GATE_PYRAR
ID GATE_PYRAR Reviewed; 608 AA.
AC A4WKM4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Pars_1379;
OS Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=340102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL Submitted (APR-2007) 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; CP000660; ABP50941.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WKM4; -.
DR SMR; A4WKM4; -.
DR STRING; 340102.Pars_1379; -.
DR EnsemblBacteria; ABP50941; ABP50941; Pars_1379.
DR KEGG; pas:Pars_1379; -.
DR HOGENOM; CLU_030702_0_0_2; -.
DR OMA; SGFQRTM; -.
DR PhylomeDB; A4WKM4; -.
DR Proteomes; UP000001567; 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..608
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT /id="PRO_1000025483"
FT REGION 401..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 67666 MW; C566705D142B9CE9 CRC64;
MDYKALGLKT GLEIHIQLNT RRKLFCHCPP VLRDDEPHFR VERRLHISVS ELGAVDPAVV
WEVRKRRKYI YEGYRDTTCL VELDEEPPHM PDEEALTTAV AVAKMFNAKL FDEIYVMRKT
VVDGSNVSGF QRTMLVAYGG RAKILGYDIG VETIALEEDA ARKMGEEGKA VVYRLDRLGI
PLIEIATEPM TYAPQQVEEV AWIIGYSVKI TGRAKRGVGT VRQDVNVSIA GGAKTEIKGV
PDLSLIPKVI EYEATRQLSL LKIAEELKRR GVEKVELSLA DVTQAFANTK SKLVRRVLDA
GGKVVAVKAP GFNKLLGAEV QPGRRFGTEL ADYVRAWTEL GGLLHSDELP GYGITADEVR
DVEARVGVNS FILLMGVDEG ELEEAARVVV ERLNAAPRGV PEETRAANPD GTTRFLRPRP
GAARMYPETD LPPVRITFEI LKKAEEVAKV TLEGKLKELT SRGLSRDLAL QLVKSPHLEK
FEDYLQRFKE VPPQQIAAVL LNISKALARE GVEITDEKVE SVLDALNRKV ITKEAVEEVL
RNMKPGESAE EAAKRLGLLR MSYDEVKKIV AEVAAQVGKE KAVGEVMRRY RGKVDVEDVR
RALAEIYL