ID A0A3M2VH82_PSESX Unreviewed; 483 AA. AC A0A3M2VH82; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 10-APR-2019, entry version 2. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {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|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 RT 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 CC organisms which lack glutaminyl-tRNA synthetase. The reaction CC takes place in the presence of glutamine and ATP through an CC activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000256|HAMAP- CC Rule:MF_00120}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + CC H(+) + 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 EC=6.3.5.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00120, CC ECO:0000256|SAAS:SAAS01115610}; CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|HAMAP- CC Rule:MF_00120}. CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00120, ECO:0000256|SAAS:SAAS00598568}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Proteomes; UP000272422; Unassembled WGS sequence. DR Gene3D; 3.90.1300.10; -; 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; PTHR11895; 1. DR Pfam; PF01425; Amidase; 1. DR SUPFAM; SSF75304; SSF75304; 1. DR TIGRFAMs; TIGR00132; gatA; 1. DR PROSITE; PS00571; AMIDASES; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00120, KW ECO:0000256|SAAS:SAAS00013898}; KW Complete proteome {ECO:0000313|Proteomes:UP000272422}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00120, KW ECO:0000256|SAAS:SAAS00013917}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00120, KW ECO:0000256|SAAS:SAAS00013943}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00120, KW ECO:0000256|SAAS:SAAS00013924}; KW Transferase {ECO:0000313|EMBL:RML37758.1}. FT DOMAIN 22 463 Amidase. {ECO:0000259|Pfam:PF01425}. FT ACT_SITE 76 76 Charge relay system. {ECO:0000256|HAMAP- FT Rule:MF_00120}. FT ACT_SITE 151 151 Charge relay system. {ECO:0000256|HAMAP- FT Rule:MF_00120}. FT ACT_SITE 175 175 Acyl-ester intermediate. FT {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 //