ID GATA_PSEP1 Reviewed; 483 AA.
AC A5VZ22;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 29-MAY-2013, entry version 40.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE Short=Glu-ADT subunit A;
DE EC=6.3.5.-;
GN Name=gatA; OrderedLocusNames=Pput_0971;
OS Pseudomonas putida (strain F1 / ATCC 700007).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F1 / ATCC 700007;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Parales R.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in
CC organisms which lack glutaminyl-tRNA synthetase. The reaction
CC takes place in the presence of glutamine and ATP through an
CC activated gamma-phospho-Glu-tRNA(Gln) (By similarity).
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 amidase family. GatA subfamily.
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DR EMBL; CP000712; ABQ77132.1; -; Genomic_DNA.
DR RefSeq; YP_001266316.1; NC_009512.1.
DR ProteinModelPortal; A5VZ22; -.
DR STRING; 351746.Pput_0971; -.
DR EnsemblBacteria; ABQ77132; ABQ77132; Pput_0971.
DR GeneID; 5192698; -.
DR KEGG; ppf:Pput_0971; -.
DR PATRIC; 19917951; VBIPsePut56420_0974.
DR eggNOG; COG0154; -.
DR HOGENOM; HOG000116699; -.
DR KO; K02433; -.
DR OMA; RYDGVKY; -.
DR ProtClustDB; PRK00012; -.
DR BioCyc; PPUT351746:GI26-999-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:0006412; P:translation; IEA:HAMAP.
DR Gene3D; 3.90.1300.10; -; 1.
DR HAMAP; MF_00120; GatA; 1; -.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR004412; GatA.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase_sig_enz; 1.
DR TIGRFAMs; TIGR00132; gatA; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1 483 Glutamyl-tRNA(Gln) amidotransferase
FT subunit A.
FT /FTId=PRO_1000015889.
FT ACT_SITE 76 76 Charge relay system (By similarity).
FT ACT_SITE 151 151 Charge relay system (By similarity).
FT ACT_SITE 175 175 Acyl-ester intermediate (By similarity).
SQ SEQUENCE 483 AA; 51531 MW; A715AD24E4FB7FF4 CRC64;
MHQLTLAEIA RGLADKSFSS EELTGALLAR IKQLDPQINS FISITDDLAL AQARAADARR
AAGETGVLLG APIAHKDLFC TNGVRTSCGS KMLDNFKAPY DATVVAKLAE AGMVTLGKTN
MDEFAMGSAN ESSHYGAVKN PWNLEHVPGG SSGGSAAAVA ARLLPATTGT DTGGSIRQPA
ALTNLTGLKP TYGRVSRWGM IAYASSLDQG GPLARTAEDC ALLLQGMAGF DAKDSTSIEE
PVPDYSASLN ASLQGLRIGL PKEYFGAGLD PRIADLVQAS VKELEKLGAV VKEISLPNMQ
HAIPAYYVIA PAEASSNLSR FDGVRFGYRC EEPKDLTDLY KRSRGEGFGV EVQRRIMVGT
YALSAGYYDA YYVKAQQIRR LIKNDFMAAF NDVDLILGPT TPNPAWKLGA KSSDPVAAYL
EDVYTITANL AGLPGLSMPA GFVDGLPVGV QLLAPYFQEG RLLNVAHRYQ QVTDWHTRAP
NGF
//
