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Database: UniProt
Entry: E1RD53_METP4
LinkDB: E1RD53_METP4
Original site: E1RD53_METP4 
ID   E1RD53_METP4            Unreviewed;       610 AA.
AC   E1RD53;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 63.
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=Mpet_2289 {ECO:0000313|EMBL:ADN37036.1};
OS   Methanolacinia petrolearia (strain DSM 11571 / OCM 486 / SEBR 4847)
OS   (Methanoplanus petrolearius).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanolacinia.
OX   NCBI_TaxID=679926 {ECO:0000313|EMBL:ADN37036.1, ECO:0000313|Proteomes:UP000006565};
RN   [1] {ECO:0000313|EMBL:ADN37036.1, ECO:0000313|Proteomes:UP000006565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11571 / OCM 486 / SEBR 4847
RC   {ECO:0000313|Proteomes:UP000006565};
RX   PubMed=21304750;
RA   Brambilla E., Djao O.D., Daligault H., Lapidus A., Lucas S., Hammon N.,
RA   Nolan M., Tice H., Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Spring S., Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Methanoplanus petrolearius type strain (SEBR
RT   4847).";
RL   Stand. Genomic Sci. 3:203-211(2010).
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; CP002117; ADN37036.1; -; Genomic_DNA.
DR   RefSeq; WP_013330213.1; NC_014507.1.
DR   AlphaFoldDB; E1RD53; -.
DR   STRING; 679926.Mpet_2289; -.
DR   GeneID; 9744774; -.
DR   KEGG; mpi:Mpet_2289; -.
DR   eggNOG; arCOG01719; Archaea.
DR   HOGENOM; CLU_030702_0_0_2; -.
DR   OMA; SGFQRTM; -.
DR   OrthoDB; 7316at2157; -.
DR   Proteomes; UP000006565; 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}; Reference proteome {ECO:0000313|Proteomes:UP000006565};
KW   Transferase {ECO:0000313|EMBL:ADN37036.1}.
FT   DOMAIN          468..606
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   610 AA;  66859 MW;  2D54C8027B7ED915 CRC64;
     MDYEKIGLMA GIEIHQQLDT AEKLFCHCPT TLRDVDERCG EFKRYLRATE SEMGEIDRAA
     EEEMKKQDRI YTYYAYDTTC LVENDEEPPA PMNPEALGLS LTLAKMMGMT PVQQVHVMRK
     LVIDGSNTSG FQRTALVALN GILPAGARIE SICLEEEAAQ RVEGDTFSLD RLGIPLAEIT
     TGPDMRTPGQ VKEVAAYIGM LLRSTGRVKR GLGTIRQDVN ISIRDGARVE IKGVQDLSLI
     DEVVRREALR QQNLVEIAGE LKKRGASVGE EVVDVTDLFK DTGSSILKRA KCILAIKLCG
     FGGLVGKEIQ PGRRLGSEMS DYAKKCGVGG LFHTDELPAY GVTAEEVKIL KDRLAAGASD
     CVILVADTKK KSECAIGQIK KRAAMAFDGV PEETRKMLEE GSSAYMRPLP GAARMYPETD
     VLPVDISGEY WDSLELPELI TNKEKRFAGE FGLDESLARQ MAYSSKAGLF EEAVSKGVKP
     NLAARTIYST IRELRRDGVS TGRIRDEEII ELLLAVERGS AAKEAIPDIL RAVSTGDSVS
     AAMEKIAPSV SEEELSAVIA GIIEDRIDFV KEQGMRSLGP LMGVVMKEMR GRVDGKVISE
     VLKKELQKVL
//
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