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Database: UniProt/SWISS-PROT
Entry: GATC_SULDN
LinkDB: GATC_SULDN
Original site: GATC_SULDN 
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   19-FEB-2014, entry version 49.
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   OrthoDB; EOG625K3N; -.
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:UniProtKB-HAMAP.
DR   GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-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
//
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