ID G2KN47_MICAA Unreviewed; 95 AA.
AC G2KN47;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 ECO:0000313|EMBL:AEP09380.1};
GN OrderedLocusNames=MICA_1052 {ECO:0000313|EMBL:AEP09380.1};
OS Micavibrio aeruginosavorus (strain ARL-13).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Micavibrio.
OX NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP09380.1, ECO:0000313|Proteomes:UP000009286};
RN [1] {ECO:0000313|EMBL:AEP09380.1, ECO:0000313|Proteomes:UP000009286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARL-13 {ECO:0000313|EMBL:AEP09380.1,
RC ECO:0000313|Proteomes:UP000009286};
RX PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA Wang Z., Kadouri D., Wu M.;
RT "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT aeruginosavorus ARL-13.";
RL BMC Genomics 12:453-453(2011).
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}.
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DR EMBL; CP002382; AEP09380.1; -; Genomic_DNA.
DR RefSeq; WP_014102603.1; NC_016026.1.
DR AlphaFoldDB; G2KN47; -.
DR STRING; 856793.MICA_1052; -.
DR KEGG; mai:MICA_1052; -.
DR eggNOG; COG0721; Bacteria.
DR HOGENOM; CLU_105899_6_1_5; -.
DR OrthoDB; 9794326at2; -.
DR Proteomes; UP000009286; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:AEP09380.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00122};
KW Reference proteome {ECO:0000313|Proteomes:UP000009286};
KW Transferase {ECO:0000313|EMBL:AEP09380.1}.
SQ SEQUENCE 95 AA; 10241 MW; E0F33517C719E798 CRC64;
MSMDKATVKK VATLARLAIT EEQADKLAPQ LGGLLKWVEQ LGEVNTDNVA PLASVVNMEM
ELRADKVTDG DIQSDVLANA PEAMEGFFVV PKVVE
//
