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Database: UniProt
Entry: U4T680_9GAMM
LinkDB: U4T680_9GAMM
Original site: U4T680_9GAMM 
ID   U4T680_9GAMM            Unreviewed;       104 AA.
AC   U4T680;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=M917_0698 {ECO:0000313|EMBL:ERL56420.1};
OS   Psychrobacter aquaticus CMS 56.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=1354303 {ECO:0000313|EMBL:ERL56420.1, ECO:0000313|Proteomes:UP000016761};
RN   [1] {ECO:0000313|EMBL:ERL56420.1, ECO:0000313|Proteomes:UP000016761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMS 56 {ECO:0000313|EMBL:ERL56420.1,
RC   ECO:0000313|Proteomes:UP000016761};
RX   PubMed=24201199;
RA   Reddy G.S., Ara S., Singh A., Kumar Pinnaka A., Shivaji S.;
RT   "Draft Genome Sequence of Psychrobacter aquaticus Strain CMS 56T, Isolated
RT   from a Cyanobacterial Mat Sample Collected from Water Bodies in the McMurdo
RT   Dry Valley Region of Antarctica.";
RL   Genome Announc. 1:e00918-13(2013).
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:ERL56420.1}.
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DR   EMBL; AUSW01000014; ERL56420.1; -; Genomic_DNA.
DR   RefSeq; WP_021813361.1; NZ_AUSW01000014.1.
DR   AlphaFoldDB; U4T680; -.
DR   STRING; 1354303.M917_0698; -.
DR   PATRIC; fig|1354303.4.peg.687; -.
DR   eggNOG; COG0721; Bacteria.
DR   OrthoDB; 9794326at2; -.
DR   Proteomes; UP000016761; 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: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:ERL56420.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Transferase {ECO:0000313|EMBL:ERL56420.1}.
SQ   SEQUENCE   104 AA;  11401 MW;  E34D552FF80EB15E CRC64;
     MSQQPATSDN TVSREEILEV ANLARLGVDE STADSYAGDI SKVLKLMHTL SNVDTTDIKP
     LANIHEACQE LRTDVANHDI NRERNQSVAP AVEDGLYLVP QVIE
//
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