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Database: UniProt/SWISS-PROT
Entry: GATA_PSEP1
LinkDB: GATA_PSEP1
Original site: GATA_PSEP1 
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   19-MAR-2014, entry version 44.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE            Short=Glu-ADT subunit A;
DE            EC=6.3.5.7;
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; FGYRCEN; -.
DR   OrthoDB; EOG61P6R9; -.
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:UniProtKB-HAMAP.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-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; SSF75304; 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
//
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