ID   SYE2_SYNAS              Reviewed;         486 AA.
AC   Q2LUT2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Glutamyl-tRNA synthetase 2;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamate--tRNA ligase 2;
DE            Short=GluRS 2;
GN   Name=gltX2; OrderedLocusNames=SYNAS_19610; ORFNames=SYN_01399;
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophaceae; Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A.,
RA   Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.;
RT   "The genome of the syntrophic bacterium Syntrophus aciditrophicus:
RT   Life dependent on negative change in electrical potential.";
RL   Submitted (JAN-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.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000252; ABC77840.1; -; Genomic_DNA.
DR   RefSeq; YP_462008.1; -.
DR   GeneID; 3882794; -.
DR   GenomeReviews; CP000252_GR; SYNAS_19610.
DR   KEGG; sat:SYN_01399; -.
DR   NMPDR; fig|56780.10.peg.1951; -.
DR   HOGENOM; Q2LUT2; -.
DR   OMA; Q2LUT2; ATMAISH.
DR   BioCyc; SACI56780:SYN_01399-MON; -.
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:0006424; P:glutamyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00022; -; 1.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004527; Glu-tRNA-synth_Ic_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Gene3D; G3DSA:1.10.10.350; tRNA_synt_bd; 1.
DR   PANTHER; PTHR10119; Glu_tRNA-synt_1c; 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    486       Glutamyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000237414.
FT   MOTIF        12     22       "HIGH" region.
FT   MOTIF       252    256       "KMSKS" region.
FT   BINDING     255    255       ATP (By similarity).
SQ   SEQUENCE   486 AA;  55617 MW;  713BE8894F195C91 CRC64;
     MNSTKPRVRF APSPTGELHI GNARTAFFNW LYARHYGGKL ILRIEDTDRQ RSTRAFEARL
     IDDLKWLSLD WDEGPDGKGE VGPYRQSERL DLYESFLKNL QKDGRVYPCY CTEDELELER
     TSLLSRKMAP RYMGKCRNLT EADRRRLEAQ GRRPTWRFRV SQGPVLFQDL IRGTMKFQGE
     AVGDFIIVRS NGTPAYNFAV VIDDHFMEIS TVIRGEDHLS NTAIQLMLYE ALGFEPPEFA
     HHSLILGKDR TKLSKRHGSV SVREFREKGI LPEALLNYLA LLGSSIGEGR EVCSLEEIIT
     AFSLDRAGKS GAVFDEDKLL WMNSLYIHEE PAIKLIERLR PFIEKAGYDV NKWETPWLDR
     MVEAVKPNLT TLADIGSYVK MIVEEPVRID EDAAAVLRET ETQMVLRTLL QLIEEGKFSH
     EDFYSQVMTA LRKVTGARGK RLFMPVRAAL TGTTRGPELD KIFVLLGEQS VKERLKKALN
     MQGNFS
//