ID B8GRV9_THISH Unreviewed; 470 AA.
AC B8GRV9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 38.
DE RecName: Full=Glutamate--tRNA ligase;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase;
GN Name=gltX; OrderedLocusNames=Tgr7_1579;
OS Thioalkalivibrio sp. (strain HL-EbGR7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A.,
RA Ivanova N., Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-
RT EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL72663.1; -; Genomic_DNA.
DR RefSeq; YP_002513650.1; NC_011901.1.
DR ProteinModelPortal; B8GRV9; -.
DR STRING; 396588.Tgr7_1579; -.
DR EnsemblBacteria; ACL72663; ACL72663; Tgr7_1579.
DR GeneID; 7316203; -.
DR KEGG; tgr:Tgr7_1579; -.
DR PATRIC; 23962702; VBIThiSp19295_1591.
DR eggNOG; COG0008; -.
DR KO; K01885; -.
DR OMA; RYRDFKG; -.
DR ProtClustDB; PRK01406; -.
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 236 240 "KMSKS" region (By similarity).
FT BINDING 239 239 ATP (By similarity).
SQ SEQUENCE 470 AA; 52950 MW; 0CD2310104E219DB CRC64;
MKVRTRFAPS PTGYLHIGGA RTALFSWLYA RKHGGDFILR VEDTDLARSN AESVNAILEG
MSWLGLEYDE GPFYQTQRFD RYKEVIQQLL DADKAYHCYC TKEELDAMRE QQMANKEKPR
YDGRCRHRTE PREGVEPVVR FRNPTEGATV VDDMVRGRVV FQNSELDDLI IARSDGSPTY
NFTVVVDDWD MQISHVIRGD DHLNNTPRQI NIFKALGVEP PRYAHLPMIL GPDGAKLSKR
HGAVSVMQYR DDGFLPQALL NYLVRLGWSH GDQEVFSLDE LIELFDIANV NHSASAINPD
KLLWLNQHYI KTSDPDHVAR HLSWHMGNHG IDPSLPPPLR DVVVAQCERA KTLVEMAANS
VYFYRDFEDY DEKAAKKNLD AEAKPVLQAL RAALDAVSDW QPEAIHAAVE GVAERLELKL
GKVAQPLRVA VSGGGVSPPI DQTLALLGRE RTLGRIERAI DYIEARSGGA
//
