ID A0A0A7V334_9ARCH Unreviewed; 632 AA.
AC A0A0A7V334;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:AJA92581.1};
GN ORFNames=A7X95_05630 {ECO:0000313|EMBL:PTL87376.1}, T478_0113
GN {ECO:0000313|EMBL:AJA92581.1};
OS Candidatus Nitrosopelagicus brevis.
OC Archaea; Nitrososphaerota.
OX NCBI_TaxID=1410606 {ECO:0000313|EMBL:AJA92581.1, ECO:0000313|Proteomes:UP000030944};
RN [1] {ECO:0000313|EMBL:AJA92581.1, ECO:0000313|Proteomes:UP000030944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN25 {ECO:0000313|EMBL:AJA92581.1}, and V2
RC {ECO:0000313|Proteomes:UP000030944};
RX PubMed=25587132; DOI=10.1073/pnas.1416223112;
RA Santoro A.E., Dupont C.L., Richter R.A., Craig M.T., Carini P.,
RA McIlvin M.R., Yang Y., Orsi W.D., Moran D.M., Saito M.A.;
RT "Genomic and proteomic characterization of "Candidatus Nitrosopelagicus
RT brevis": An ammonia-oxidizing archaeon from the open ocean.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:1173-1178(2015).
RN [2] {ECO:0000313|EMBL:PTL87376.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U25 {ECO:0000313|EMBL:PTL87376.1};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000241022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U25 {ECO:0000313|Proteomes:UP000241022};
RA Dupont C., Santoro A.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PTL87376.1, ECO:0000313|Proteomes:UP000241022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U25 {ECO:0000313|EMBL:PTL87376.1,
RC ECO:0000313|Proteomes:UP000241022};
RA Carini P.;
RT "Transcriptomics of ammonia oxidizing archaea.";
RL Submitted (APR-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP007026; AJA92581.1; -; Genomic_DNA.
DR EMBL; LXWN01000002; PTL87376.1; -; Genomic_DNA.
DR RefSeq; WP_048104353.1; NZ_LXWN01000002.1.
DR STRING; 1410606.T478_0113; -.
DR GeneID; 24816012; -.
DR KEGG; nbv:T478_0113; -.
DR HOGENOM; CLU_030702_0_0_2; -.
DR OrthoDB; 7316at2157; -.
DR Proteomes; UP000030944; Chromosome.
DR Proteomes; UP000241022; 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:UP000030944};
KW Transferase {ECO:0000313|EMBL:AJA92581.1}.
FT DOMAIN 485..627
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 632 AA; 70834 MW; 65B50C522BC45095 CRC64;
MSEVDIKNIG LKVGLEIHQQ LDTKKKLFCD CTPIEEEEFS RKFSRKLRAA KSELGKIDPA
ALFESTKSKT IVYYANPRSS CLVCEDEEPP HSLDISAKKI ALLISSALES KIFSEIHVMR
KTVIDGSNTT GFQRTMLVSQ GGHIEVNGEK VGVQSICLEE DAGKLVKDEG NHRFFSLDRL
GVPLVEIALD PVEGDPKFVK DIALTLGRLL RVTKKVMRGI GTIRQDVNIS VEGGGVIEVK
GVQQLDQLEK IIEFEAKRQH GLKLISDKIN QIGFTEISRK EDVFDITDIM QECNSKIIKK
SIKKQEKIFG IKIKKLKGIF GFEPYSDIRL GKEIGQLVRF FGIGGVFHSD ELPNYGIEET
DIKRVIEKLD VQNDDAFLII AGEKISVGFA IDSIINRIEL AKEGPPAETR AATQNGDTIF
LRPRPGASRM YPETDIPTVK VSEKELSEAV SNIPKSWEAS IKELESKYEI NNQLAEQIFD
SEYFEIFEQI CSKKQSSPNF VVSILCSTIT NLERSGLDSS LLNDEQIMKT FELLGEEKIN
KESIEIIFEQ IMSKKADNVL QALEKASITQ LTDEELDKIL DDIIQKNMNK VKEEQSRALS
GLMGIAMKEV RGKASGKIIN EKLKAKIQNF LN
//
