ID GATE_METBF Reviewed; 633 AA.
AC Q469Y2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
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=Mbar_A2389;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ71310.1; -; Genomic_DNA.
DR AlphaFoldDB; Q469Y2; -.
DR SMR; Q469Y2; -.
DR STRING; 269797.Mbar_A2389; -.
DR PaxDb; 269797-Mbar_A2389; -.
DR KEGG; mba:Mbar_A2389; -.
DR eggNOG; arCOG01719; Archaea.
DR HOGENOM; CLU_030702_0_0_2; -.
DR OrthoDB; 7316at2157; -.
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_1000025477"
SQ SEQUENCE 633 AA; 70820 MW; A828830043B34553 CRC64;
MEKYDYSELG LKAGLEIHQQ LDSKEKLFCR CPTLIRDVKE SDFEFFRYLR ATESEMGEKD
RAAVEQTKIR RKYIYKAYDT TCLIENDEEP PRELNKEALD ISLGIAKLFN MKPVDQMHVM
RKIVVDGSNT SGFQRTAFLA SDGFIETSQG LCGIDSLCVE EEAAQKIEEI GDSIIYSLDR
LGIPLVEIAT APDIKSPRHA REVAEQIGMF LRSTGKVKRG LGTIRQDVNV SIAEGARVEI
KGVQALDLIE DIIRREVERQ LNLLFIRQEL IERKAFVCEE IYDITGLFVD TKSKVLQKGV
KKGAVLAAHL KKFEGLVGKE VQPGRRLGTE FSDRAKTAGV GGIFHTDELP NYGITEKEVK
TVRDAIGASA GDAVIMVADE PEKARLAIEA VIQRAKEAME GIPEETRKAL PDGNTAYMRP
LPGAARMYPE TDVPQIEISQ EYFDSIEIPE LLTERAKRFV SENGLNQELA EKIAYSKHLP
LFEELIETYG KDENVNSTLI ARTLVGIVPE IRRNGVETEN LTDEHFKGLF VAISNQEIAK
EAIQDLLAAL AEEPELSTPE AISNLGLSAF DPEEVENFIK KTVREREDFI KEKGPAALGP
LMGIVMKEYR GTVDGKILSQ MLKKELDSFI NQG
//
