ID   D4LFI1_RUMC1            Unreviewed;        92 AA.
AC   D4LFI1;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, C subunit {ECO:0000313|EMBL:CBL18376.1};
DE            EC=6.3.5.6 {ECO:0000313|EMBL:CBL18376.1};
DE            EC=6.3.5.7 {ECO:0000313|EMBL:CBL18376.1};
GN   OrderedLocusNames=RUM_23870 {ECO:0000313|EMBL:CBL18376.1};
OS   Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / KCTC 15320 /
OS   18P13).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL18376.1, ECO:0000313|Proteomes:UP000007054};
RN   [1] {ECO:0000313|Proteomes:UP000007054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18848 / JCM 17042 / 18P13
RC   {ECO:0000313|Proteomes:UP000007054};
RA   Pajon A., Turner K., Parkhill J., Bernalier A.;
RT   "The genome sequence of Ruminococcus sp. 18P13.";
RL   Submitted (MAR-2010) 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:0000256|ARBA:ARBA00024799}.
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:0000256|ARBA:ARBA00000352};
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:0000256|ARBA:ARBA00000924};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC       {ECO:0000256|ARBA:ARBA00011123}.
CC   -!- SIMILARITY: Belongs to the GatC family.
CC       {ECO:0000256|ARBA:ARBA00010757}.
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; FP929052; CBL18376.1; -; Genomic_DNA.
DR   RefSeq; WP_015559282.1; NZ_BBEP01000014.1.
DR   AlphaFoldDB; D4LFI1; -.
DR   STRING; 213810.RUM_23870; -.
DR   GeneID; 83157028; -.
DR   KEGG; rch:RUM_23870; -.
DR   PATRIC; fig|213810.4.peg.2282; -.
DR   HOGENOM; CLU_105899_6_2_9; -.
DR   BioCyc; RCHA213810:RUM_RS11615-MONOMER; -.
DR   Proteomes; UP000007054; Chromosome.
DR   GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR   Gene3D; 1.10.20.60; Glu-tRNAGln amidotransferase C subunit, N-terminal domain; 1.
DR   InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR   InterPro; IPR003837; GatC.
DR   NCBIfam; TIGR00135; gatC; 1.
DR   Pfam; PF02686; GatC; 1.
DR   SUPFAM; SSF141000; Glu-tRNAGln amidotransferase C subunit; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:CBL18376.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007054};
KW   Transferase {ECO:0000313|EMBL:CBL18376.1}.
SQ   SEQUENCE   92 AA;  10745 MW;  8A5E2C34596619BA CRC64;
     MDKTTLAHLC ELSKLDFTEE QQDAVIAQMD DIIALMDQIK EYDVTYDDTQ DHNEIPYQAL
     REDVAQPSYD TARLQQNTQP RDDCYVVPKM ME
//