GATA_RICPU
ID GATA_RICPU Reviewed; 493 AA.
AC C4K0R4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=RPR_01255;
OS Rickettsia peacockii (strain Rustic).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=562019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rustic;
RX PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT with virulent Rickettsia rickettsii: identification of virulence factors.";
RL PLoS ONE 4:E8361-E8361(2009).
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; CP001227; ACR47165.1; -; Genomic_DNA.
DR AlphaFoldDB; C4K0R4; -.
DR SMR; C4K0R4; -.
DR EnsemblBacteria; ACR47165; ACR47165; RPR_01255.
DR KEGG; rpk:RPR_01255; -.
DR HOGENOM; CLU_009600_0_3_5; -.
DR OMA; EVSCPHF; -.
DR Proteomes; UP000005015; 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_1000203043"
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; 53106 MW; 65451420361792B2 CRC64;
MTELNKLTVA DSIKGLKNKD FTSTELIGAH IKQIEKHRNL NAYVTETFDL ALKQAEAADQ
NYAQNNARTL EGIPFAAKDL FCTKGIRTTA CSNILKNFIP NYESSVTQNI FDKGGVMLGK
TNMDEFAMGS ANITSCFGNV ISPWKANDDN ADLVPGGSSG GSAAAVSGFM ASAALGSDTG
GSVRQPASFT GLVGFKPTYG RCSRYGMISF ASSLDQAGIF TRSVLDSSIM LEAMMGFDEK
DSTSIKAEVP ELQSAIGSSM KNMKIGVPLS LGEGSIIEPD IMKMWQDTIE LLKNAGAEIV
DITLPHAKYG VAVYYVIAPA EASSNLSRYD GIRYGLRVER ENMTLDEMYE MTRSTGFGEE
VKRRIMIGTY VLSSSGMDAY YLKAQKVRRL VANDFNNAFA KVDAILLPAA PTAAFKIGEK
QNDPTIMYLN DLFTIPASLA GLPCASVPAG LSARGLPLGI QIIGKQLDEY NVLKVASTIE
SGVKHIKFEP KGF