SYE_AFIC5
ID SYE_AFIC5 Reviewed; 473 AA.
AC B6JH82; F8BW48;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022};
DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022};
DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022};
GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022};
GN OrderedLocusNames=OCAR_5972, OCA5_c20520;
OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS (Oligotropha carboxidovorans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Afipia.
OX NCBI_TaxID=504832;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=18539730; DOI=10.1128/jb.00614-08;
RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT carboxidovorans OM5T.";
RL J. Bacteriol. 190:5531-5532(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=21742883; DOI=10.1128/jb.05619-11;
RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA Meyer O.;
RT "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT carboxidovorans strains OM4 and OM5.";
RL J. Bacteriol. 193:5043-5043(2011).
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; CP001196; ACI93092.1; -; Genomic_DNA.
DR EMBL; CP002826; AEI06759.1; -; Genomic_DNA.
DR RefSeq; WP_012563119.1; NC_015684.1.
DR AlphaFoldDB; B6JH82; -.
DR SMR; B6JH82; -.
DR STRING; 504832.OCAR_5972; -.
DR EnsemblBacteria; AEI06759; AEI06759; OCA5_c20520.
DR KEGG; oca:OCAR_5972; -.
DR KEGG; ocg:OCA5_c20520; -.
DR PATRIC; fig|504832.7.peg.2172; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_6_3_5; -.
DR OMA; WDEGPFF; -.
DR OrthoDB; 1409413at2; -.
DR Proteomes; UP000007730; 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: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; Reference proteome.
FT CHAIN 1..473
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_1000090094"
FT MOTIF 11..21
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 240..244
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ SEQUENCE 473 AA; 52213 MW; 0641DCF01364B4C4 CRC64;
MTEPVVTRFA PSPTGFLHIG GARTALFNWL YARKQGGKML LRIEDTDRER STDAAIKAIL
DGLNWLGIEW DGEVIYQFSR AARHREVAEQ LLAEGKAYRC YATPEELTKM REAARAEGRA
VRYDGRWRDR DPSEAPADVK PVIRLKAPQT GETVIEDQVQ GRVVWQNENL DDLVLLRSDG
TPTYMLAVVV DDHDMGVTHV IRGDDHLINA ARQKHIYDAL GWTVPTMAHI PLIHGPDGSK
LSKRHGALGV EAYRTMGYLP AALRNYLVRL GWSHGDQEIF STSEMIEAFE LSGIGRSAAR
FDFAKLENLN GHYMRASGDA ELVKAFEDIL QFLPQGPALQ AKLNDTTRAQ LLQAMPGLKE
RAKTLLELID SAAYIFADRP LALDAKASAV LTPQVRALLG ELRSSLANVT DWNAANTEAA
MRAYAEKNNL KLGAVAQPLR AALTGRTTSP GIFDVLAVLG RDDALARLQD QAA
