ID   GATE_THEKO              Reviewed;         629 AA.
AC   Q5JI74;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=TK0911;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD85100.1; -; Genomic_DNA.
DR   RefSeq; WP_011249862.1; NC_006624.1.
DR   AlphaFoldDB; Q5JI74; -.
DR   SMR; Q5JI74; -.
DR   STRING; 69014.TK0911; -.
DR   EnsemblBacteria; BAD85100; BAD85100; TK0911.
DR   GeneID; 3235000; -.
DR   KEGG; tko:TK0911; -.
DR   PATRIC; fig|69014.16.peg.890; -.
DR   eggNOG; arCOG01719; Archaea.
DR   HOGENOM; CLU_030702_0_0_2; -.
DR   InParanoid; Q5JI74; -.
DR   OMA; SGFQRTM; -.
DR   OrthoDB; 35861at2157; -.
DR   PhylomeDB; Q5JI74; -.
DR   Proteomes; UP000000536; 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; IBA:GO_Central.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.410; -; 1.
DR   Gene3D; 1.10.150.380; -; 1.
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; IPR018027; Asn/Gln_amidotransferase.
DR   InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR029351; GAD_dom.
DR   InterPro; IPR042114; GatB_C_1.
DR   InterPro; IPR023168; GatB_Yqey_C_2.
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; PF02938; GAD; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF55261; SSF55261; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   SUPFAM; SSF89095; SSF89095; 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..629
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT                   /id="PRO_0000140080"
SQ   SEQUENCE   629 AA;  71154 MW;  A0DEC9D2F38F8804 CRC64;
     MTDKFNYEEL GLKVGLEIHR QLDTKKLFSP VPSELSDEVD FTFERRLRPT MSELGEIDPA
     ALEEFKKGRK YIYEGNYRLT DLVYMDEEPP RGPDREALEV ALQIGYLLNA KPVDEVHFMR
     KIVIDGSNVS GFQRTAIVAV NGKVDTPWGS VGIPTVCLEE DACRIVERKE KEVIYRIDRL
     GIPLVEISTT PDIHHPEQAK VVAKYIGDAL RATRKVKRGL GTIRQDLNVS IRGGARVEIK
     GVQELDMIPL IIEREVERQL NLLRIRDELK RRGVKPEDIK EEFYDVTEIF QNTGSKIIAR
     AIKSGGKVLA VKLPKFRGLI GKEIQPGRRL GTEMADRAKK YVRGIFHIDE LPNYGITELE
     VNAVIEKLGL GEEDAFVLVA AEEETAKNAL REVIKRAREA IEGVPEETRR ALPDGNTQYM
     RPLPGKARMY PETDIPSIFL PPEEKERIRA NLPELPQERV ERYVKEYKID RSLAETLVND
     ERDELFEELV EKGVKPSLAA SILVVVLKGL KKEVPVENIT DGHIMEAFQL YLEGKIAKEA
     FEEIFKELAL HPEKTAKQVA EEKGLTLLSE EEVEKIIDEV IQQNIEVIKA KGMGAMGMIM
     GRAMAKLRGR ADGKLVSSLV RKKIQEIAG