ID   SYE_CLOD6               Reviewed;         493 AA.
AC   Q18CD6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, 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};
GN   OrderedLocusNames=CD630_00510;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ66865.1; -; Genomic_DNA.
DR   RefSeq; WP_003435581.1; NZ_JAUPES010000031.1.
DR   RefSeq; YP_001086514.1; NC_009089.1.
DR   AlphaFoldDB; Q18CD6; -.
DR   SMR; Q18CD6; -.
DR   STRING; 272563.CD630_00510; -.
DR   EnsemblBacteria; CAJ66865; CAJ66865; CD630_00510.
DR   GeneID; 66352547; -.
DR   KEGG; cdf:CD630_00510; -.
DR   KEGG; pdc:CDIF630_00114; -.
DR   PATRIC; fig|272563.120.peg.55; -.
DR   eggNOG; COG0008; Bacteria.
DR   OrthoDB; 9807503at2; -.
DR   PhylomeDB; Q18CD6; -.
DR   BioCyc; PDIF272563:G12WB-103-MONOMER; -.
DR   Proteomes; UP000001978; 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; HUPs; 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; 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   NCBIfam; TIGR00464; gltX_bact; 1.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..493
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_1000001890"
FT   MOTIF           9..19
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           258..262
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   BINDING         261
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   493 AA;  56612 MW;  6676EAF97EB1B6CB CRC64;
     MNVRVRFAPS PTGFVHIGSL RTALYNYLFA KKMGGEYILR VEDTDQSRLV EGAIENMLNA
     MKWAGVNHSE GVILDDSGKV VQKGEYGPYI QSQRLDIYQE YIKQLLDSGK AYYCFCTKER
     LDEVRDAQRA AGETAKYDGH CKNLSKEEVE ANIKAGIPYV IRLRLPENHT IKFTDLVRGD
     MEFNTNDLDD QVLMKTDGFP TYHFAVVVDD YLMKITHVIR GEEWVSSTPK HVYLYEAFGW
     EAPVFVHLPN ILNKEKKKLS KRQGDVAVED FKKKGYLPEG LVNYVALVGW SPEDNQELFT
     MEELEKAFSV ERVSKSGGVF DTEKLNWVNQ HYIKDGDDAY LTDLAIPFLI EDGFITEEEA
     TNKYDFLKSM ISVLKEKLQY VKEVTEHASI FFGDKIEVET EEGREFLRLE HIPTLIDALR
     EKIEKTEVLN AEFVQAMLKE IQKEYKIKGK NLFMGSRIIL TGQMHGPDLP KVMEVLGKET
     CLNRIAYVKN NIL
//