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Database: UniProt
Entry: A0A1F8FTS0_9BACT
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ID   A0A1F8FTS0_9BACT        Unreviewed;       100 AA.
AC   A0A1F8FTS0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C {ECO:0000256|HAMAP-Rule:MF_00122};
DE            Short=Asp/Glu-ADT subunit C {ECO:0000256|HAMAP-Rule:MF_00122};
DE            EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_00122};
GN   Name=gatC {ECO:0000256|HAMAP-Rule:MF_00122};
GN   ORFNames=A3C88_01695 {ECO:0000313|EMBL:OGN16574.1};
OS   Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_02_FULL_50_12.
OC   Bacteria; Candidatus Yanofskybacteria.
OX   NCBI_TaxID=1802685 {ECO:0000313|EMBL:OGN16574.1, ECO:0000313|Proteomes:UP000178117};
RN   [1] {ECO:0000313|EMBL:OGN16574.1, ECO:0000313|Proteomes:UP000178117}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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|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:0000256|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:0000256|HAMAP-Rule:MF_00122};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_00122}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00122}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGN16574.1}.
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DR   EMBL; MGJZ01000029; OGN16574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8FTS0; -.
DR   STRING; 1802685.A3C88_01695; -.
DR   Proteomes; UP000178117; Unassembled WGS sequence.
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   Gene3D; 1.10.20.60; Glu-tRNAGln amidotransferase C subunit, N-terminal domain; 1.
DR   HAMAP; MF_00122; GatC; 1.
DR   InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR   InterPro; IPR003837; GatC.
DR   NCBIfam; TIGR00135; gatC; 1.
DR   PANTHER; PTHR15004:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR15004; UNCHARACTERIZED; 1.
DR   Pfam; PF02686; GatC; 1.
DR   SUPFAM; SSF141000; Glu-tRNAGln amidotransferase C subunit; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00122}.
SQ   SEQUENCE   100 AA;  11336 MW;  40C72D108651E3F1 CRC64;
     MLTDAEVEKI AALARLTLKD DEKERLKKDM SSILDYVETL NKVDTSGVEP LYQTTGLVNA
     TRTDEPRNEF PMSEKLNELL IGQAPQTKDR FIKVPSILKK
//
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