SYE_AZOBR
ID SYE_AZOBR Reviewed; 446 AA.
AC P45631; O07044;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 105.
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};
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sp245;
RA Costacurta A., Keijers V., Vanderleyden J.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=9608743; DOI=10.1007/s002849900317;
RA Zimmer W., Wesche M., Timmermans L.;
RT "Identification and isolation of the indole-3-pyruvate decarboxylase gene
RT from Azospirillum brasilense Sp7: sequencing and functional analysis of the
RT gene locus.";
RL Curr. Microbiol. 36:327-331(1998).
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; U17699; AAA61907.1; -; Genomic_DNA.
DR EMBL; X99587; CAA67900.1; -; Genomic_DNA.
DR AlphaFoldDB; P45631; -.
DR SMR; P45631; -.
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..446
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119496"
FT MOTIF 9..19
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"
FT CONFLICT 6
FT /note="P -> R (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="V -> L (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..81
FT /note="AT -> RY (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="S -> V (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="A -> S (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="P -> R (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="S -> A (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="A -> R (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="L -> V (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 220..223
FT /note="VGGA -> LTNSEGGGV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="T -> A (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="K -> E (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 423..424
FT /note="GQ -> PE (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="H -> E (in Ref. 1; AAA61907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 49179 MW; A7CE141B79416572 CRC64;
MSVAVPFAPS PTGLLHVGNV RLALVNWLFA RKAGGNFLVR LDDTDEERSK PEYAEGIERD
LTWLGLTWDR FARESDRYGA TDEVAAALKA SGRLYPCYET PEELNLKRAS LSSQGRPPIY
DRAALRLGDA DRARLEAEGR KPHWRFKLEH TPVEWTDLVR GPVHFEGSAL SDPVLIAEDG
RPLYTLTSVV DDADLAITHV IRGEDHLANT AVQIQIFEAV GGAVPVFAHL PLLTDATGQG
LSKRLGSLSV ASLREEEGIE PMALASLLAK LGTSDAIEPR LTLDELVAEF DIAKVSRATP
KFDPEELLRL NARILHLLPF ERVAGELAAS VWMMPTPAFW EAVPNLSRVA EARDWWAVTH
APVARRRTIP LFLAEAATLL PKEPWDLSTW GTWTGAVKAK TGRKGKDLFL PLRRALTGRD
HGGQLKNLLP LIGRTRAHKR LAGETA
