ID GATC_SULDN Reviewed; 96 AA.
AC Q30R53;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 29-MAY-2013, entry version 46.
DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C;
DE Short=Asp/Glu-ADT subunit C;
DE EC=6.3.5.-;
GN Name=gatC; OrderedLocusNames=Suden_1250;
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251)
OS (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Sulfurimonas.
OX NCBI_TaxID=326298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251;
RX PubMed=18065616; DOI=10.1128/AEM.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J.,
RA Hemp J., Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S.,
RA Malfatti S.A., Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K.,
RA Diaz E., Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A.,
RA Long A., Mobberley J.M., Pantry S.N., Pazder G., Peterson S.,
RA Quintanilla J.D., Sprinkle R., Stephens J., Thomas P., Vaughn R.,
RA Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(2008).
CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn)
CC or Gln-tRNA(Gln) through the transamidation of misacylated Asp-
CC tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both
CC of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction
CC takes place in the presence of glutamine and ATP through an
CC activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP
CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits (By similarity).
CC -!- SIMILARITY: Belongs to the GatC family.
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DR EMBL; CP000153; ABB44528.1; -; Genomic_DNA.
DR RefSeq; YP_393763.1; NC_007575.1.
DR ProteinModelPortal; Q30R53; -.
DR STRING; 326298.Suden_1250; -.
DR EnsemblBacteria; ABB44528; ABB44528; Suden_1250.
DR GeneID; 3763710; -.
DR KEGG; tdn:Suden_1250; -.
DR PATRIC; 23771126; VBISulDen68967_1298.
DR eggNOG; COG0721; -.
DR HOGENOM; HOG000017523; -.
DR KO; K02435; -.
DR OMA; LEIKDEH; -.
DR ProtClustDB; PRK00034; -.
DR BioCyc; SDEN326298:GH9P-1298-MONOMER; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:HAMAP.
DR HAMAP; MF_00122; GatC; 1; -.
DR InterPro; IPR003837; Asp/Glu-ADT_csu.
DR Pfam; PF02686; Glu-tRNAGln; 1.
DR TIGRFAMs; TIGR00135; gatC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1 96 Aspartyl/glutamyl-tRNA(Asn/Gln)
FT amidotransferase subunit C.
FT /FTId=PRO_1000016239.
SQ SEQUENCE 96 AA; 10961 MW; D6DBD1E58E3B3693 CRC64;
MQVDDVLLSR LEKLSFLKIS EDKREEIVSQ LSEIVNFVEN LSLLDTQNVD EKFAMSNDST
FLREDTAFCD TSINESILKN APLSSDNFFV VPKIIE
//
