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Database: UniProt/SWISS-PROT
Entry: GATA_PARPJ
LinkDB: GATA_PARPJ
Original site: GATA_PARPJ 
ID   GATA_PARPJ              Reviewed;         495 AA.
AC   B2T1M4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   18-SEP-2019, entry version 71.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            Short=Glu-ADT subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00120};
GN   Name=gatA {ECO:0000255|HAMAP-Rule:MF_00120};
GN   OrderedLocusNames=Bphyt_0328;
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX   PubMed=21551308; DOI=10.1128/jb.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J.,
RA   Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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). {ECO:0000255|HAMAP-
CC       Rule:MF_00120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP +
CC         H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC         EC=6.3.5.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00120};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00120}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00120}.
DR   EMBL; CP001052; ACD14753.1; -; Genomic_DNA.
DR   RefSeq; WP_012431397.1; NC_010681.1.
DR   SMR; B2T1M4; -.
DR   STRING; 398527.Bphyt_0328; -.
DR   PRIDE; B2T1M4; -.
DR   EnsemblBacteria; ACD14753; ACD14753; Bphyt_0328.
DR   KEGG; bpy:Bphyt_0328; -.
DR   eggNOG; ENOG4105C3P; Bacteria.
DR   eggNOG; COG0154; LUCA.
DR   HOGENOM; HOG000116699; -.
DR   KO; K02433; -.
DR   OMA; MYLSDIF; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000001739; Chromosome 1.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
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; IPR036928; AS_sf.
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    495       Glutamyl-tRNA(Gln) amidotransferase
FT                                subunit A.
FT                                /FTId=PRO_1000095116.
FT   ACT_SITE     75     75       Charge relay system. {ECO:0000255|HAMAP-
FT                                Rule:MF_00120}.
FT   ACT_SITE    150    150       Charge relay system. {ECO:0000255|HAMAP-
FT                                Rule:MF_00120}.
FT   ACT_SITE    174    174       Acyl-ester intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00120}.
SQ   SEQUENCE   495 AA;  52835 MW;  1B4677DC726294EC CRC64;
     MHEKSLTELR AALTAKECSA VELAQLYLKR IDAANSLNAF IQVDPDLTLA QAKAADALLH
     TGHAGPLVGL PIAHKDVFVT KGWRSTAGSK MLSNYESPFD ATVVARLQNA GMVCVGKTNM
     DEFAMGSSNE NSYFGPVQNP WDVKAVPGGS SGGSAAAVAA RLAPAATGTD TGGSIRQPAS
     FSGITGIKPT YGRVSRYGMI AFASSLDQGG PMAQSAADCA TLLNAMAGFD ERDSTSLVRD
     DEDYTRYLGK PWKEESAAKP LAGLRIGLPK EYFGAGLADD VRASVDAALK QYEALGATLV
     DVSLPKTELS IPVYYVIAPA EASSNLSRFD GVRFGHRAAE YRDLLDMYKK SRAEGFGPEV
     KRRILVGAYV LSHGYYDAYY LQAQKIRRII AQDFQEAFKQ CDVIMGPVAP SVAWDLGAKG
     DDPVQMYLAD IYTLSVSLAG LPGMSVPCGF GAGANAQRPV GLQIIGNYFN EARMLQVADA
     FQRATDWHRK APAGV
//
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