GATE_PYRIL
ID GATE_PYRIL Reviewed; 607 AA.
AC A1RRJ9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=Pisl_0403;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000504; ABL87581.1; -; Genomic_DNA.
DR RefSeq; WP_011762158.1; NC_008701.1.
DR AlphaFoldDB; A1RRJ9; -.
DR SMR; A1RRJ9; -.
DR STRING; 384616.Pisl_0403; -.
DR PRIDE; A1RRJ9; -.
DR EnsemblBacteria; ABL87581; ABL87581; Pisl_0403.
DR GeneID; 4618288; -.
DR KEGG; pis:Pisl_0403; -.
DR eggNOG; arCOG01719; Archaea.
DR HOGENOM; CLU_030702_0_0_2; -.
DR OMA; SGFQRTM; -.
DR OrthoDB; 35861at2157; -.
DR Proteomes; UP000002595; 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; 1.10.150.380; -; 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; 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..607
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT /id="PRO_1000025485"
SQ SEQUENCE 607 AA; 68083 MW; B736E2B6F055CD08 CRC64;
MDYRSLGLKV GLEIHIQLNT KRKLFCHCPP VLRDDEPHFR IERRLHLSVS ELGAVDPAVL
WEVRKRRRYI YEGYRDTTCL VELDEEPPHL PDEEALATAV AVAKMFNAKI FDEIHVMRKI
VIDGSNVSGF QRTMLIAYGG KKKILGYDIG VETIALEEDA ARKIAEEGKT VVYRLDRLGI
PLIEIATEPM SYPPQQVEEV AWIIGYSVKI TGRAKRGLGT VRQDVNVSIA GGAKTEIKGV
PDLSLIPKVI EYEVQRQLSL LKISEELRRR GVGKLELSTV DVTQVFTNTK SKIVKRVLET
GGKVVAVKTP GFQKIFGVEV QPGRRFGTEL ADYVRAWTEL GGLLHSDELP GYGITAEEVR
DIISKLGVES FILLMGVDDR ELEEAATVVV DRLNTALQGV PEETRGANPD GTTRFLRPRP
GAARMYPETD IPPIRITFEI LKKSEEIAKV SLEGKLSELT SLGLSKDLAL QLIKSPYLEK
FEDYVSKYKV PPQQIATILL NISRALAREG VEITDEKIAS VLEALEKKII TKEAVEEVLR
NMKAGESAEE VAKRLGLVRM SYEEVKKVVG EVVREVGKDR ALGEVMRRYR GRIDVEDVRR
ALSELYF