ID D5VL46_CAUST Unreviewed; 490 AA.
AC D5VL46;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 01-MAY-2013, entry version 22.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE Short=Glu-ADT subunit A;
DE EC=6.3.5.-;
GN Name=gatA; OrderedLocusNames=Cseg_2771;
OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC
OS 15250 / LMG 17158 / TK0059) (Mycoplana segnis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=509190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 /
RC TK0059;
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse
RT alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(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) (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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP002008; ADG11219.1; -; Genomic_DNA.
DR RefSeq; YP_003593837.1; NC_014100.1.
DR EnsemblBacteria; ADG11219; ADG11219; Cseg_2771.
DR GeneID; 9104282; -.
DR KEGG; cse:Cseg_2771; -.
DR PATRIC; 37205642; VBICauSeg118057_2818.
DR HOGENOM; HOG000116699; -.
DR KO; K02433; -.
DR OMA; RYDGVKY; -.
DR BioCyc; CSEG509190:GHVG-2809-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: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; Transferase.
FT ACT_SITE 78 78 Charge relay system (By similarity).
FT ACT_SITE 158 158 Charge relay system (By similarity).
FT ACT_SITE 182 182 Acyl-ester intermediate (By similarity).
SQ SEQUENCE 490 AA; 51898 MW; 7361B821044AA265 CRC64;
MSALTKLTLK AAVDGLAKGE FTSVELTKAH IDAVEAARGL NAYILETPEK ALDMAAKSDA
RRAQGQAGPL EGAPLGVKDL FCTEGVRTTA CSKILENFVP TYESTVTSQL WRDGAVMLGK
LNLDQFAMGS SNETSYFGPV TNPWRVQGSN KALTPGGSSG GSAAAVAADL CLGATATDTG
GSIRQPAAFT GTVGIKPTYG RCSRWGVVAF ASSLDQAGPI AKTVEDAALL LTSMSGHDPK
DSTSLDVPVP DFTQFVGKSV KGLRIGVPKE YRVDGMPAEI EKLWQDGIAW LKEAGCEIVD
ISLPHTKYAL PAYYIVAPAE ASSNLARYDG MRYGLREDGA NLTEIYENTR AAGFGDEVKR
RILIGTYVLS AGYYDAYYLK ALKVRRRIAE DFDNAWEKVD AILTPTAPSA AFGLGENSND
PIAMYLNDVF TVTTNLAGLP GLSLPAGLDA NGLPLGLQII GKPLDEGTVF SVAGALEKAA
GFKAKAEKWW
//
