ID   GATE_SULTO              Reviewed;         628 AA.
AC   Q971W7;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=STK_12620;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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; BA000023; BAB66303.1; -; Genomic_DNA.
DR   RefSeq; WP_010979281.1; NC_003106.2.
DR   AlphaFoldDB; Q971W7; -.
DR   SMR; Q971W7; -.
DR   STRING; 273063.STK_12620; -.
DR   EnsemblBacteria; BAB66303; BAB66303; STK_12620.
DR   GeneID; 1459261; -.
DR   KEGG; sto:STK_12620; -.
DR   PATRIC; fig|273063.9.peg.1420; -.
DR   eggNOG; arCOG01719; Archaea.
DR   OMA; SGFQRTM; -.
DR   OrthoDB; 35861at2157; -.
DR   Proteomes; UP000001015; 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;
KW   Reference proteome.
FT   CHAIN           1..628
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT                   /id="PRO_0000140083"
SQ   SEQUENCE   628 AA;  71366 MW;  8F4F687A586195ED CRC64;
     MTELDYSKIG LKVGLEIHQQ LNTAHKLFCE CPTTLHEEYH TQLERYLRPS FSELGEIDIA
     ALFEWQKGKK YVYRVPPNSC LVECDEEPPH IIDEEALSIA VAVSLALHST LVDEVYVMRK
     IVIDGSNTSG FQRTAIISLG GYIEDNGQRI GIQTIALEED AARKITDSPT EIIYNLDRLG
     IPLIEISTAP DIKTPEQAER VALKIGQLLR LTGRVKRGIG TIRQDLNVSI QGGVKTEIKG
     VQLLELIPDI IKNEARRQYE LLRIKEELQK RNLNKDIVKN SFKIVDLTEE FKDTNSKIIR
     KELEKNGRIY GLKIAGFKGI FGWQLMPNRR FGTEVADYVR ALAGLGGLFH SDELPNYGIT
     KEEVEKVRKI LQINENDAFI IIVGPKEKLD IATNTILDRI LYAFDGVPKE TRAALDDGTT
     KFMRPQPGSA RMYPETDIPP RRIDERILEL SKQFVPEQPE IKLKKLIELG LSKDLANTML
     NSLRLDLFEE LVKKYSPKVS PTFIASTLEI TVKYVKSKGG DISVITDNIL EELIKYVYED
     KISKDAVQEI LLELATSKTQ LNEIIKKYTP LNETELEKII IETIEENKKE IENKKDKAFN
     IIMSKVMNKV RGRADSKKVI ELIKKHLG