ID   SYE1_NOVAD              Reviewed;         442 AA.
AC   Q2G9R1;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Glutamyl-tRNA synthetase 1;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamate--tRNA ligase 1;
DE            Short=GluRS 1;
GN   Name=gltX1; OrderedLocusNames=Saro_0967;
OS   Novosphingobium aromaticivorans (strain DSM 12444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a
CC       two-step reaction: glutamate is first activated by ATP to form
CC       Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC       diphosphate + L-glutamyl-tRNA(Glu).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000248; ABD25412.1; -; Genomic_DNA.
DR   RefSeq; YP_496246.1; -.
DR   GeneID; 3915749; -.
DR   GenomeReviews; CP000248_GR; Saro_0967.
DR   KEGG; nar:Saro_0967; -.
DR   NMPDR; fig|48935.1.peg.3073; -.
DR   HOGENOM; Q2G9R1; -.
DR   OMA; Q2G9R1; LRLDDTD.
DR   BioCyc; NARO279238:SARO_0967-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00022; -; 1.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004527; Glu-tRNA-synth_Ic_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Gene3D; G3DSA:1.10.10.350; tRNA_synt_bd; 1.
DR   PANTHER; PTHR10119; Glu_tRNA-synt_1c; 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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    442       Glutamyl-tRNA synthetase 1.
FT                                /FTId=PRO_0000237380.
FT   MOTIF         9     19       "HIGH" region.
FT   MOTIF       240    244       "KMSKS" region.
FT   BINDING     243    243       ATP (By similarity).
SQ   SEQUENCE   442 AA;  48922 MW;  841180C310E17DF3 CRC64;
     MATVTRFAPS PTGKLHVGNV RTALHNWLLA KKTGGRFLLR IDDTDAERSR EEYVESIRAD
     LQWLGLIPDG EERQSLRTEL YEREFQRLVE AGRIYRAYET AQELDLKRKI LLGRGLPPIY
     DRAALKLTEA DHAAKAAAGE RPHWRFLLDH DQPITWDDGI RGPQSFDPRQ MSDPVIRRAD
     GSWLYMLPSA IDDIAMGITD VLRGEDHVSN TATQIQMFTA LGAEPPRFAH EALLTGSEGK
     LSKRLGALGM ADFREQGIEP EAIVALLARL GTSDPVDAAL DAAALATSFD LSRFGRAPAR
     FDEADLHRVN AQIVHRLPYA RVAHLLPQGM GEAAWEAIRP NLAHIDEARD WWNVVTGPVT
     APTFDDETRA FLAQAAKTAA SLDWSADPWR ALTATLKDGT GRKGKALFLP LRQALTGHDH
     GPEMAALLPL IAQDEAVRRL SA
//