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Database: UniProt/TrEMBL
Entry: C6CNK7_DICZE
LinkDB: C6CNK7_DICZE
Original site: C6CNK7_DICZE 
ID   C6CNK7_DICZE            Unreviewed;       471 AA.
AC   C6CNK7;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   11-JUN-2014, entry version 40.
DE   RecName: Full=Glutamate--tRNA ligase;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamyl-tRNA synthetase;
GN   Name=gltX; OrderedLocusNames=Dd1591_1055;
OS   Dickeya zeae (strain Ech1591).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Dickeya.
OX   NCBI_TaxID=561229;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ech1591;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Dickeya zeae Ech1591.";
RL   Submitted (JUN-2009) 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 (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP001655; ACT05927.1; -; Genomic_DNA.
DR   RefSeq; YP_003003406.1; NC_012912.1.
DR   ProteinModelPortal; C6CNK7; -.
DR   STRING; 561229.Dd1591_1055; -.
DR   EnsemblBacteria; ACT05927; ACT05927; Dd1591_1055.
DR   GeneID; 8120332; -.
DR   KEGG; dze:Dd1591_1055; -.
DR   PATRIC; 21798042; VBIDicZea111179_1083.
DR   eggNOG; COG0008; -.
DR   HOGENOM; HOG000252722; -.
DR   KO; K01885; -.
DR   OMA; DSHEHHA; -.
DR   OrthoDB; EOG6DRPF7; -.
DR   BioCyc; DZEA561229:GJ85-1095-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 1.10.1160.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_00022_B; Glu_tRNA_synth_B; 1.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR10119; PTHR10119; 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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   MOTIF         9     19       "HIGH" region (By similarity).
FT   MOTIF       237    241       "KMSKS" region (By similarity).
FT   BINDING     240    240       ATP (By similarity){EA2}.
SQ   SEQUENCE   471 AA;  53473 MW;  AB3A63CDB4147CD5 CRC64;
     MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RHHGGEFVLR IEDTDLERST KEAIDAIMDG
     MNWLNLDWDE GPYYQTKRFD RYNAVIDQML ENGTAYKCYC SKERLEALRE QQMANGDKPR
     YDGCCRDSHE HHADDEPHVV RFRNPQDGSV IFDDRIRGPI EFSNLELDDL IIRRTDGAPT
     YNFCVVIDDW DMGITHVIRG EDHINNTPRQ INILKALGAP VPEYAHVSMI LGDDGKKLSK
     RHGAVGVMQY RDDGYLPEAL LNYLVRLGWA NGDQEIFSID EMKQLFSLDS VSKSASAFNT
     EKLQWLNHHY INHLPPEYVA THLSWHIEQA GIDTRTGPQL SELVTLLGER CKTLKEIAES
     CRYFYEEFAE FDADAAKKHL RPVARQPLEL VRSKLAAITD WTPENIHHAI QDTADELQQG
     MGKVGMPLRV AVTGAGQSPG VDVTVHAIGQ SRTLARIDQA LVFIAEREAQ Q
//
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