ID   SYE_HELMI               Reviewed;         496 AA.
AC   B0TBU3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Helmi_13070;
GN   ORFNames=HM1_1355;
OS   Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliomicrobium.
OX   NCBI_TaxID=498761;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51547 / Ice1;
RX   PubMed=18441057; DOI=10.1128/jb.00299-08;
RA   Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA   Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA   Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA   Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT   "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT   of the Firmicutes containing the simplest photosynthetic apparatus.";
RL   J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ83932.1; -; Genomic_DNA.
DR   RefSeq; WP_012282448.1; NC_010337.2.
DR   AlphaFoldDB; B0TBU3; -.
DR   SMR; B0TBU3; -.
DR   STRING; 498761.HM1_1355; -.
DR   EnsemblBacteria; ABZ83932; ABZ83932; HM1_1355.
DR   KEGG; hmo:HM1_1355; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_6_3_9; -.
DR   OMA; WDEGPFF; -.
DR   OrthoDB; 1409413at2; -.
DR   Proteomes; UP000008550; 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..496
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000367689"
FT   MOTIF           10..20
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           251..255
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   BINDING         254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   496 AA;  55178 MW;  FF6746621E7D6ADD CRC64;
     MENIRVRFAP SPTGPLHIGG ARSALFNFLL ARRFGGQFIV RVEDTDLERS SRESEDNILD
     ALEWLGITWD EGIRVGGPHA PYRQTERLHT YREAADKLLA EGKAYRCYCS EEELEAERQA
     FAEKGELPRY SGRCRSLSAD DEARLRAEGR KPVIRFRVPD EGAVAIDDLV RGHVSFECAG
     IGDFIIVKSD GIPTYNFAVV IDDAQMAITH VIRGEEHLSN TPRQLLIYDA LGLTPPKFAH
     VSLILGKDRS KMSKRHGSTS VVAYQRQGYL PEALVNFLVL LGWSPGGEEE IFSLDDLIAQ
     FSLDRVAKSP AVFDFEKLNW INGVYLRKAD LDRLVALAMP HLIEAGVVQE PLDEAAARKV
     RYMVQAIQEK VSYMAQIVDF IPLFFGDAIT FESDEAKAVL TEEQVPKVLK ACLRKLTEGR
     DLTPDNVKAM LKEVTKETKE KGRNVFMPIR VALTGQQHGP DLNALITALG REGAVNRIRR
     AAELAGVALG SSPFSC