ID S0AQX4_FERAC Unreviewed; 617 AA.
AC S0AQX4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 ORFNames=FACI_IFERC00001G1638 {ECO:0000313|EMBL:AGO61618.1};
OS Ferroplasma acidarmanus Fer1.
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Ferroplasmaceae; Ferroplasma.
OX NCBI_TaxID=333146 {ECO:0000313|EMBL:AGO61618.1, ECO:0000313|Proteomes:UP000014660};
RN [1] {ECO:0000313|EMBL:AGO61618.1, ECO:0000313|Proteomes:UP000014660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=fer1 {ECO:0000313|Proteomes:UP000014660};
RX PubMed=17267615; DOI=10.1073/pnas.0604851104;
RA Allen E.E., Tyson G.W., Whitaker R.J., Detter J.C., Richardson P.M.,
RA Banfield J.F.;
RT "Genome dynamics in a natural archaeal population.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1883-1888(2007).
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|HAMAP-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; CP004145; AGO61618.1; -; Genomic_DNA.
DR RefSeq; WP_019841736.1; NC_021592.1.
DR AlphaFoldDB; S0AQX4; -.
DR GeneID; 16025824; -.
DR KEGG; fac:FACI_IFERC01G1638; -.
DR PATRIC; fig|333146.12.peg.1667; -.
DR HOGENOM; CLU_030702_0_0_2; -.
DR Proteomes; UP000014660; 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; 3.30.1360.30; GAD-like domain; 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; IPR004115; GAD-like_sf.
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; PF02934; GatB_N; 1.
DR SUPFAM; SSF55261; GAD domain-like; 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:UP000014660}.
FT DOMAIN 1..426
FT /note="Aspartyl/Glutamyl-tRNA(Gln) amidotransferase subunit
FT B/E catalytic"
FT /evidence="ECO:0000259|Pfam:PF02934"
SQ SEQUENCE 617 AA; 69447 MW; 267229AC9026BBF3 CRC64;
MKIGLEIHFQ LGGNKLFCSC STEGTELNES FTRKLTPVMG ELGKLDTAVE YETIRNRNFL
YRASSNSCLV EKDEEPPHPV NPDALKTTIA ISKALHCKVL DYTSFMRKIV VDGSNTSGFQ
RTGIVGMDGY VKTSRGNVRI STITLEEDAC RKLSEKEGVV EYSLDRLGIP LIEISTEPDI
IDPDHALETA KAIGHYVMSM QNFRGEVDSI RQDVNFSMGF GRVEIKGVSK LSFIKDTIEY
EIKRQSSLEA ISRILAEKPH EIGNFIDITG MFTNTDSSMI KKSIASGKSV MCARVSACNG
LMKHGNYKLG REFADVAKNM GLGGLMHSDE FPAYGLSDEE LHSIYSTAGK GDNDAVIVVL
GEKSRIEKLK PLLDERFDKI LKMQLEETRS ATPSGETRYL RPLAGKERMY PETDIPAVKI
TEAIMESIEK LVPKSLEETM NELTKKFKLS QVEAESLINN NLLSLFKALA GNFDNPHILS
RILLQTIPEL ENKKGKKLSQ VQMVDIFGNQ YLEARQLPQY HNTDSILELS RREKWDRNTF
ETALSLYIID NIPVSELEKR EELKMLNDNE IKKILDELVK DGNVTQKNVI PLFRGKTKQS
FNPSDVIKIF VTMQNQK
//
