ID   SYE_CHLCH               Reviewed;         502 AA.
AC   Q3ATL0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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}; OrderedLocusNames=Cag_0392;
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CaD3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) 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: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; CP000108; ABB27665.1; -; Genomic_DNA.
DR   RefSeq; WP_011361438.1; NC_007514.1.
DR   AlphaFoldDB; Q3ATL0; -.
DR   SMR; Q3ATL0; -.
DR   STRING; 340177.Cag_0392; -.
DR   EnsemblBacteria; ABB27665; ABB27665; Cag_0392.
DR   KEGG; cch:Cag_0392; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_6_3_10; -.
DR   OMA; WDEGPFF; -.
DR   OrthoDB; 1409413at2; -.
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..502
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000237353"
FT   MOTIF           12..22
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           259..263
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   BINDING         262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   502 AA;  57687 MW;  710022D59566A909 CRC64;
     MVGQRVRTRF APSPTGYLHV GGLRTALYNF LFAKKMKGDF IIRIEDTDQS RKVEGAQQNL
     IKTLEWAGII ADESPQHGGS CGPYIQSERL DIYAKHCKQL LEDHHAYYCF ATPEELEENR
     QLQLKQGLQP KYNRKWLPEE MGGTMPESLI RQKLEAGEPY VIRMKVPDYI SVWFEDIIRG
     PIEFDSATID DQVLMKSDGF PTYHFASVID DHLMEISHII RGEEWLSSMP KHLLLYEFFG
     WEAPKVAHLP LLLNPDRSKL SKRQGDVAVE DYIRKGYSSE AIVNFVALLG WNEGEGCEQE
     VYSLQELTDK FSLERVGKAG SIFTLDKLKW LEKQYIKNRS VEKLLSVVKP LLLEELEKKP
     SIMAREQITS DSYLSSVIEL MRERVGFEHE FVTFSTYFYF EPESYDEESV KKRWQPNTNE
     LLADFIPQLE ALSDFTAENI EAALKAFVEP KGMKNAVLIH PLRIVTSGVG FGPSLYHMLE
     VLGKETVLRR IRKGLECITM PA