ID GATC_OPITP Reviewed; 94 AA. AC B1ZQN2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 01-APR-2015, entry version 46. DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C {ECO:0000255|HAMAP-Rule:MF_00122}; DE Short=Asp/Glu-ADT subunit C {ECO:0000255|HAMAP-Rule:MF_00122}; DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00122}; GN Name=gatC {ECO:0000255|HAMAP-Rule:MF_00122}; GN OrderedLocusNames=Oter_2359; OS Opitutus terrae (strain DSM 11246 / PB90-1). OC Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae; OC Opitutus. OX NCBI_TaxID=452637; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11246 / PB90-1; RX PubMed=21398538; DOI=10.1128/JB.00228-11; RA van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A., RA Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., RA Schmutz J., Larimer F.W., Land M.L., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.; RT "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an RT abundant inhabitant of rice paddy soil ecosystems."; RL J. Bacteriol. 193:2367-2368(2011). CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) CC or Gln-tRNA(Gln) through the transamidation of misacylated Asp- CC tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both CC of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction CC takes place in the presence of glutamine and ATP through an CC activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). CC {ECO:0000255|HAMAP-Rule:MF_00122}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00122}. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00122}. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP- CC Rule:MF_00122}. CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP- CC Rule:MF_00122}. 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; CP001032; ACB75641.1; -; Genomic_DNA. DR RefSeq; WP_012375178.1; NC_010571.1. DR RefSeq; YP_001819241.1; NC_010571.1. DR STRING; 452637.Oter_2359; -. DR EnsemblBacteria; ACB75641; ACB75641; Oter_2359. DR GeneID; 6206477; -. DR KEGG; ote:Oter_2359; -. DR PATRIC; 22816373; VBIOpiTer17422_2461. DR eggNOG; COG0721; -. DR HOGENOM; HOG000017523; -. DR KO; K02435; -. DR OMA; KFREDEV; -. DR OrthoDB; EOG61S35Z; -. DR BioCyc; OTER452637:GHBR-2410-MONOMER; -. DR Proteomes; UP000007013; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00122; GatC; 1. DR InterPro; IPR003837; Asp/Glu-ADT_csu. DR Pfam; PF02686; Glu-tRNAGln; 1. DR TIGRFAMs; TIGR00135; gatC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 94 Aspartyl/glutamyl-tRNA(Asn/Gln) FT amidotransferase subunit C. FT /FTId=PRO_1000122578. SQ SEQUENCE 94 AA; 10051 MW; 5E9479420C801673 CRC64; MATDLNIDHV ANLARLALTP EEKATFAQQL GDVLHHIEQL AKVDVAGVEP TAHAFAVTNV WADDAPQPGL SVEAALKNAP AQREHMVVVP KVVE //