AC MF_00121; DC Protein; auto c? or TR HAMAP; MF_00121; -; 1; level=0 XX Names: GatB XX ID GATB DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; DE Short=Asp/Glu-ADT subunit B; DE EC=6.3.5.-; GN Name=gatB; XX CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or CC Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) CC or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- CC tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the CC presence of glutamine and ATP through an activated phospho-Asp- CC tRNA(Asn) or phospho-Glu-tRNA(Gln). 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; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) CC + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate; CC Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216; CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily. XX DR Pfam; PF02934; GatB_N; 1; trigger=no DR Pfam; PF02637; GatB_Yqey; 1; trigger=no DR NCBIfam; TIGR00133; GatB; 1; trigger=no DR PROSITE; PS01234; GATB; 1; trigger=no XX KW ATP-binding KW Ligase KW Nucleotide-binding KW Protein biosynthesis XX GO GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity GO GO:0006412; P:translation XX FT None XX Size: 449-517; Related: MF_00588; Template: O30509; Q9LCX2; O27341; Scope: Bacteria Archaea Fusion: Nter: MF_00126 (glnS) Cter: None Duplicate: in SYNAS Plasmid: None Comments: None XX # Revision 1.28 2023/06/01 //