ID K9SF57_9CYAN Unreviewed; 96 AA.
AC K9SF57;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=Pse7367_0505 {ECO:0000313|EMBL:AFY68813.1};
OS Pseudanabaena sp. PCC 7367.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY68813.1, ECO:0000313|Proteomes:UP000010386};
RN [1] {ECO:0000313|EMBL:AFY68813.1, ECO:0000313|Proteomes:UP000010386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY68813.1,
RC ECO:0000313|Proteomes:UP000010386};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL Submitted (MAY-2012) 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; CP003592; AFY68813.1; -; Genomic_DNA.
DR RefSeq; WP_015163787.1; NC_019701.1.
DR AlphaFoldDB; K9SF57; -.
DR STRING; 82654.Pse7367_0505; -.
DR KEGG; pseu:Pse7367_0505; -.
DR PATRIC; fig|82654.3.peg.578; -.
DR eggNOG; COG0721; Bacteria.
DR HOGENOM; CLU_105899_2_0_3; -.
DR OrthoDB; 9813938at2; -.
DR Proteomes; UP000010386; 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:AFY68813.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00122};
KW Reference proteome {ECO:0000313|Proteomes:UP000010386};
KW Transferase {ECO:0000313|EMBL:AFY68813.1}.
SQ SEQUENCE 96 AA; 10856 MW; A5BEF6B4CE297C38 CRC64;
MIDRQQVQHV AHLARLQLSE AEESKFTQQL GDILDYFDQL NELDPLLEGV EPTLRAIANV
NVTRPDAKIP SLDREGVLES APAREDEFFQ VPQIMG
//
