ID   C1DUZ1_SULAA            Unreviewed;       478 AA.
AC   C1DUZ1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   01-MAY-2013, entry version 39.
DE   RecName: Full=Glutamate--tRNA ligase;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamyl-tRNA synthetase;
GN   Name=gltX; OrderedLocusNames=SULAZ_0955;
OS   Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium.
OX   NCBI_TaxID=204536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Az-Fu1 / DSM 15241 / OCM 825;
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the
RT   Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001229; ACN98629.1; -; Genomic_DNA.
DR   RefSeq; YP_002728928.1; NC_012438.1.
DR   ProteinModelPortal; C1DUZ1; -.
DR   STRING; 204536.SULAZ_0955; -.
DR   EnsemblBacteria; ACN98629; ACN98629; SULAZ_0955.
DR   GeneID; 7673345; -.
DR   KEGG; saf:SULAZ_0955; -.
DR   PATRIC; 23763038; VBISulAzo123226_0922.
DR   eggNOG; COG0008; -.
DR   HOGENOM; HOG000252720; -.
DR   KO; K01885; -.
DR   OMA; DDFDMEI; -.
DR   ProtClustDB; PRK01406; -.
DR   BioCyc; SAZO204536:GHRE-530-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       248    252       "KMSKS" region (By similarity).
FT   BINDING     251    251       ATP (By similarity).
SQ   SEQUENCE   478 AA;  55798 MW;  EC511FD686551D01 CRC64;
     MKRVRFAPSP TGYLHLGNAR TALFNYLFAK HENGSLILRI EDTDLERSKK EYEEMLIEDL
     KWLGIQWDEG PDVGGNYGPY RQSERLEIYY KYVDKLLKSG DAYYCYCSEE ELEKEREKAI
     AEGRPYRYSG KCRNLTPEER ADYEAQGIKP VVRFKVPDKT VIFEDIIRGH VEIDTKEFGD
     FVIVRQDGMP VYNFVVVIDD ALMGITHVIR GEDHLSNTPK QIVIYEALGF NIPQFAHLPI
     ILGEDRTKLS KRHGAVSVRA LKDDGFLSEA VFNYLSLLGW HPKDEREILP KEEIIKQFRI
     EDVNKSPAIF DRTKLRWMNG VYIREILDLE ELTKRSVEFF EGFGYKADFE FYKKVMEAIR
     DSIETLMDIK ERAKVFFVDE FPFTDEIVAE VKSDPNFYKV VEIFYEKVKG LDKLTKEDFK
     TITKEIQKEY GFKGKALFHP IRIALTGESS GVSLDLLVEV IGIERVKFRL KRFLEYFG
//