ID F6BEG2_METIK Unreviewed; 557 AA.
AC F6BEG2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Glutamate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02076};
DE EC=6.1.1.17 {ECO:0000256|HAMAP-Rule:MF_02076};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02076};
DE Short=GluRS {ECO:0000256|HAMAP-Rule:MF_02076};
GN Name=gltX {ECO:0000256|HAMAP-Rule:MF_02076};
GN OrderedLocusNames=Metig_0062 {ECO:0000313|EMBL:AEF95623.1};
OS Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanotorris.
OX NCBI_TaxID=880724 {ECO:0000313|Proteomes:UP000009227};
RN [1] {ECO:0000313|EMBL:AEF95623.1, ECO:0000313|Proteomes:UP000009227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5666 / JCM 11834 / Kol 5
RC {ECO:0000313|Proteomes:UP000009227};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Chertkov O., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M.,
RA Whitman W., Woyke T.;
RT "Complete sequence of Methanotorris igneus Kol 5.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC then transferred to the acceptor end of tRNA(Glu). {ECO:0000256|HAMAP-
CC Rule:MF_02076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02076};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC ChEBI:CHEBI:456215; EC=6.1.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000948};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_02076}.
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DR EMBL; CP002737; AEF95623.1; -; Genomic_DNA.
DR RefSeq; WP_013798232.1; NC_015562.1.
DR AlphaFoldDB; F6BEG2; -.
DR STRING; 880724.Metig_0062; -.
DR GeneID; 10642897; -.
DR KEGG; mig:Metig_0062; -.
DR HOGENOM; CLU_001882_1_3_2; -.
DR OrthoDB; 10470at2157; -.
DR Proteomes; UP000009227; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd09287; GluRS_non_core; 1.
DR Gene3D; 2.40.240.100; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR049437; tRNA-synt_1c_C2.
DR NCBIfam; TIGR00463; gltX_arch; 1.
DR PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02076};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02076};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02076};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02076};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02076};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02076}; Reference proteome {ECO:0000313|Proteomes:UP000009227}.
FT DOMAIN 95..396
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 400..475
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 493..543
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT MOTIF 102..112
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02076"
SQ SEQUENCE 557 AA; 65020 MW; 7AC9CA9C63F2D084 CRC64;
MRDIVLKYVL QNAIKYNGKA NPKAVLGKFL AENAEYRKNA KEVLSIIEEV AKEVEKLSVE
EQIAKLKEIA PEMLEEDKGR QKKDKDLELK NVKGKVIMRF APNPSGPLHL GHARAAVLND
YFVKKYGGKL ILRLEDTDPK RVLPEAYDMI KEDLEWLGVK VDEVVIQSDR MDIYYEYGKK
LIEMGHAYVC ECDPEEFREL RNKGIPCKCR ERDVEENLEL WEKMLNGEVE NVAVRLKTDI
KHKNPSIRDF PIFRIEKTPH PRTGDKYCVY PLMNFSVPID DHLLGMTHVL RGKDHIVNTE
KQSYIYNYFG WEMPEYLHYG ILKIEGTVLS TSKMYEGIKE GIYKGWDDPR LGTLRALRRR
GIQPEAIYEI MKKIGIKQAD VRFSWENLYA INKDLIDKNA RRFFFVENPK KVIVKDAEKE
VLHLRMHPDN KELGTRELIF DGEIYVSDEL EEGKVYRLME LFNIVIEKVE DNIIYAKYHS
KDFKIARENK AKIIHWVPVK DCVKTTIIDT DAKEHVGVAE KDFKVANVGE IVQFERVGFV
RVDNKKDDEV VCYFAHK
//
