ID SYE1_JANSC Reviewed; 470 AA.
AC Q28RA3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 01-MAY-2013, entry version 59.
DE RecName: Full=Glutamate--tRNA ligase 1;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase 1;
DE Short=GluRS 1;
GN Name=gltX1; OrderedLocusNames=Jann_1842;
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Jannaschia.
OX NCBI_TaxID=290400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E.,
RA Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A.,
RA Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-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 (By similarity).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family.
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DR EMBL; CP000264; ABD54759.1; -; Genomic_DNA.
DR RefSeq; YP_509784.1; NC_007802.1.
DR ProteinModelPortal; Q28RA3; -.
DR STRING; 290400.Jann_1842; -.
DR EnsemblBacteria; ABD54759; ABD54759; Jann_1842.
DR GeneID; 3934293; -.
DR KEGG; jan:Jann_1842; -.
DR PATRIC; 22147416; VBIJanSp43325_1975.
DR eggNOG; COG0008; -.
DR HOGENOM; HOG000252722; -.
DR KO; K01885; -.
DR OMA; FKISEQE; -.
DR ProtClustDB; PRK01406; -.
DR BioCyc; JSP290400:GI1R-1895-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 CHAIN 1 470 Glutamate--tRNA ligase 1.
FT /FTId=PRO_0000330975.
FT MOTIF 15 25 "HIGH" region.
FT MOTIF 241 245 "KMSKS" region.
FT BINDING 244 244 ATP (By similarity).
SQ SEQUENCE 470 AA; 51878 MW; EF92569AE1D3EFEE CRC64;
MSSDAASPVV TRIAPSPTGT MHIGTARTGL FNWLFARKHG GKFVLRIEDT DRERSTPEAT
QAILDGMAWL GLDYDGEAVS QFARADRHRE VAEQMLAEGH AYKCFSTQDE IAAFRDAAKA
DGRSTLFLSP WREASDHPDA PYVIRLKAPR DGTTVIRDRV QSDVTIQNAT LDDMILLRSD
GTPTYMHAVV VDDHDMGVTH VVRGDDHLNN AARQIQIYAA MGWAEPVWSH IPLIHGDDGK
KLSKRHGATG VMEYAEMGIP AAAMRNYLTR LGWSHGDEEL FTDEQARDWF DLDGIGKSPS
RLDMKKLANV TGWHIARTDD ADLVAQIEGY LALTGAPALS QAQHDGLTRA MYCLKDRAKS
LPDLLDKGRF VLENRPFDYD EKSVTMLDPV SRSILRELTA QLQNARWTRD TLEGVLNAAA
DSHGLKFGKL AGPLRAALSG RSVSPSVFDM MLVIGRDETL ARLDEAASLT
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