ID A0A1D2WD62_9EURY Unreviewed; 620 AA.
AC A0A1D2WD62;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=A9507_05475 {ECO:0000313|EMBL:OEC88379.1};
OS Methanobacterium sp. A39.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=1860100 {ECO:0000313|EMBL:OEC88379.1, ECO:0000313|Proteomes:UP000094736};
RN [1] {ECO:0000313|EMBL:OEC88379.1, ECO:0000313|Proteomes:UP000094736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A39 {ECO:0000313|EMBL:OEC88379.1,
RC ECO:0000313|Proteomes:UP000094736};
RA Woodcroft B.J.;
RT "Validation of picogram- and femtogram-input DNA libraries for microscale
RT metagenomics.";
RL Submitted (JUN-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}.
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:OEC88379.1}.
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DR EMBL; LZPM01000006; OEC88379.1; -; Genomic_DNA.
DR RefSeq; WP_069582853.1; NZ_LZPM01000006.1.
DR AlphaFoldDB; A0A1D2WD62; -.
DR STRING; 1860100.A9507_05475; -.
DR Proteomes; UP000094736; 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:UP000094736};
KW Transferase {ECO:0000313|EMBL:OEC88379.1}.
FT DOMAIN 475..616
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 620 AA; 69172 MW; 576350039A5147C8 CRC64;
MDYEKLGLKM GLEVHQQLNT KEKLFCPCDC NLTDKEPEFK ILRNLRPTQS ELGKIDRAAF
EEARRKLNFI YDAYAHETCL VEADEEPPHP LNREALEVSL IIATLLNMHV VDEFHTMRKQ
VIDGSNTGGF QRTGLVATEG VLETKYGNVK IDVLCLEEDA ARRIGQEKGK VNFRLDRLGI
PLVEITTAPS ITHPEQVKEV AYHIGQVLRS TKVKRGIGTI RQDLNISIKE GARVELKGVQ
DLDLMSTMVE NEVKRQVNLL KIKDELNNRN ASVEDELHDI APLLKETKSK IIAKAESVFA
IKLNGFKGLI GIEIQPGRRF GTELAGYAKK MGVSGLFHTD ELPAYGITED EVNAINEFLG
LGDEDAFILI ADEKEKVINA LQEVQRRAKI SLQAVPEETR KALPDGNSDY LRPLPTASRM
YVETDIPAIS VSKELLGDIK SDLPELPDEK KVRIIKQYNL SEDLAKQLVR RNRADSFEKI
KAESGVDSTT IASTLAYTLK ELKRDGCSID ELNNSILLEA FELLENGKIS KDALPQILAN
VCSEGNSPQE AAESLNLMML SEDDVEKIIA EIVSSNKKMV EERGMGAMGP LMGMSMKKLK
GKADGKLVNK LLRDKLQNIE
//
