ID B1L646_KORCO Unreviewed; 631 AA.
AC B1L646;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 OrderedLocusNames=Kcr_1179 {ECO:0000313|EMBL:ACB07925.1};
OS Korarchaeum cryptofilum (strain OPF8).
OC Archaea; Candidatus Korarchaeota; Korarchaeum.
OX NCBI_TaxID=374847 {ECO:0000313|EMBL:ACB07925.1, ECO:0000313|Proteomes:UP000001686};
RN [1] {ECO:0000313|EMBL:ACB07925.1, ECO:0000313|Proteomes:UP000001686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF8 {ECO:0000313|Proteomes:UP000001686};
RX PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA Richardson P., Keller M., Stetter K.O.;
RT "A korarchaeal genome reveals new insights into the evolution of the
RT Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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; CP000968; ACB07925.1; -; Genomic_DNA.
DR RefSeq; WP_012309822.1; NC_010482.1.
DR AlphaFoldDB; B1L646; -.
DR STRING; 374847.Kcr_1179; -.
DR EnsemblBacteria; ACB07925; ACB07925; Kcr_1179.
DR GeneID; 6094456; -.
DR KEGG; kcr:Kcr_1179; -.
DR eggNOG; arCOG01719; Archaea.
DR HOGENOM; CLU_030702_0_0_2; -.
DR InParanoid; B1L646; -.
DR OrthoDB; 7316at2157; -.
DR PhylomeDB; B1L646; -.
DR Proteomes; UP000001686; 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; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
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:UP000001686}.
FT DOMAIN 487..625
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 631 AA; 71512 MW; 6CEE3D3219125543 CRC64;
MEDSFYRDVG LKVGLEIHQR LDSHKLFCNC PSILREEEPH SWISRNLSVS YSELGTIDPA
ARFESLRRRN FLYGIYFDTT CEVEIDEAPP HPLNEDALEI SIQVALMLRM KPIDEIHVMR
KIVVDGSNTT GFQRTALVAL GHGESYIETS KGKVRLETLC LEEESAYIVE STPEFAKYRL
DRLGIPLVEI STAPDIWHPE QAMEAALKIG RILRATGRVQ RGIGTIRQDI NVSIEGGARQ
EIKGIQELEL IPEVIRREIL RQQNLLKIQE ELRKRGIDEK DVDDPIYDIT DALSQTGSQL
IKRSLTRGER IFGMRVKGFR GLIGKEIQPE RRFGTELADY ARVFGGVKGI LHGDELPGYG
IGDEEVKRIR DALSCDDDDS FILVIGERSS STLALESVRS RIKFSIRGIP SETRRALPDG
NTSFMRPMPG AARMYPETDI LPVKTAPIIN RIRELPKMPE ETVSELIKEY GINSELAWDL
YDEGKISLFK KLVSYGAPAS FTAATLTSTM RMLRREGENI ERITEDHLVE LFRFLGDGML
AKEAVPEVLR GIARGDYSSV HDYLKSYSMS LDELDSLIDS TLERFRDKVL ERGDRAFGML
MGEVMRVARG RIDGSIVSER LRIKLKEFLK T
//
