GATA_RICPR
ID GATA_RICPR Reviewed; 493 AA.
AC Q9ZE10;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=RP152;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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) (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ235270; CAA14620.1; -; Genomic_DNA.
DR PIR; E71725; E71725.
DR RefSeq; NP_220543.1; NC_000963.1.
DR RefSeq; WP_004597217.1; NC_000963.1.
DR AlphaFoldDB; Q9ZE10; -.
DR SMR; Q9ZE10; -.
DR STRING; 272947.RP152; -.
DR EnsemblBacteria; CAA14620; CAA14620; CAA14620.
DR GeneID; 57569281; -.
DR KEGG; rpr:RP152; -.
DR PATRIC; fig|272947.5.peg.157; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_5; -.
DR OMA; EVSCPHF; -.
DR Proteomes; UP000002480; 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;
KW Reference proteome.
FT CHAIN 1..493
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000105197"
FT ACT_SITE 78
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 182
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 493 AA; 53259 MW; 885F71DA7A49DF0D CRC64;
MTELNKLTVA ESVKGLKNKD FTSKELVNAY IKQIEKYKNL NAYVTETFDL ALKQAEAADQ
NYGQNKARTL EGIPFAVKDL FCTKGIRTTA CSNILKNFIP HYESSVTQNI FDKGGVILGK
TNMDEFAMGS ANITSCFGNV ISPWKANDDN SDLVPGGSSG GSAAAVSAFM ASAALGSDTG
GSVRQPASFT GLVGFKPTYG RCSRYGMVSF ASSLDQAGIF TRSVLDSSIM LEAMMGFDEK
DSTSINAQVP ELQSAIGSSM KNMKIGVPLS LGEGGIIEHD IMKMWHDTIE LLKNAGAEIV
DITLPHAKYG VAVYYVIAPA EAASNLSRYD GVRYGLRVEC ENMTLDEMYE MTRSAGFGEE
VKRRIMLGTY VLSSHCMDAY YFKAQKVRRL VANDFNNAFA KVNAILLPTA PSAAFKIGKK
QNDPTIMYLN DLFTIPASLA GLPCASVPAG LSARGLPLGM QIIGKQLDEY NVLKVASTIE
TGVKHIKFEP AGF