GATC_THET8
ID GATC_THET8 Reviewed; 89 AA.
AC Q9LCX4; Q5SJX6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C;
DE Short=Glu-ADT subunit C;
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00122};
GN Name=gatC {ECO:0000255|HAMAP-Rule:MF_00122}; OrderedLocusNames=TTHA0876;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10913601; DOI=10.1016/s0014-5793(00)01697-5;
RA Becker H.D., Min B., Jacobi C., Raczniak G., Pelaschier J., Roy H.,
RA Klein S., Kern D., Soell D.;
RT "The heterotrimeric Thermus thermophilus Asp-tRNA(Asn) amidotransferase can
RT also generate Gln-tRNA(Gln).";
RL FEBS Lett. 476:140-144(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00122};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_00122}.
CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC Rule:MF_00122}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD70699.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF202446; AAF91175.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70699.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_024119135.1; NC_006461.1.
DR RefSeq; YP_144142.1; NC_006461.1.
DR PDB; 3KFU; X-ray; 3.00 A; G/J=1-89.
DR PDBsum; 3KFU; -.
DR AlphaFoldDB; Q9LCX4; -.
DR SMR; Q9LCX4; -.
DR STRING; 300852.55772258; -.
DR EnsemblBacteria; BAD70699; BAD70699; BAD70699.
DR GeneID; 3168271; -.
DR KEGG; ttj:TTHA0876; -.
DR PATRIC; fig|300852.9.peg.869; -.
DR eggNOG; COG0721; Bacteria.
DR HOGENOM; CLU_105899_1_1_0; -.
DR OMA; ELVNVMR; -.
DR EvolutionaryTrace; Q9LCX4; -.
DR Proteomes; UP000000532; 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:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00122; GatC; 1.
DR InterPro; IPR003837; Asp/Glu-ADT_csu.
DR InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR Pfam; PF02686; Glu-tRNAGln; 1.
DR SUPFAM; SSF141000; SSF141000; 1.
DR TIGRFAMs; TIGR00135; gatC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..89
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C"
FT /id="PRO_0000105353"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 21..39
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:3KFU"
SQ SEQUENCE 89 AA; 9957 MW; DDD291293407C8ED CRC64;
MELSPELLRK LETLAKIRLS PEEEALLLQD LKRILDFVDA LPRVEEGGAE EALGRLREDE
PRPSLPQAEA LALAPEAEDG FFRVPPVLE
