ID GATA_ACIB5 Reviewed; 492 AA.
AC B7I7N2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=AB57_3285;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(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; CP001182; ACJ41864.1; -; Genomic_DNA.
DR RefSeq; WP_000130656.1; NC_011586.2.
DR AlphaFoldDB; B7I7N2; -.
DR SMR; B7I7N2; -.
DR KEGG; abn:AB57_3285; -.
DR HOGENOM; CLU_009600_0_3_6; -.
DR Proteomes; UP000007094; 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..492
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000117601"
FT ACT_SITE 79
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 178
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 492 AA; 53026 MW; 3F73F9087E594F69 CRC64;
MTDLHRLSIR ELAEGLSQAK FSSRELTEHY LKRIAKIDPQ VKSYVTVTPE QALREADAAD
AALKAGNATA LTGIPLAHKD IFCTKGIKTT AGSKMLDNFI SPYDATVVEK TKAAGLVTLG
KVNMDEFAMG STSESSYVGA TSNPWALDHV PGGSSGGSAA AVAADLAPFA TGTDTGGSIR
QPASFCGLTG LKPTYGRVSR FGIIAYASSL DQAGPMARSA EDCAYLMNVI AGHDAKDSTS
VKKELDDYVA NLNNTSVKGL RIGIPKQYFN VAGLDADVKA RVEESLKKLE EMGAALVEID
LNMTEAYVPT YYLIAPAEAS SNLSRYDGVR YGYRCENPAD LMDLYKRSRS EGFGPEVQRR
ILIGTYALSA GYYDAYYVKA QKVRRLIQQD FLKAFENVDV IAAPAAPTTA YKIGASLDPV
EMYLGDIYTI AVNLAGLPAI NAPVGFDKDN LPVGLQLIGN YWSESQLLSI VHQYQQNTDW
HTKRAAIAEE NA
//
