ID A0A365TBT5_9EURY Unreviewed; 622 AA.
AC A0A365TBT5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=DMJ13_14325 {ECO:0000313|EMBL:RBI61852.1};
OS halophilic archaeon.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX NCBI_TaxID=29295 {ECO:0000313|EMBL:RBI61852.1, ECO:0000313|Proteomes:UP000252983};
RN [1] {ECO:0000313|EMBL:RBI61852.1, ECO:0000313|Proteomes:UP000252983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H22 {ECO:0000313|EMBL:RBI61852.1,
RC ECO:0000313|Proteomes:UP000252983};
RA Chen S.;
RT "Draft genome sequence of Haloarchaeon sp. H22 isolated from a salt mine.";
RL Submitted (JUL-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBI61852.1}.
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DR EMBL; QNGA01000003; RBI61852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365TBT5; -.
DR Proteomes; UP000252983; Unassembled WGS sequence.
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:UP000252983};
KW Transferase {ECO:0000313|EMBL:RBI61852.1}.
FT DOMAIN 477..618
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 622 AA; 67795 MW; 82B4AEA46C26D763 CRC64;
MSEYDYEDLG LVAGLEIHQQ LDTETKLFCE CPTRLRDPEE AARTFTRYLH PTKSELGEID
EAALEESQVD REFEYLAYDT TCLVEEDDEP PHRLDDEARE VVLEIAQLLD MDAVDQAQVM
RKIVVDGSNT SGFQRSTLVA RDGEIETSEG PVGVEDLMLE EESAQRVEER EDGVLYSLDR
LGIPLVEIGT KPDISTPEQA REAAERIGML LRSTGQVKRG LGTIRQDVNV SIEEGARVEM
KGVQSLDDID DLVRNEVERQ VELLAIRDEL RERDAAVGET RDVTDVFADT DSGVIRSALD
DGGAVTAVPL YGFDGLVGRE IQPDRRLGTE LSDHAKRRGA GGIFHTDELP AYGVTEDEVA
ALRDAVDAGE DDAVAIVAAA PDVAEGAIEA AAERAEVAVE AVPEETRGAN EDGTSRYLRP
LPGAARMYPE TDVPPVDLDP TEVETPELLT EKVDRYQDEY GLDAGLAEQV AYGRRMTLFE
RAVEAGVDAT LAAGTLESTV TELRRDGVSV ENLTDDHFLD ALGLVADDEV PKGSVGELLT
ALAETPELTA REAVEREDLG SADEDEVREA VVEVVERNDE QVEEQGMGAF SALMGECMGA
LGGQADGDLV SEMLREEIGK RA
//
