ID A0A3M2VH82_PSESX Unreviewed; 483 AA. AC A0A3M2VH82; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 22-FEB-2023, entry version 11. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000256|ARBA:ARBA00014428, ECO:0000256|HAMAP-Rule:MF_00120}; DE Short=Glu-ADT subunit A {ECO:0000256|HAMAP-Rule:MF_00120}; DE EC=6.3.5.7 {ECO:0000256|ARBA:ARBA00012739, ECO:0000256|HAMAP-Rule:MF_00120}; GN Name=gatA {ECO:0000256|HAMAP-Rule:MF_00120}; GN ORFNames=ALQ96_03387 {ECO:0000313|EMBL:RML37758.1}; OS Pseudomonas syringae pv. atrofaciens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=192087 {ECO:0000313|EMBL:RML37758.1, ECO:0000313|Proteomes:UP000272422}; RN [1] {ECO:0000313|EMBL:RML37758.1, ECO:0000313|Proteomes:UP000272422} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5025 {ECO:0000313|EMBL:RML37758.1, RC ECO:0000313|Proteomes:UP000272422}; RA Dillon M., Thakur S., Almeida R.N.D., Weir B.S., Guttman D.S.; RT "Recombination of ecologically and evolutionarily significant loci RT maintains genetic cohesion in the Pseudomonas syringae species complex."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|ARBA:ARBA00001243, ECO:0000256|HAMAP- CC Rule:MF_00120}; CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. CC {ECO:0000256|ARBA:ARBA00011123, ECO:0000256|HAMAP-Rule:MF_00120}. CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily. CC {ECO:0000256|ARBA:ARBA00008069, ECO:0000256|HAMAP-Rule:MF_00120}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RML37758.1}. 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; RBNQ01000022; RML37758.1; -; Genomic_DNA. DR RefSeq; WP_004416170.1; NZ_RBNQ01000022.1. DR AlphaFoldDB; A0A3M2VH82; -. DR EnsemblBacteria; RML37758; RML37758; ALQ96_03387. DR Proteomes; UP000272422; Unassembled WGS sequence. 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:0016740; F:transferase activity; IEA:UniProtKB-KW. 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 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 TIGRFAMs; TIGR00132; gatA; 1. DR PROSITE; PS00571; AMIDASES; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00120}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00120}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00120}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00120}; Transferase {ECO:0000313|EMBL:RML37758.1}. FT DOMAIN 22..463 FT /note="Amidase" FT /evidence="ECO:0000259|Pfam:PF01425" FT ACT_SITE 76 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120" FT ACT_SITE 151 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120" FT ACT_SITE 175 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120" SQ SEQUENCE 483 AA; 51854 MW; BD2397C78EC63A2F CRC64; MHQMTLAEIA RGLADKKFSS EELTRVLLSR IATLDPQLNS FISLTEDLAI TQAQAADARR AAGENGPLLG APLAHKDLFC TQGIRTSCGS LMLDNFKAPY DATVVSRLAS AGTVTLGKTN MDEFAMGSAN ESSHYGAVKN PWNLECVPGG SSGGSAAAVA ARLLPAATGT DTGGSIRQPA ALTNLTGLKP TYGRVSRWGM IAYASSLDQA GPMARTAEDC ALLLQGMAGF DPQDSTSIDE PVPDYSASLN TSLKGLRIGV PKEYFSAGLD PRIAQLVHES VKELEKLGAI VKEVSLPNLQ HAIPAYYVIA PAEASSNLSR FDGVRFGYRC EDPKDLTDLY KRSRAEGFGP EVQRRIMVGA YALSAGYYDA YYLQAQKIRR LIKNDFMSAF VDVDVILGPT TPNPAWKIGA KTNDPIAEYL EDFYTTTANL AGLPGLSMPA GFVDGLPVGV QLLAPYFQEG RLLNVAHQYQ QVTDWHTRAP EGF //