ID   GATC_PSEPG              Reviewed;          95 AA.
AC   B0KQG1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=PputGB1_0939;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) 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; CP000926; ABY96849.1; -; Genomic_DNA.
DR   RefSeq; WP_003255165.1; NC_010322.1.
DR   AlphaFoldDB; B0KQG1; -.
DR   SMR; B0KQG1; -.
DR   STRING; 76869.PputGB1_0939; -.
DR   EnsemblBacteria; ABY96849; ABY96849; PputGB1_0939.
DR   GeneID; 58529330; -.
DR   GeneID; 61772612; -.
DR   GeneID; 66676487; -.
DR   KEGG; ppg:PputGB1_0939; -.
DR   eggNOG; COG0721; Bacteria.
DR   HOGENOM; CLU_105899_2_2_6; -.
DR   OMA; VTPMAMK; -.
DR   Proteomes; UP000002157; 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..95
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit C"
FT                   /id="PRO_1000076191"
SQ   SEQUENCE   95 AA;  10392 MW;  97B7F2D6F77DF0A4 CRC64;
     MALERCDVEK IAHLARLGLN DGELPRITDA LNSILGLVDQ MQAVDTTGIE PLAHPLEASQ
     RLRPDQVTES NQRDAYQAIA PSTESGLYLV PKVIE