ID A0A0K9ERS0_9ACTO Unreviewed; 98 AA.
AC A0A0K9ERS0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 49.
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:VDG76947.1};
GN ORFNames=ACU19_09395 {ECO:0000313|EMBL:KMY22561.1}, ACU21_09060
GN {ECO:0000313|EMBL:OCA93873.1}, NCTC10327_01584
GN {ECO:0000313|EMBL:VDG76947.1}, SAMN05421878_1114
GN {ECO:0000313|EMBL:SDE50049.1};
OS Actinobaculum suis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=1657 {ECO:0000313|EMBL:KMY22561.1, ECO:0000313|Proteomes:UP000037036};
RN [1] {ECO:0000313|EMBL:KMY22561.1, ECO:0000313|Proteomes:UP000037036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U311 {ECO:0000313|EMBL:KMY22561.1,
RC ECO:0000313|Proteomes:UP000037036};
RA Moreno L.Z., Amigo C.R., Gobbi D.S., Ferreira T.S., Santos A.P.,
RA Moreno A.M.;
RT "Draft genome sequences of Brazilian Actinobaculum suis isolated from urine
RT and preputial swab.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OCA93873.1, ECO:0000313|Proteomes:UP000093494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C1-9-1 {ECO:0000313|EMBL:OCA93873.1,
RC ECO:0000313|Proteomes:UP000093494};
RA Moreno L.Z., Amigo C.R., Moreno A.M.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000182744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20639 {ECO:0000313|Proteomes:UP000182744};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:SDE50049.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 20639 {ECO:0000313|EMBL:SDE50049.1};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:VDG76947.1, ECO:0000313|Proteomes:UP000269974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10327 {ECO:0000313|EMBL:VDG76947.1,
RC ECO:0000313|Proteomes:UP000269974};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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|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; LFUS01000048; KMY22561.1; -; Genomic_DNA.
DR EMBL; MASY01000039; OCA93873.1; -; Genomic_DNA.
DR EMBL; FNAU01000011; SDE50049.1; -; Genomic_DNA.
DR EMBL; UYIO01000001; VDG76947.1; -; Genomic_DNA.
DR RefSeq; WP_049620467.1; NZ_UYIO01000001.1.
DR AlphaFoldDB; A0A0K9ERS0; -.
DR STRING; 1657.ACU20_03530; -.
DR PATRIC; fig|1657.3.peg.2017; -.
DR OrthoDB; 5295223at2; -.
DR Proteomes; UP000037036; Unassembled WGS sequence.
DR Proteomes; UP000093494; Unassembled WGS sequence.
DR Proteomes; UP000182744; Unassembled WGS sequence.
DR Proteomes; UP000269974; Unassembled WGS sequence.
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:VDG76947.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00122};
KW Reference proteome {ECO:0000313|Proteomes:UP000182744};
KW Transferase {ECO:0000313|EMBL:KMY22561.1}.
SQ SEQUENCE 98 AA; 10510 MW; BC2220A3E5A92EFC CRC64;
MSSFSKERVA HIADLARISL TEDEARQMST ELEAVEEWVK AVSEVAGPDI PGTVNPLPIE
DVTRPDVPGE TLDRDELLAA APAAEDGKFL VPQILGGE
//
