ID GATA_GEOUR Reviewed; 485 AA.
AC A5G9J9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 29-MAY-2013, entry version 46.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE Short=Glu-ADT subunit A;
DE EC=6.3.5.-;
GN Name=gatA; OrderedLocusNames=Gura_4324;
OS Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=351605;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rf4;
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., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Shelobolina E., Aklujkar M., Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
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; CP000698; ABQ28467.1; -; Genomic_DNA.
DR RefSeq; YP_001233040.1; NC_009483.1.
DR ProteinModelPortal; A5G9J9; -.
DR SMR; A5G9J9; 1-485.
DR STRING; 351605.Gura_4324; -.
DR EnsemblBacteria; ABQ28467; ABQ28467; Gura_4324.
DR GeneID; 5162797; -.
DR KEGG; gur:Gura_4324; -.
DR PATRIC; 22039120; VBIGeoUra13052_4605.
DR eggNOG; COG0154; -.
DR HOGENOM; HOG000116699; -.
DR KO; K02433; -.
DR OMA; RYDGVKY; -.
DR ProtClustDB; PRK00012; -.
DR BioCyc; GURA351605:GI6A-4380-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 1 485 Glutamyl-tRNA(Gln) amidotransferase
FT subunit A.
FT /FTId=PRO_1000076131.
FT ACT_SITE 78 78 Charge relay system (By similarity).
FT ACT_SITE 153 153 Charge relay system (By similarity).
FT ACT_SITE 177 177 Acyl-ester intermediate (By similarity).
SQ SEQUENCE 485 AA; 52464 MW; 8128ED0853247D01 CRC64;
MELFELTIHE LHDKLKKKEV SSVEATRALL ARIDAVEPRV NAFITVTPEE ALKNAEAADR
RIAAGDMQLL TGIPIALKDI FLTKGVRTTC ASRILDNFIP PYDATSVARL KAQGMVLVGK
LNQDEFAMGS STESSYYGKT HNPWNLECIP GGSSGGSAAA IAARQAIATL GTDTGGSIRQ
PASHCGCVGL KPTYGRVSRY GVIAYASSLD QVGPVTRDVT DCAIMLGAVA GFDPKDSTSV
DLPVPDYSKA LSNDVKGLKI GLPKEYFIAG LDPDVQKTMD AAIETYKGLG AQFVEISLPH
TDYAVATYYL IATAEASSNL ARYDGVRFGH RSSEAQGLID MYRKSRSEGF GEEVKRRIML
GTYALSSGYY DAYYLKAQKV RTLIMQDFSR AFEEVDVILT PVAPTPAFRI GEKSADPLQM
YLSDIFTIPV NLAGTCGMSI PAGFSKDGLP VGLQLVGRPF GEECILRAAY AFEQNTDWHE
RKASL
//
