ID   SYE_KOCRD               Reviewed;         506 AA.
AC   B2GFK2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   05-FEB-2025, 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};
GN   OrderedLocusNames=KRH_10280;
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX   PubMed=18408034; DOI=10.1128/jb.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(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=tRNA(Glu) + L-glutamate + ATP = L-glutamyl-tRNA(Glu) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA-
CC         COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215;
CC         EC=6.1.1.17; Evidence={ECO:0000255|HAMAP-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; AP009152; BAG29375.1; -; Genomic_DNA.
DR   RefSeq; WP_012398096.1; NC_010617.1.
DR   AlphaFoldDB; B2GFK2; -.
DR   SMR; B2GFK2; -.
DR   STRING; 378753.KRH_10280; -.
DR   KEGG; krh:KRH_10280; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_6_1_11; -.
DR   OrthoDB; 9807503at2; -.
DR   Proteomes; UP000008838; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   FunFam; 3.40.50.620:FF:000149; Glutamate--tRNA ligase; 1.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 1.10.8.70; Glutamate-tRNA synthetase, class I, anticodon-binding domain 1; 1.
DR   Gene3D; 1.10.1160.10; Glutamyl-trna Synthetase, Domain 2; 1.
DR   Gene3D; 3.90.800.10; Glutamyl-tRNA Synthetase, Domain 3; 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; IPR020752; Glu-tRNA-synth_I_codon-bd_sub1.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR   InterPro; IPR049940; GluQ/Sye.
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..506
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000367694"
FT   REGION          124..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           24..34
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           268..272
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   COMPBIAS        128..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   506 AA;  55925 MW;  C10CE1BD0C9FC98E CRC64;
     MTDDASTLHP TVPADAPVRV RFCPSPTGTP HVGLIRTALF NWAWARHTGG TLVFRIEDTD
     AARDSEESFQ QILDALDWLG ITWDEGVNVG GPHEPYRQSQ RGEIYQDVLA KLVDSGYVYE
     DFSTPEEVEQ RHRAKGEDPK RGYDNYDRDL TDEQKAAFRA EGRQPVLRLR MPDEDISFTD
     LVRGEITFKA GSVPDFVVAR ANGKPLYTLV NPVDDALMGI TQVLRGEDLL SSTPRQIALY
     RALVAIGVAE FIPEFGHLPY VMGEGNKKLS KRDPESNLFH HRDNGFIPEG LLNYLALLGW
     SLSADEDIFT VEQLVANFDI HDVLANPARF DVKKATAING THVRMLDPQD FRDRLVPYLR
     AAGLVGETLT PRENEILDRA APLVQERMNL LGETEGLLGF LFRGDDEIVV APDAAKQLKD
     SAPEVLDAAL AALEPLDDFT AEAIETALRE AIVDGLGIKP RLAFGPVRTA VSGQRISPPL
     FESLEILGRE SSLARIAALR AELAAN
//