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Database: UniProt
Entry: L9VML8_9EURY
LinkDB: L9VML8_9EURY
Original site: L9VML8_9EURY 
ID   L9VML8_9EURY            Unreviewed;       622 AA.
AC   L9VML8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
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=C496_16827 {ECO:0000313|EMBL:ELY38306.1};
OS   Natronorubrum tibetense GA33.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronorubrum.
OX   NCBI_TaxID=1114856 {ECO:0000313|EMBL:ELY38306.1, ECO:0000313|Proteomes:UP000011599};
RN   [1] {ECO:0000313|EMBL:ELY38306.1, ECO:0000313|Proteomes:UP000011599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA33 {ECO:0000313|EMBL:ELY38306.1,
RC   ECO:0000313|Proteomes:UP000011599};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY38306.1}.
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DR   EMBL; AOHW01000042; ELY38306.1; -; Genomic_DNA.
DR   RefSeq; WP_006091400.1; NZ_KB913017.1.
DR   AlphaFoldDB; L9VML8; -.
DR   STRING; 1114856.GCA_000383975_00040; -.
DR   PATRIC; fig|1114856.3.peg.3481; -.
DR   eggNOG; arCOG01719; Archaea.
DR   OrthoDB; 7316at2157; -.
DR   Proteomes; UP000011599; 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}; Transferase {ECO:0000313|EMBL:ELY38306.1}.
FT   DOMAIN          477..618
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
FT   REGION          425..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  67314 MW;  001C154BB822B8CC CRC64;
     MSEYDYDELG LVAGLEIHQQ LDTATKLFCQ CPTELREPEE STRTFTRYLH PTRSELGEID
     QAALEESKVD REFEYLAYDS TCLVEEDDEP PHELDNEALE TVLEIAQLMD MKPVDQANVM
     RKLVVDGSNT SGFQRSTLIA TEGEIETDDG AVGIEDLLLE EESAQRVEET DEGVRYSLDR
     LGIPLVEIGT KPDISSPEQA LEAAERIGML LRSTGKVKRG LGTIRQDVNV SIAEGARVEI
     KGVQSLDDID DIVRNEVARQ ARLVEIREEL EGREASVGET QDVTGVFEGT DSGVIGGALD
     SGGSVMAVPL YGFDGIVGRE VAPDRRLGTE FSDYAKRHGA GGIFHTDELP AYGVTEEEVA
     DLREAVGAGS EDAVAIVAAE TDVAEGSIEA VAERAGVALE GVPEETRGAN DDGTTRYLRP
     LPGAARMYPE TDVPPVEPDP SEVPEPELLT EKVERYQDEY DLSAGLAEQV AYGRRMPLFE
     DVVTDGTDPT LAATTLESTL TELRRDDVPV ENLTDSHIEA VLGMVDAGDV PNEGLPDLLE
     ALAEEPGRTA AEAAEAADLG SADEDAVRET IVEVVERNEG QVEEEGMQAF SGLMGECMGA
     LRGKADGDLV SEVLREEIQK RA
//
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