ID GATE_METVS Reviewed; 633 AA.
AC A6UPR3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=Mevan_0578;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-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; CP000742; ABR54485.1; -; Genomic_DNA.
DR RefSeq; WP_011972388.1; NC_009634.1.
DR AlphaFoldDB; A6UPR3; -.
DR SMR; A6UPR3; -.
DR STRING; 406327.Mevan_0578; -.
DR GeneID; 5326034; -.
DR KEGG; mvn:Mevan_0578; -.
DR eggNOG; arCOG01719; Archaea.
DR HOGENOM; CLU_030702_0_0_2; -.
DR OrthoDB; 7316at2157; -.
DR Proteomes; UP000001107; 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; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 1.10.150.380; GatB domain, N-terminal subdomain; 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 NCBIfam; TIGR00134; gatE_arch; 1.
DR PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1.
DR PANTHER; PTHR11659:SF2; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT E; 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; GAD domain-like; 1.
DR SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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_1000025482"
SQ SEQUENCE 633 AA; 71126 MW; 816DB9B5877FB617 CRC64;
MDYDYEKLGL KVGLEIHQQL NTKRKLFCNC PTKIRDDEPH GEIERFLRPS QSEMGQVDKA
AILESRKEKK FIYQYYNDTT CLVELDDEPP HNVSEEGLNT ALEVSTLMNM NFADEIHVMR
KMVIDGSNTS GFQRTMFVSQ DGFIETEYGK IRITSLCLEE DSCKKVEDGR DYTKYCVDRL
GIPLLEITTE PDITSPKMGK EAARRIGTIL RATGKVKRGL GTIRQDVNIS IKNGARIEVK
GVQNLDLIEK IIENEVTRQV SLNNLKEELI GRNAEVLDEI IDVTELLNDT ESKVLRGALK
NKGVIKAILL KGFSGLIGKE VQPGRRLGTE FSDRGKVLGG VGGLFHTDEL PKYGITDEEV
NKLKKFMNCG ENDAVILVAD AKNKAERALL AVIERAKESL IGIPEETRKA LDDGNTSYLR
PLPGAARMYP ETDVPKILIT SEICERIKNN LPEMPEEKTI RFIKEYELNE DLAKQMVMSY
NVELFENLSK KYPNIKPTLI ATTLEATLKE IKREGLDTEV LTDEHLNELF LGLSEDKMSK
EAIPEVIKGY INNPNMKLDE VLDVAGLSKM SKEEVEAVIL DIINQNILIV NEKGMGATGL
LMGRCMAQLR GKADGKLINV TLQNKLKEKV QGQ
//
