ID C6CNK7_DICZE Unreviewed; 471 AA.
AC C6CNK7;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 01-MAY-2013, entry version 35.
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; RYRDFKG; -.
DR ProtClustDB; PRK01406; -.
DR BioCyc; DZEA561229:GJ85-1095-MONOMER; -.
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:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA: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_Ib_bac/mito.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth_Ib.
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 PANTHER; PTHR10119:SF1; PTHR10119:SF1; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; tRNA-synt_bind; 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).
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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