ID A0A1J1ABQ3_9EURY Unreviewed; 622 AA.
AC A0A1J1ABQ3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit E {ECO:0000256|HAMAP-Rule:MF_00588};
DE Short=Glu-ADT subunit E {ECO:0000256|HAMAP-Rule:MF_00588};
DE EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_00588};
GN Name=gatE {ECO:0000256|HAMAP-Rule:MF_00588,
GN ECO:0000313|EMBL:APE95562.1};
GN ORFNames=HSR6_1113 {ECO:0000313|EMBL:APE95562.1};
OS Halodesulfurarchaeum formicicum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halodesulfurarchaeum.
OX NCBI_TaxID=1873524 {ECO:0000313|EMBL:APE95562.1, ECO:0000313|Proteomes:UP000186165};
RN [1] {ECO:0000313|Proteomes:UP000186165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSR6 {ECO:0000313|Proteomes:UP000186165};
RA Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA Golyshin P.N., Rojo D., Ciordia S., Mena Md.C., Ferrer M., Smedile F.,
RA Messina E., La Cono V., Yakimov M.M.;
RT "Discovery of first anaerobic lithoheterotrophic haloarchae widely
RT represented in hypersaline habitats.";
RL Submitted (AUG-2016) 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:0000256|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:0000256|ARBA:ARBA00000924, ECO:0000256|HAMAP-
CC Rule:MF_00588};
CC -!- SUBUNIT: Heterodimer of GatD and GatE. {ECO:0000256|HAMAP-
CC Rule:MF_00588}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatE subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00588}.
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DR EMBL; CP016804; APE95562.1; -; Genomic_DNA.
DR RefSeq; WP_071933067.1; NZ_CP016804.1.
DR AlphaFoldDB; A0A1J1ABQ3; -.
DR GeneID; 30417637; -.
DR KEGG; hhsr:HSR6_1113; -.
DR OrthoDB; 7316at2157; -.
DR Proteomes; UP000186165; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00588};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00588};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00588};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00588}; Reference proteome {ECO:0000313|Proteomes:UP000186165};
KW Transferase {ECO:0000313|EMBL:APE95562.1}.
FT DOMAIN 477..618
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
FT REGION 405..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 66952 MW; 9EF785318BCFE6A2 CRC64;
MTEFDYEELG LVAGLEIHQQ LDTETKLFCN CPTTQREAAE SVRSFTRYLH PTPSELGEVD
EAALEESQVE REFEYLGYDS TCLVEEDDEP PHPMDDEALE LSLEIAQLLS MTPVDQAHVM
RKVVIDGSNT SGFQRTSLIA TDGEIQTEAG PVGIEDLMLE EESARRVEET DSGVVFSLDR
LGVPLVEIGT EPDITSPKQA REAAGRLGMI LRSTGSVKRG LGTIRQDVNV SIEEGARVEV
KGVQDLEGIE NIVRGEVRRQ AELLEISEEL QDRNAAVGDV QAVSDVFADT DSGVIRGALD
AGGAVKAVPL FGFDGLVGRE IQPDRRLGTE LSDHAKRHGA GGIFHTDELP AYGVTEEEVV
ALRDAVDAGE EDAVAIVAAD TETAELAIEA AADRAAVAIE GVPEETRDAN EDGTTSYLRP
LPGAARMYPE TDVPPVDIDP AAVETPELLD EKVDRYVEAY DLDPGLAEQV AFGRRFTTFE
QAVEQGVDPA LAATTVESTS TELRRDDVPV ENLTDEHFLD VLEQVDAGDL AKEGVGEVLT
VLAEQPELSA ATAIEEAGLG AVDEAAVREA VREVVERNAS QVEDEGMEAF SALMGEAMGA
LRGKADGEVV SSVLREEIQA KL
//
