ID F4DR72_PSEMN Unreviewed; 95 AA.
AC F4DR72;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 03-APR-2013, entry version 14.
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=MDS_0943;
OS Pseudomonas mendocina (strain NK-01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1001585;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NK-01;
RX PubMed=21551299; DOI=10.1128/JB.05068-11;
RA Guo W., Wang Y., Song C., Yang C., Li Q., Li B., Su W., Sun X.,
RA Song D., Yang X., Wang S.;
RT "Complete genome of Pseudomonas mendocina NK-01, which synthesizes
RT medium-chain-length polyhydroxyalkanoates and alginate
RT oligosaccharides.";
RL J. Bacteriol. 193:3413-3414(2011).
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-aspartyl-tRNA(Asn) + L-glutamine = ADP
CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC + phosphate + L-glutaminyl-tRNA(Gln) + 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; CP002620; AEB56974.1; -; Genomic_DNA.
DR RefSeq; YP_004378726.1; NC_015410.1.
DR EnsemblBacteria; AEB56974; AEB56974; MDS_0943.
DR GeneID; 10455725; -.
DR KEGG; pmk:MDS_0943; -.
DR PATRIC; 54482440; VBIPseMen187712_0962.
DR KO; K02435; -.
DR BioCyc; PMEN1001585:GIWS-949-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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; Transferase.
SQ SEQUENCE 95 AA; 10425 MW; BFB0F93002C9A5FF CRC64;
MALERSEVEK IAHLARLGLN EGDIPQTTET LNNILGLIDQ MQAVDTQGIE PLAHPLEATQ
RLRADVVNES NHRDAYQAIA PAVESGLYLV PKVIE
//
