GATC_ACIET
ID GATC_ACIET Reviewed; 99 AA.
AC B9MB32;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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}; OrderedLocusNames=Dtpsy_0232;
OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Diaphorobacter.
OX NCBI_TaxID=535289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPSY;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT "Complete sequence of Diaphorobacter sp. TPSY.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000255|HAMAP-Rule:MF_00122}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00122};
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 Evidence={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}.
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DR EMBL; CP001392; ACM31716.1; -; Genomic_DNA.
DR RefSeq; WP_012655331.1; NC_011992.1.
DR AlphaFoldDB; B9MB32; -.
DR SMR; B9MB32; -.
DR STRING; 535289.Dtpsy_0232; -.
DR EnsemblBacteria; ACM31716; ACM31716; Dtpsy_0232.
DR KEGG; dia:Dtpsy_0232; -.
DR eggNOG; COG0721; Bacteria.
DR HOGENOM; CLU_105899_2_2_4; -.
DR OMA; VTPMAMK; -.
DR OrthoDB; 1780195at2; -.
DR Proteomes; UP000000450; Chromosome.
DR GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
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:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00122; GatC; 1.
DR InterPro; IPR003837; Asp/Glu-ADT_csu.
DR InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR PANTHER; PTHR15004; PTHR15004; 1.
DR Pfam; PF02686; Glu-tRNAGln; 1.
DR SUPFAM; SSF141000; SSF141000; 1.
DR TIGRFAMs; TIGR00135; gatC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..99
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit C"
FT /id="PRO_1000122566"
SQ SEQUENCE 99 AA; 10912 MW; BE27D0A5D018F22D CRC64;
MALTPQDIGR IANLARLELS PGESERMLTQ LNGFFGIVEK MQAVDTHGIA PLSHPVAVVR
DVQLRLREDV ASEPDQREAN QRSAPAVERG LFLVPKVIE
