ID GATA_LACH4 Reviewed; 479 AA.
AC A8YTZ6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=lhv_0554;
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571;
RX PubMed=17993529; DOI=10.1128/jb.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(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; CP000517; ABX26734.1; -; Genomic_DNA.
DR RefSeq; WP_012211518.1; NC_010080.1.
DR AlphaFoldDB; A8YTZ6; -.
DR SMR; A8YTZ6; -.
DR KEGG; lhe:lhv_0554; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_9; -.
DR Proteomes; UP000000790; 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; Amidase signature (AS) domain; 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 NCBIfam; TIGR00132; gatA; 1.
DR PANTHER; PTHR11895:SF151; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A; 1.
DR PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..479
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000071368"
FT ACT_SITE 71
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 170
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 479 AA; 51788 MW; 4BA3A72CBB180238 CRC64;
MNYLNENIDS LNKKLASGDL SADKLAKDTV ANIKDTDKKL NAWITVVDDA KPAENLDFSK
SKLAGIPIAI KDNIITNGIK TTAASHMLYN YMPMYDATVI SKLKKAGATF VGKTNMDEFA
MGSSTEHSYY GVTHNPWNLD KVPGGSSGGS AAAVAGGQVV AALGSDTGGS IRQPAAFNGI
FGIKPTYGRV SRWGLIAFGS SLDQIGVMTK RVKDSAEVLN VIAGGDEHDS TVSTREVPDF
TKFIGQDVKG LRVAVPKEYM EAVSGEMREV IQKQIDALKD AGAIINEVSL PHTKYVVPDY
YIIASSEASS NLQRYDGIRY GYRAEDTKSL LDVYVKSRSE GFGAEVKRRI MLGSFALSAG
SYDRFFRQAA KVRTLICNDF DKIFAENDVI VGPTTTEPAF DIGSEISDPI KMYNNDILTI
SANLAGIPAA SVPAGLVDGM PVGLQVMAKR FDEGNVFKTA DFIERTNKFY EKTPTGMED
//
