ID GATA_BACLD Reviewed; 485 AA. AC Q65MP8; Q62Y42; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 109. 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}; GN OrderedLocusNames=BLi00731, BL00601; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism RT with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017333; AAU39666.1; -; Genomic_DNA. DR EMBL; CP000002; AAU22316.1; -; Genomic_DNA. DR RefSeq; WP_003179591.1; NC_006322.1. DR AlphaFoldDB; Q65MP8; -. DR SMR; Q65MP8; -. DR STRING; 279010.BL00601; -. DR GeneID; 66217127; -. DR KEGG; bld:BLi00731; -. DR KEGG; bli:BL00601; -. DR eggNOG; COG0154; Bacteria. DR HOGENOM; CLU_009600_0_3_9; -. DR Proteomes; UP000000606; 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; KW Reference proteome. FT CHAIN 1..485 FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A" FT /id="PRO_0000241071" 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 485 AA; 52882 MW; 4D3F944611FFDEE3 CRC64; MSLFDHKISE LKRLIHNKEI SISDLVDESY KRIHEVDGKV QAFLQLDEEK ARAYAKELDE ALDTRDEHGL LFGMPIGIKD NIVTKDLRTT CASKILENFD PIYDATVVER LHEAEAVTIG KLNMDEFAMG SSTENSGFKK TKNPWNLETV PGGSSGGSAA AVAAGEVPFS LGSDTGGSIR QPASFCGVVG LKPTYGRVSR YGLVAFASSL DQIGPITRSV EDNAYLLQAI SGVDKMDSTS ANVDVPDYLS ALTGDIKGLK IAVPKEYLGE GVSEEAKQSV LEALKVLESL GATWEEVSLP HSKYALATYY LLSSSEASAN LARFDGIRYG YRTDNADNLI DLYKQTRSEG FGNEVKRRIM LGTFALSSGY YDAYYKKAQK VRTLIKKDFE DVFANYDVII GPTTPTPAFK IGEKTSDPLT MYANDILTIP VNLAGVPGIS VPCGFANGLP LGLQIIGKHF DESTVYRVAH AFEQATDHHK AKPEL //