ID GATA_PROMP Reviewed; 484 AA. AC Q7V1D0; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 24-JAN-2024, entry version 99. 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=PMM0946; OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / OS MED4). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=59919; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1986 / NIES-2087 / MED4; RX PubMed=12917642; DOI=10.1038/nature01947; RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C., RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., RA Chisholm S.W.; RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche RT differentiation."; RL Nature 424:1042-1047(2003). 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; BX548174; CAE19405.1; -; Genomic_DNA. DR RefSeq; WP_011132579.1; NC_005072.1. DR AlphaFoldDB; Q7V1D0; -. DR SMR; Q7V1D0; -. DR STRING; 59919.PMM0946; -. DR KEGG; pmm:PMM0946; -. DR eggNOG; COG0154; Bacteria. DR HOGENOM; CLU_009600_0_3_3; -. DR OMA; EVSCPHF; -. DR OrthoDB; 9811471at2; -. DR Proteomes; UP000001026; 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..484 FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A" FT /id="PRO_0000105188" FT ACT_SITE 74 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120" FT ACT_SITE 149 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120" FT ACT_SITE 173 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120" SQ SEQUENCE 484 AA; 52186 MW; 1A473E5882F6FE6F CRC64; MNFNSFRKEI YSGNASVKEL VNEFFLKIDS LNPKINAYTC LTKKIANSQS ENIDKLITNN QKLPSLAGIP IAIKDNICTK GVVTSCSSKM LKDFVSPYES SASGKLWSLG GICLGKTNLD EFAMGSSTET SVFGTTSNPW DVNRVPGGSS GGSAASVAAG LCLAAIGSDT GGSIRQPASF CGVVGLKPTY GRVSRWGLIA FASSLDQIGP ITNTVSDAAE ILYSISGKDN LDSTCLDKPV PNYLSDLDKS IKGIKIGIIE ECFDHPGLDP EVKESVLSSV ERFRSLGAEI HDIKCPRFND GIATYYVIAP CEASANLARY DGVKYGYRSE GESNLLEMIC KSRAEGFGDE VQRRILIGTY ALSAGYSDAY YKKAQRVRTL IRSDFDNAFN EVDVLLTPTC PTTAFLKGDF VNDPLSMYLS DLLTVPVNLA GLPAISIPCG FDKKGLPIGL QLIGNVLEEH RILNVANIFE KDAEVMNTKP NIEI //