ID   GATC_SYNWW              Reviewed;          94 AA.
AC   Q0AZZ3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Swol_0372;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI67711.1; -; Genomic_DNA.
DR   RefSeq; WP_011639819.1; NC_008346.1.
DR   AlphaFoldDB; Q0AZZ3; -.
DR   SMR; Q0AZZ3; -.
DR   STRING; 335541.Swol_0372; -.
DR   EnsemblBacteria; ABI67711; ABI67711; Swol_0372.
DR   KEGG; swo:Swol_0372; -.
DR   eggNOG; COG0721; Bacteria.
DR   HOGENOM; CLU_105899_6_1_9; -.
DR   OMA; VTPMAMK; -.
DR   OrthoDB; 1780195at2; -.
DR   Proteomes; UP000001968; 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;
KW   Reference proteome.
FT   CHAIN           1..94
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit C"
FT                   /id="PRO_1000076202"
SQ   SEQUENCE   94 AA;  10510 MW;  02CDB41DD114396A CRC64;
     MALSPEEVNH VAMLARLALS EDEKTAFAEQ LTLILDYVER LNELDTGEVE PLIHILPVFN
     VLRQDEALPG SSQEEILSNA PLVEDGQYKV PRII