ID   SYE1_MAGSA              Reviewed;         444 AA.
AC   Q2W7Y6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Glutamate--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            Short=GluRS 1 {ECO:0000255|HAMAP-Rule:MF_00022};
GN   Name=gltX1 {ECO:0000255|HAMAP-Rule:MF_00022}; OrderedLocusNames=amb1235;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP007255; BAE50039.1; -; Genomic_DNA.
DR   RefSeq; WP_011383647.1; NC_007626.1.
DR   AlphaFoldDB; Q2W7Y6; -.
DR   SMR; Q2W7Y6; -.
DR   STRING; 342108.amb1235; -.
DR   PRIDE; Q2W7Y6; -.
DR   EnsemblBacteria; BAE50039; BAE50039; amb1235.
DR   KEGG; mag:amb1235; -.
DR   HOGENOM; CLU_015768_6_1_5; -.
DR   OMA; PHWRFKL; -.
DR   OrthoDB; 1409413at2; -.
DR   Proteomes; UP000007058; 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:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; 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..444
FT                   /note="Glutamate--tRNA ligase 1"
FT                   /id="PRO_0000237368"
FT   MOTIF           10..20
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           241..245
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   BINDING         244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   444 AA;  49181 MW;  9A252B67868D01F6 CRC64;
     MTSPVVRFAP SPTGLLHVGN ARVALLNRLF AKAHGGSFIL RLDDTDLERS RPEFAEAILD
     DLRWLGLDWD RLERQSARLD AYAAAAERLK VSGRVYACYE TPDELELRRK VQLGRGLPPV
     YDRAALKLAP DEIARLEAEG RRPHWRFKLE LEDVRWDDCV RGPSHYHGGN LSDPVLIRGD
     GSFLYTLPSV VDDIEFGVTH IIRGEDHVTN TAPQIQLFQA LGAVPPAFAH LPLLTGATGE
     GLSKRLGSGS LKDLRATGIH PMALNSLLAK LGSSDAIDIR HTLAELEAEF AWDKFGRGTP
     KFDSAELERL DARLMHTASF AEVRDRLGID GADEEFWLAV RPNLNHLAEA EAWWAICRQD
     LTPVIEDGEF TRAAAALLPD GAWDHATWGA WTETVKQATG RKGKALFHPL RLALTGRENG
     PELKTLLPLI GHDRARARLM GEIA