ID   SYE_NITHX               Reviewed;         474 AA.
AC   Q1QMM2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   24-JAN-2024, entry version 98.
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=Nham_1709;
OS   Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=323097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10229 / NCIMB 13809 / X14;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA   O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA   Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE62525.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000319; ABE62525.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041357859.1; NC_007964.1.
DR   AlphaFoldDB; Q1QMM2; -.
DR   SMR; Q1QMM2; -.
DR   STRING; 323097.Nham_1709; -.
DR   KEGG; nha:Nham_1709; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_6_0_5; -.
DR   OrthoDB; 9807503at2; -.
DR   Proteomes; UP000001953; 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; 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   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.
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..474
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000330985"
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   474 AA;  52770 MW;  4D1430BDAD4ECD54 CRC64;
     MIASVVTRFA PSPTGFLHIG GARTALFNWL YARKHGGKML LRIEDTDRAR STTAAIEAIL
     DGLKWLGIDW DDDVVYQFSR VARHRDIAEQ LLAEGKAYRC YATPEELAEM REKARAEGRA
     KLYDGRWRDR DPSEAPPDLK PTIRLKAPLS GETVIEDQVQ GRVVWQNENL DDLVLLRGDG
     TPTYMLAVVV DDHDMGVTHI IRGDDHLINA ARQKQIYDTL GWALPTMAHI PLIHGPDGSK
     LSKRHGALGV DAYRAMGYLP AALRNYLVRL GWSHGDQEIF STQEMIDAFD LSAIGRSAAR
     FDFAKLENLN GHYIRNCDDH VLVDLFQDAL DYVPRGADLK PKLNDATRAQ LLRAMPGLKE
     RAKTLIELID SARFIFADRP LTLDAKAIPL LTSETRALIG RLRTTLETVT SWSAQTTEAA
     MRTFAEQNNL KLGAIAQPLR IALTGRTTSP GIFDVLAVLG KETCLARLDD QSSP
//