ID   GATE_SULIN              Reviewed;         633 AA.
AC   C3NHQ1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=YN1551_1573;
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001404; ACP48661.1; -; Genomic_DNA.
DR   RefSeq; WP_012711296.1; NC_012623.1.
DR   AlphaFoldDB; C3NHQ1; -.
DR   SMR; C3NHQ1; -.
DR   EnsemblBacteria; ACP48661; ACP48661; YN1551_1573.
DR   GeneID; 7809166; -.
DR   GeneID; 7941021; -.
DR   GeneID; 8761219; -.
DR   KEGG; sin:YN1551_1573; -.
DR   HOGENOM; CLU_030702_0_0_2; -.
DR   OMA; SGFQRTM; -.
DR   Proteomes; UP000006818; 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; 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.
FT   CHAIN           1..633
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT                   /id="PRO_1000212160"
SQ   SEQUENCE   633 AA;  71528 MW;  9CFE6D53D8077CE7 CRC64;
     MSELNYEELG LKVGLEIHQQ LNTSHKLFCN CSTNLKEDYK LTLERYLRPA LSELGEVDVA
     ALFEWKKGKK YVYRIPITTS CLVEADEEPP HAINEEALKI ALAIAIALNS NIVDEIYVMR
     KIVIDGSNTT GFQRTAIVAL GGMLKDEGVT IQTIAVEEDA ARKIDERTDQ VTYSLDRLGI
     PLIEISTGPD IRSPEQAERV ALKIGQLLRM TGKVKRGIGT IRQDLNISIK GGTKIEIKGV
     QKLELIPDIV RYEAMRQFNL LKIKEELNKR GVSKNLILSN FVVKDLTELF KNTNSKIIKS
     GIEKGGLVYG IRAYKLKGIL GWELIPKKRR FGTEIADYVR ALAELGGLFH SDELPNYGIT
     EEEINKVREA LNATTEDGFI LIVGERERLD KAVEVIRDRI LLAFDGIPKE TRGALDDGTT
     KFLRPQPSSA RMYPETDIPP RRIDEKLLED AKKFVPESPE SKMKRYITLG LSEELAKEII
     RDPRLDLFEE LVNKYSPKVS PVVIASTITN TLKYVKSKGG DISKINEEDI EELIKSVYEN
     KISKDSISEI LLEYTTNKNV ELKDVIRKYE ALPTEELEKI IDDVISSNLD EIRKRKDKAV
     NLIMSKVMSK VKGRAEGKVI LELIKSRLKN VME