GATE_THEVO
ID GATE_THEVO Reviewed; 598 AA.
AC Q979L9;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=TV1141;
GN ORFNames=TVG1166951;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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; BA000011; BAB60283.1; -; Genomic_DNA.
DR RefSeq; WP_010917375.1; NC_002689.2.
DR AlphaFoldDB; Q979L9; -.
DR SMR; Q979L9; -.
DR STRING; 273116.14325379; -.
DR EnsemblBacteria; BAB60283; BAB60283; BAB60283.
DR GeneID; 1441257; -.
DR KEGG; tvo:TVG1166951; -.
DR eggNOG; arCOG01719; Archaea.
DR HOGENOM; CLU_030702_0_0_2; -.
DR OMA; SGFQRTM; -.
DR OrthoDB; 35861at2157; -.
DR PhylomeDB; Q979L9; -.
DR Proteomes; UP000001017; 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.
FT CHAIN 1..598
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT /id="PRO_0000140085"
SQ SEQUENCE 598 AA; 67355 MW; 6777EB8F039F8CCF CRC64;
MTHRNIKIGL EIHFQLNTGK LFCRCPVETS GTEKYRFERH LHVSESEMGR IDAAAKYESE
RSRTFEYVVT DNSCLVECDE DPPKMPNEDA IATAISVARA LNCDILDYIT YMRKIVIDGS
NTSGFQRTAI IGINGYIETS KGKVRISTVC LEEDAARKIE EKEGTVVYSL DRLGIPLIEI
STEPDIIDEE HAVEVAKKIG YYVISTGKSR KAPDSVRQDV NFSMGFGRVE IKGVSKLSQI
KEVLKYEIQR QDMLKKASDL IKLRGGFDRS RFYFIDVTDL LVNTSSKVVN SGLKTGRAYA
ALCTNLAGTL KSGEYRLGKE LADLVRAYGL KGLLHSDELP GYGLKESDIQ PIYDRLQKDE
LDGVIILLSP QEKIGIIEEE IANRIEKLIS LDLSETRGPT EDSTVFLRPM PGKDRMYPET
DIPVIAVSKD ILQKSDKIKS VGFEDLVSSI ITKYGISKQV AESLASDMKI QELEELSTYL
DPRESARVLT QIIPYLEKKY AKKFDNNLIF VLVRLMSDRK FDRYQVEKAL EILFSENKDP
ALIVSDERLI ELTKDEICEI IDKLKKSGIT ITKANVVSVL KKNTDRIFDP SMAIECLG
