GATE_THEAC
ID GATE_THEAC Reviewed; 603 AA.
AC Q9HJJ6;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit E {ECO:0000255|HAMAP-Rule:MF_00588};
DE Short=Glu-ADT subunit E {ECO:0000255|HAMAP-Rule:MF_00588};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00588};
GN Name=gatE {ECO:0000255|HAMAP-Rule:MF_00588}; OrderedLocusNames=Ta0971;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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). The GatDE system is specific for glutamate and does not act
CC on aspartate. {ECO:0000255|HAMAP-Rule:MF_00588}.
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00588};
CC -!- SUBUNIT: Heterodimer of GatD and GatE. {ECO:0000255|HAMAP-
CC Rule:MF_00588}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00588}.
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DR EMBL; AL445066; CAC12100.1; -; Genomic_DNA.
DR RefSeq; WP_010901382.1; NC_002578.1.
DR AlphaFoldDB; Q9HJJ6; -.
DR SMR; Q9HJJ6; -.
DR STRING; 273075.Ta0971; -.
DR PRIDE; Q9HJJ6; -.
DR EnsemblBacteria; CAC12100; CAC12100; CAC12100.
DR GeneID; 1456498; -.
DR KEGG; tac:Ta0971; -.
DR eggNOG; arCOG01719; Archaea.
DR HOGENOM; CLU_030702_0_0_2; -.
DR OMA; SGFQRTM; -.
DR OrthoDB; 35861at2157; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; 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; 3.30.1360.30; -; 1.
DR HAMAP; MF_00588; GatE; 1.
DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR004414; GatE.
DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11659; PTHR11659; 1.
DR PANTHER; PTHR11659:SF2; PTHR11659:SF2; 1.
DR Pfam; PF02934; GatB_N; 1.
DR SUPFAM; SSF55261; SSF55261; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR00134; gatE_arch; 1.
DR PROSITE; PS01234; GATB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..603
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT /id="PRO_0000140084"
SQ SEQUENCE 603 AA; 67704 MW; 0854A5BA15728FA6 CRC64;
MDTKIGLEVH FQLNTGKLFC RCPVEQSSGE LMRFSRKLHI SASELGNIDA AASYESMRSR
SFQYVVTDNS CLVEMDEEPP KTPDERAIAT AISVSKALNC DIVDHITYMR KIVIDGSNTT
GFQRTAIVGI NGHIETSKGP VRISTVCLEE DAARKIEEIG NTVVYSLDRL GIPLIEISTE
PDIVDEDHAV EVARSIGYIV ISTGNARHAV DAVRQDVNFS MGYGRVEIKG VSKLTQIRDV
IRYEKERQEN LRAAVDLIKS RGGLDRVSFN LKDVSDLFAG TKSKIIRSGI ESGGVYAGIL
KNMAGTLKNG KLRMGKEIAD LVRSYGIKGV MHSDELPGYG LTQDEVEALY RYLGKGDNDA
VLLIAINQSR VKMIENSIFD RIQKIISMDL SETRGPAGEE TVFLRPMPGK DRMYPETDIP
VIKVDSKLME MSSSIKPRTY AEVVQDLVDR YGISKQNAEY IASEMVVDAF RNIAEFVEAR
EAARILTQIV PDLERRTKKI IDHDRIIELC RRSKDLHFDR YQLEMALEIL YERDDVASVL
GDSRLKELSR EEIKSIIREI LSSGRNATQN SIIALIKEKT ERVFDPRVAM ECFNEVKNKN
NVF
