GATC_AQUAE
ID GATC_AQUAE Reviewed; 94 AA.
AC O67904;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C;
DE Short=Glu-ADT subunit C;
DE EC=6.3.5.-;
GN Name=gatC; OrderedLocusNames=aq_2149;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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) (By similarity). {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07874.1; -; Genomic_DNA.
DR PIR; D70484; D70484.
DR RefSeq; NP_214473.1; NC_000918.1.
DR RefSeq; WP_010881409.1; NC_000918.1.
DR PDB; 3H0L; X-ray; 2.30 A; C/F/I/L/O/R/U/X=1-94.
DR PDB; 3H0M; X-ray; 2.80 A; C/F/I/L/O/R/U/X=1-94.
DR PDB; 3H0R; X-ray; 3.00 A; C/F/I/L/O/R/U/X=1-94.
DR PDBsum; 3H0L; -.
DR PDBsum; 3H0M; -.
DR PDBsum; 3H0R; -.
DR AlphaFoldDB; O67904; -.
DR SMR; O67904; -.
DR STRING; 224324.2984354; -.
DR EnsemblBacteria; AAC07874; AAC07874; AAC07874.
DR KEGG; aae:aq_2147a; -.
DR PATRIC; fig|224324.8.peg.1661; -.
DR eggNOG; COG0721; Bacteria.
DR HOGENOM; CLU_105899_6_1_0; -.
DR InParanoid; O67904; -.
DR OMA; VTPMAMK; -.
DR OrthoDB; 1780195at2; -.
DR EvolutionaryTrace; O67904; -.
DR Proteomes; UP000000798; 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; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
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 PANTHER; PTHR15004; PTHR15004; 1.
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..94
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C"
FT /id="PRO_0000105271"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 20..36
FT /evidence="ECO:0007829|PDB:3H0L"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3H0L"
SQ SEQUENCE 94 AA; 11215 MW; 3D4E4E712F92E8D0 CRC64;
MVDREWVLKI AKLARLELKE EEIEVFQKQL SDILDFIDQL KELDTENVEP YIQEFEETPM
REDEPHPSLD REKALMNAPE RKDGFFVVPR VVEV
