GATA_RICCK
ID GATA_RICCK Reviewed; 493 AA.
AC A8EXM1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
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}; OrderedLocusNames=A1E_00780;
OS Rickettsia canadensis (strain McKiel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=293613;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=McKiel;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia canadensis.";
RL Submitted (SEP-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 organisms
CC which lack glutaminyl-tRNA synthetase. The reaction takes place in the
CC presence of glutamine and ATP through an activated gamma-phospho-Glu-
CC tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_00120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC 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; EC=6.3.5.7;
CC 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}.
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DR EMBL; CP000409; ABV73104.1; -; Genomic_DNA.
DR RefSeq; WP_012148305.1; NC_009879.1.
DR AlphaFoldDB; A8EXM1; -.
DR SMR; A8EXM1; -.
DR STRING; 293613.A1E_00780; -.
DR EnsemblBacteria; ABV73104; ABV73104; A1E_00780.
DR KEGG; rcm:A1E_00780; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_5; -.
DR OMA; EVSCPHF; -.
DR OrthoDB; 1239251at2; -.
DR Proteomes; UP000007056; Chromosome.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; 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; Ligase; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..493
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000015899"
FT ACT_SITE 78
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 182
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 493 AA; 53207 MW; 7197130A3AC7319B CRC64;
MTELNKLTLA DSIKGLKNKD FTSTELVNAH IQQIEKHKNL NAYVTKTFDL ALKGAQIADQ
NYAQNKARTL EGIPFAAKDL FCTKGIRTTA CSNILKNFIP NYESSVTQNI FNNGGVMLGK
TNMDEFAMGA ANITSCFGNV INPWKANNDN SDLVPGGSSG GSAASVSGFM ASAALGSDTG
GSVRQPASFT GLVGFKPTYG RCSRYGMVSF ASSLDQAGIF TRSVLDSAIM LEAMMGFDEK
DSTSLKAEVP QLQSAIGSSV KNMKIGVPLS LGEGSIIEPD VMKMWQDTIE LLKNAGTEIV
DITLPYAKYG VAVYYVIAPA EASSNLSRYD GVRYGLRVER ENMTLDEMYE MTRSAGFGEE
VKRRIMIGTY VLSSSCMDAY YLKAQKVRSL VANDFNNAFT KVDTILLPAA PSEAFKIGEK
QNDPTIMYLN DLFTIPASLA GLPCVSVPAG LSARGLPLGM QIIGKQLDEY NVLKVASTIE
SGVKHIKFEP KGF