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Database: UniProt/TrEMBL
Entry: D9TLF5_CALOO
LinkDB: D9TLF5_CALOO
Original site: D9TLF5_CALOO 
ID   D9TLF5_CALOO            Unreviewed;       480 AA.
AC   D9TLF5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   19-FEB-2014, entry version 26.
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   OMA; NKLTWIN; -.
DR   BioCyc; COBS608506:GH1S-1589-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; 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_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         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
//
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