ID A0A117MGB8_9EURY Unreviewed; 558 AA.
AC A0A117MGB8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=XE11_1693 {ECO:0000313|EMBL:KUL02643.1};
OS Methanomicrobiales archaeon 53_19.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=1641394 {ECO:0000313|EMBL:KUL02643.1, ECO:0000313|Proteomes:UP000054757};
RN [1] {ECO:0000313|Proteomes:UP000054757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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}.
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:KUL02643.1}.
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DR EMBL; LGHF01000037; KUL02643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117MGB8; -.
DR PATRIC; fig|1641394.3.peg.2275; -.
DR Proteomes; UP000054757; Unassembled WGS sequence.
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 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}; Cytoplasm {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}.
FT DOMAIN 101..402
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 406..477
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 496..544
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT MOTIF 107..117
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02076"
SQ SEQUENCE 558 AA; 62858 MW; 9F50658E8CF3D47A CRC64;
MDEEIRRILE EYALQNAVKH KNVPRAGAVI GAVLGSHPEL RSRAHELNGM IGSVLADVEA
LSPGERETRL LALAPDLAAS MHQKKERSTE LPPLPDAEGG VVMRFAPNPS GPLHLGHARA
SILNDAYIHR YGGKYIYRIE DTDPKRVDPD AYQMVREDLE WLGIEISDII YQSDRLDIYY
EYARLLIELG GAYVCTCEAE RFRELKIEKK ACPCRTLTPE ENLLRYDQMF DGTFIEGQAT
VRIKTEIDHP DPAIRDYSAM RIVNSTIHPR VDATVYPLMN FSVAIDDHLL GMTHVIRGKD
HIANTRRQRY IFDYFGWKPP HYLHYGRMSI EGLVLSTSSM HEGISKGTYS GWDDIRLGTL
RALARRGIRP EAVRAAITEI GIGETDISFS WDNLFAKNRD IIDKESNRYF FVPEPISLRV
EGGPNQIAEA PRYPGDEERG YRKLHFTGEV LIPASEMKGG EMIRLKDLFN ITITGDQSAE
YAGDSLADAR AAKAPIIQWL PPESAVPCRI LTPEGVLEGF AEAEAADFAG RTIQFERVGF
VRIDSVEKNS ITAYFTHR
//
