ID GATC_NEIMB Reviewed; 96 AA.
AC Q9JZ00;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 107.
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=NMB1355;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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}.
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DR EMBL; AE002098; AAF41729.1; -; Genomic_DNA.
DR PIR; D81091; D81091.
DR RefSeq; NP_274373.1; NC_003112.2.
DR RefSeq; WP_002219137.1; NC_003112.2.
DR AlphaFoldDB; Q9JZ00; -.
DR SMR; Q9JZ00; -.
DR STRING; 122586.NMB1355; -.
DR PaxDb; 122586-NMB1355; -.
DR KEGG; nme:NMB1355; -.
DR PATRIC; fig|122586.8.peg.1695; -.
DR HOGENOM; CLU_105899_2_2_4; -.
DR InParanoid; Q9JZ00; -.
DR OrthoDB; 9794326at2; -.
DR Proteomes; UP000000425; 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 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; Ligase; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..96
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C"
FT /id="PRO_0000105315"
SQ SEQUENCE 96 AA; 10958 MW; EECAEC185A42D335 CRC64;
MALTLADVDK IARLSRLHLT AEEKEKSLQE LNDIFTMVEQ MQTINTDGIE PMAHPHEAAL
RLREDEVTET DRAAEYQAGA PEVRNRLYIV PQVIEE
//
