ID   SYE2_RHOCS              Reviewed;         468 AA.
AC   B6IST4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   09-APR-2025, entry version 80.
DE   RecName: Full=Glutamate--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            Short=GluRS 2 {ECO:0000255|HAMAP-Rule:MF_00022};
GN   Name=gltX2 {ECO:0000255|HAMAP-Rule:MF_00022};
GN   OrderedLocusNames=RC1_1191;
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW;
RA   Touchman J.W., Bauer C., Blankenship R.E.;
RT   "Genome sequence of Rhodospirillum centenum.";
RL   Submitted (MAR-2007) 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=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; CP000613; ACI98605.1; -; Genomic_DNA.
DR   RefSeq; WP_012566393.1; NC_011420.2.
DR   AlphaFoldDB; B6IST4; -.
DR   SMR; B6IST4; -.
DR   STRING; 414684.RC1_1191; -.
DR   KEGG; rce:RC1_1191; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_6_3_5; -.
DR   OrthoDB; 9807503at2; -.
DR   Proteomes; UP000001591; 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:000007; Glutamate--tRNA ligase; 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; 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.
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..468
FT                   /note="Glutamate--tRNA ligase 2"
FT                   /id="PRO_0000367750"
FT   MOTIF           9..19
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           238..242
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   BINDING         241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   468 AA;  52030 MW;  36817233D98A55D0 CRC64;
     MTIVTRFAPS PTGFLHIGGA RTALFNWLYA RGHGGKFLLR IEDTDRARST QAAVDAILDG
     LDWLGLEWDG DPISQFERKD RHAEVAHEML RRGMAYRCYA SPEELEAMKE EQRRQGLPMR
     YDGRWRDRDP SEAPAGVNPV IRLKAPQEGE TVVRDHVQGE VRVQNAQLDD MILLRSDGTP
     TYLLAVVVDD YDMGVTHVVR GDDHLTNTFR QLQIYAAMGW TPPEYAHVPL IHGPDGAKLS
     KRHGALGVDA YRDMGYLPET MRNYLLRLGW SHGDDEIIST DQAKAWFNLD DIGRSPSRLD
     FAKLDNLNGH YIRQSDDARL VSLVVPMVEK RLGRPLTGSE HARLLAAMPG FKPRVKTLVE
     LADGCLFLFA LRPLAMDDKA AALLTPEAKA QLGELHALFS GLGDWTGGAL EQAVRDFAER
     TGLKLGKVAQ PLRAALTGST VSPPIFEVAE VLGRTETLER IDDARKAG
//