ID GATA_METJA Reviewed; 434 AA.
AC Q58560;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 110.
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=MJ1160;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB99163.1; -; Genomic_DNA.
DR PIR; G64444; G64444.
DR RefSeq; WP_010870673.1; NC_000909.1.
DR AlphaFoldDB; Q58560; -.
DR SMR; Q58560; -.
DR STRING; 243232.MJ_1160; -.
DR PaxDb; 243232-MJ_1160; -.
DR EnsemblBacteria; AAB99163; AAB99163; MJ_1160.
DR GeneID; 1452058; -.
DR KEGG; mja:MJ_1160; -.
DR eggNOG; arCOG01717; Archaea.
DR HOGENOM; CLU_009600_0_3_2; -.
DR InParanoid; Q58560; -.
DR OrthoDB; 7931at2157; -.
DR PhylomeDB; Q58560; -.
DR Proteomes; UP000000805; 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; Amidase signature (AS) domain; 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 NCBIfam; TIGR00132; gatA; 1.
DR PANTHER; PTHR11895:SF7; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 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..434
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000105233"
FT ACT_SITE 57
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 48008 MW; 0A95BF0C62161F5F CRC64;
MIVERVEEYL DRIEKINKDI NALIEVKPEK VLEEAKKLEK DEKAKKKPLY GKIIVVKANI
NVEGYTISCA SKTLENYIAP YDATVIEKIK ENGGLIIGIA NMDEFACGSS GETSYFGPTK
NPRAKDRIPG GSSSGSAAAV SADLCDMALG SDTGGSIRNP ASHCGVVGFK PSYGVVSRYG
LCDLAMSFDQ IGPLTKTAED ALLLTNIIKG KDLRDTTTVE TKPFEKKDIK GFKVGVVKEF
MDVADEKIRD KVEKAIEVFK DLGCEIVELS YKYVDLALPT YYLINYVEFF SSTRRYDGRR
YGYKIEEVCG EEVLRRIMIG SMISQKEYSG KYYKNALKAR NLMRNEMIKI MKDVDIIVGA
TVPKLPHKLG EKLTPMEMYS YDVLTVPANI CGLCAGVVPC GDINGIPVGL QIQGKPFEDE
KVLSAMIAFE KAME
//
