ID D9TLF5_CALOO Unreviewed; 480 AA.
AC D9TLF5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 01-MAY-2013, entry version 24.
DE RecName: Full=Glutamate--tRNA ligase;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase;
GN Name=gltX; OrderedLocusNames=COB47_1550;
OS Caldicellulosiruptor obsidiansis (strain ATCC BAA-2073 / strain OB47).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis;
OC Caldicellulosiruptor.
OX NCBI_TaxID=608506;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2073 / strain OB47;
RX PubMed=20851897; DOI=10.1128/JB.00950-10;
RA Elkins J.G., Lochner A., Hamilton-Brehm S.D., Davenport K.W.,
RA Podar M., Brown S.D., Land M.L., Hauser L.J., Klingeman D.M.,
RA Raman B., Goodwin L.A., Tapia R., Meincke L.J., Detter J.C.,
RA Bruce D.C., Han C.S., Palumbo A.V., Cottingham R.W., Keller M.,
RA Graham D.E.;
RT "Complete genome sequence of the cellulolytic thermophile
RT Caldicellulosiruptor obsidiansis OB47T.";
RL J. Bacteriol. 192:6099-6100(2010).
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; CP002164; ADL42837.1; -; Genomic_DNA.
DR RefSeq; YP_003840823.1; NC_014392.1.
DR ProteinModelPortal; D9TLF5; -.
DR EnsemblBacteria; ADL42837; ADL42837; COB47_1550.
DR GeneID; 9606006; -.
DR KEGG; cob:COB47_1550; -.
DR PATRIC; 42230435; VBICalObs143161_1663.
DR HOGENOM; HOG000252722; -.
DR KO; K01885; -.
DR BioCyc; COBS608506:GH1S-1589-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; 1.10.8.70; -; 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; IPR020752; aa-tRNA-synth_I_codon-bd_sub1.
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 8 18 "HIGH" region (By similarity).
FT MOTIF 249 253 "KMSKS" region (By similarity).
FT BINDING 252 252 ATP (By similarity).
SQ SEQUENCE 480 AA; 55892 MW; 7E8C096C8515515A CRC64;
MVRVRFAPSP TGQLHIGGAR TALFNYLFAK KHNGKFILRI EDTDLERSRE EWAEGIMRSL
RWLGIEWDEG PDIGGEFGPY FQSQRKEIYL EYIQKLLEEG KAYYCFCTQE EIEREREIAR
QQKIPYKYSK KCRNISLEEA KKRIENGEKA VVRIKAPVEG TTVVHDIIRG DVEFSNDQLD
DFIILKSDGN PTYNFVCVID DYLMKISHVI RAEEHLSNTP KQLIIYEALN IQPPQFAHVP
MILAPDRSKL SKRHGATSVE EFFENGYLKE AIVNYLLLLG WSPGEDKTII SLDEAIQKFE
LEKISKNAAI YDINKLTWIN GYYLKEIDID DLYERMKYFY SKVGIEITSF DKEYVKSVLK
LVREKVKTLV EVVSASIYFF DSNYEYEQKG VEKYFTPDNL KNLQLLLDDL KNIKPFSAEE
IEKLVRRKAE ELNTKAANII HTIRMCISGR TVTPGLFEMM EVLGKDEVIN RIEKTLKIFS
//
