ID B7R0G5_9EURY Unreviewed; 628 AA.
AC B7R0G5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
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=TAM4_791 {ECO:0000313|EMBL:EEB74846.1};
OS Thermococcus sp. AM4.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB74846.1, ECO:0000313|Proteomes:UP000009277};
RN [1] {ECO:0000313|EMBL:EEB74846.1, ECO:0000313|Proteomes:UP000009277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM4 {ECO:0000313|EMBL:EEB74846.1,
RC ECO:0000313|Proteomes:UP000009277};
RX PubMed=22123768; DOI=10.1128/JB.06259-11;
RA Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A., Bartlett D.H.,
RA Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
RT "Complete Genome Sequence of the Hyperthermophilic Archaeon Thermococcus
RT sp. Strain AM4, Capable of Organotrophic Growth and Growth at the Expense
RT of Hydrogenogenic or Sulfidogenic Oxidation of Carbon Monoxide.";
RL J. Bacteriol. 193:7019-7020(2011).
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; CP002952; EEB74846.1; -; Genomic_DNA.
DR RefSeq; WP_014121405.1; NC_016051.1.
DR AlphaFoldDB; B7R0G5; -.
DR STRING; 246969.TAM4_791; -.
DR GeneID; 7419680; -.
DR KEGG; tha:TAM4_791; -.
DR eggNOG; arCOG01719; Archaea.
DR HOGENOM; CLU_030702_0_0_2; -.
DR OrthoDB; 7316at2157; -.
DR Proteomes; UP000009277; 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}; Transferase {ECO:0000313|EMBL:EEB74846.1}.
FT DOMAIN 484..624
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 628 AA; 71216 MW; 790B03EFD6E36CE8 CRC64;
MTEKFDYREL GLKVGLEIHR QLDTKKLFSP VPSELTEKVD FTFERHLRPT MSELGEIDPA
ALEEFKKGRK YIYEGNYELS DLVYMDEEPP RGPDKEALEV TLQIAYLLNA KPVDEVHFMR
KIVIDGSNVS GFQRTAIIAL DGKVDTPWGS VGIPTICLEE DACRIVERKE KEVIYRLDRL
GIPLVEISTT PDIHHPEQAK VVAKYIGDAL RATRKVKRGL GTIRQDLNVS IKGGARVEIK
GVQELDMIPL IIEREVERQL NLLKIRDELR ARGVKPEDIR EEFYDVTDVF ENTESKIIAR
TIKKGGKVLA VKLPKFRGLI GREIQPGRRL GTEMADRAKK YVKGIFHIDE LPNYGITEKE
VNAVIEKLGL GELDAFVLVA ADEETAKKAL REVIKRAREA IEGVPEETRR ALPDGNTQYM
RPLPGKARMY PETDIPSIFI PPEEKKRIKA NLPELPQERI ERYVKEYKID KSLAETLVND
ERDELFEELV KKGVKPSLAA SILVVVLKGL KKEVPIENIT DEHIREAFEL YLDGKIAKEA
FEEIFKELAR NPEKTAEQVA EEKGLTLLSE EEVEKIIDEV IQANIDVIKA KGMGAMGMIM
GRAMAKLRGR ADGKLVSSLV RKKIQELS
//
