SYE1_BRUAB
ID SYE1_BRUAB Reviewed; 457 AA.
AC Q57DB3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glutamate--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00022};
DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE AltName: Full=Glutamyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00022};
DE Short=GluRS 1 {ECO:0000255|HAMAP-Rule:MF_00022};
GN Name=gltX1 {ECO:0000255|HAMAP-Rule:MF_00022}; Synonyms=gltX-1;
GN OrderedLocusNames=BruAb1_1021;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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:0000255|HAMAP-
CC Rule:MF_00022}.
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:0000255|HAMAP-
CC Rule:MF_00022};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00022}.
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DR EMBL; AE017223; AAX74371.1; -; Genomic_DNA.
DR RefSeq; WP_002966819.1; NC_006932.1.
DR AlphaFoldDB; Q57DB3; -.
DR SMR; Q57DB3; -.
DR EnsemblBacteria; AAX74371; AAX74371; BruAb1_1021.
DR GeneID; 3788733; -.
DR KEGG; bmb:BruAb1_1021; -.
DR HOGENOM; CLU_015768_6_1_5; -.
DR OMA; PHWRFKL; -.
DR Proteomes; UP000000540; Chromosome I.
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:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00808; GluRS_core; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR033910; GluRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00464; gltX_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..457
FT /note="Glutamate--tRNA ligase 1"
FT /id="PRO_0000237343"
FT MOTIF 9..19
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 250..254
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ SEQUENCE 457 AA; 50828 MW; CB61D0FD9A6C460D CRC64;
MTVTVRFAPS PTGYIHIGNT RTALSNWLYA SKNNGKFILR YDDTDVERSK DEYAQAIAVD
LDWLGVRPDR VEYQSKRFDI YAKAVEKLKT AGLLYACYET ADELERRRKF RLARRLPPVY
GREALKLTDA EKAALEAEGR KPHWRFLLPN FESDPFATQR TEVHWDDLVR GPQTVDLASM
SDPILVREDG TYLYTLPSVV DDIDMGVTHI IRGDDHVTNT GVQISIFKAL GATPPVFGHH
NLLTTISGEG LSKRTGALSV GSLREAGYEP MAVASLAILI GTSESVTAAP DMAALAEHFD
LASISKSSAK FDPSELDALN RSLLHEMPFE KAKPRLEALG ICGAKAESFW LAVRGNLDRF
SDVSHWWQVV SGDLPEAPDL SGEDRDFVRH AFDLLPPEPW NGQTWKSWTE AVKSATGRKG
KNLFMPLRLA LTGQAHGPEL ADLLVLVGLE RTKSRRP
