ID GATA_PSELT Reviewed; 467 AA.
AC A8F5H6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=Tlet_0844;
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=416591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-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; CP000812; ABV33410.1; -; Genomic_DNA.
DR AlphaFoldDB; A8F5H6; -.
DR SMR; A8F5H6; -.
DR STRING; 416591.Tlet_0844; -.
DR KEGG; tle:Tlet_0844; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_0; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000002016; 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:SF151; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A; 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..467
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000076147"
FT ACT_SITE 57
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 156
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 467 AA; 51152 MW; E59127AB0BAA755E CRC64;
MFEKMTIEDC LSKESDLINL SLERIKCIDS AVKSFITVVD KQEELEGPYK GIPIAIKDNI
TTKNIRTTCG SKMLENYTPP YDATCVKRLK NYGFAIVGKT NLDEFAMGSS TERSAFFVTR
NPWDLDYVAG GSSGGSAAAV ASGEVVAALG SDTGGSVRQP AAFCGIVGFK PTYGLVSRYG
LVAFASSLDQ IGPMTKSVRD AALIMEVIAG KDPMDSTTVS KKLDFLTHIE DGISGMKFAV
PEEVYKYEQL DREVSDRFEE ALKTAEKLGA KVSRVKIPTI KYAVATYYII APAEASSNLA
RYDGVKYGLR IEEPGLMDTY MKTRNVGFGE EVRRRIFLGT FTLSAAYYEA YFGKAQKVRK
LLSDDLNRVL ADFDAILTPT SPSPAFKIGS VADPLTYYLM DIFTIPANLS GLPAISVPFG
FAKNLPVGLQ IMGRRFDDPK VLAIARAFEK YSPYNINGRI PLPVVRI
//
