ID   GATE_HALSA              Reviewed;         622 AA.
AC   Q9HQ32;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=VNG_1352G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(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; AE004437; AAG19685.1; -; Genomic_DNA.
DR   PIR; A84290; A84290.
DR   RefSeq; WP_010902981.1; NC_002607.1.
DR   AlphaFoldDB; Q9HQ32; -.
DR   SMR; Q9HQ32; -.
DR   STRING; 64091.VNG_1352G; -.
DR   PaxDb; Q9HQ32; -.
DR   EnsemblBacteria; AAG19685; AAG19685; VNG_1352G.
DR   GeneID; 5954373; -.
DR   KEGG; hal:VNG_1352G; -.
DR   PATRIC; fig|64091.14.peg.1033; -.
DR   HOGENOM; CLU_030702_0_0_2; -.
DR   InParanoid; Q9HQ32; -.
DR   OMA; SGFQRTM; -.
DR   OrthoDB; 35861at2157; -.
DR   PhylomeDB; Q9HQ32; -.
DR   Proteomes; UP000000554; 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..622
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT                   /id="PRO_0000140070"
SQ   SEQUENCE   622 AA;  66826 MW;  779D19183DE56EBE CRC64;
     MTEFDYDELG LVAGLEIHQQ LDTATKLFCA CPTTRREPAE ADRTFTRYLH PTRSELGEID
     EAALEESRVE REFEYLAYDT TCLVEEDDEP PHRLDEDALA AALEIGHLLG MDAVDRAHVM
     RKVVIDGSNT GGFQRSTMVA EGGAIDTSEG PVGIEDLMLE EESAQRIEDR EDGVLYSLDR
     LGIPLVEIGT KPDISSPAQA REAAERIGML LRSTGKVKRG LGTIRQDVNV SIADGARVEM
     KGVQSLDDID DLVREEVRRQ VELLDIVDEL DARDAAVGKP RDVTDVFADT ESGVIRGALD
     DGGEVHAVPL HGFDGLVGRE LQADRRLGTE FSDHATRHGA GGIFHTDELP AYGVTAAEVA
     ALRDAVGAGE DDAVAIVADD PETAAQSIQA VAERAETAMA GVPEETRGAN DDGTSKYLRP
     LPGAARMYPE TDVPPVDPDP SAVETPELLT EKVERYQADF DLDAGLAEQV AYGRRWQLFE
     QQVEAGVDAT LAAQTLESTV TELRRDDVPV GRLTDAHFRG VLGLVADGDL AQEGVPELLA
     ALAEQPGSDP AVLAEELGLG SAAEDEVREA VVGVVERNSD QVAAEGMGAF SALMGECMGA
     LRGKADGDLV SEVLREEIQQ RS