEAFENYDLI LSPVSPVLPF KIGEKKADPL
     QMYLADIYTV NINLAGIPAI SLPCSVSKEG LPIGLQLLGP HFGEKKIFRA ARALEKER