ID A0A1R1E997_9BACL Unreviewed; 95 AA.
AC A0A1R1E997;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=BK138_31445 {ECO:0000313|EMBL:OMF48292.1}, FHS19_006666
GN {ECO:0000313|EMBL:MBB3131940.1};
OS Paenibacillus rhizosphaerae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=297318 {ECO:0000313|EMBL:OMF48292.1, ECO:0000313|Proteomes:UP000187172};
RN [1] {ECO:0000313|EMBL:OMF48292.1, ECO:0000313|Proteomes:UP000187172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0378 {ECO:0000313|EMBL:OMF48292.1,
RC ECO:0000313|Proteomes:UP000187172};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3131940.1, ECO:0000313|Proteomes:UP000517523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5831 {ECO:0000313|EMBL:MBB3131940.1,
RC ECO:0000313|Proteomes:UP000517523};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) 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 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|ARBA:ARBA00000352, ECO:0000256|HAMAP-
CC 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|ARBA:ARBA00000924, ECO:0000256|HAMAP-
CC Rule:MF_00122};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC {ECO:0000256|ARBA:ARBA00011123, ECO:0000256|HAMAP-Rule:MF_00122}.
CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000256|ARBA:ARBA00010757,
CC ECO:0000256|HAMAP-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:OMF48292.1}.
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DR EMBL; JACHXJ010000009; MBB3131940.1; -; Genomic_DNA.
DR EMBL; MRTP01000017; OMF48292.1; -; Genomic_DNA.
DR RefSeq; WP_076176038.1; NZ_MRTP01000017.1.
DR AlphaFoldDB; A0A1R1E997; -.
DR STRING; 297318.BK138_31445; -.
DR Proteomes; UP000187172; Unassembled WGS sequence.
DR Proteomes; UP000517523; 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|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00122};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00122};
KW Reference proteome {ECO:0000313|Proteomes:UP000187172};
KW Transferase {ECO:0000313|EMBL:OMF48292.1}.
SQ SEQUENCE 95 AA; 10716 MW; 093A0184C9FA9215 CRC64;
MSITNQDVQH VAKLARLNFT PEEEQMLTEQ LNAILQYAEK LNELDTDGVE PTTHVLHLSN
VMREDEAKDS LPIEKVMANA PEEEDGQFKV PAVLD
//
