ID   SYE1_SYNAS              Reviewed;         472 AA.
AC   Q2LQN4;
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 1;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamate--tRNA ligase 1;
DE            Short=GluRS 1;
GN   Name=gltX1; OrderedLocusNames=SYNAS_01920; ORFNames=SYN_02557;
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   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
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; ABC76071.1; -; Genomic_DNA.
DR   RefSeq; YP_460239.1; -.
DR   GeneID; 3884491; -.
DR   GenomeReviews; CP000252_GR; SYNAS_01920.
DR   KEGG; sat:SYN_02557; -.
DR   NMPDR; fig|56780.10.peg.190; -.
DR   HOGENOM; Q2LQN4; -.
DR   OMA; Q2LQN4; MAHIPLI.
DR   BioCyc; SACI56780:SYN_02557-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:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
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; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    472       Glutamyl-tRNA synthetase 1.
FT                                /FTId=PRO_0000237413.
FT   MOTIF        13     23       "HIGH" region.
FT   MOTIF       239    243       "KMSKS" region.
FT   METAL       102    102       Zinc (By similarity).
FT   METAL       104    104       Zinc (By similarity).
FT   METAL       129    129       Zinc (By similarity).
FT   METAL       131    131       Zinc (By similarity).
FT   BINDING     242    242       ATP (By similarity).
SQ   SEQUENCE   472 AA;  53248 MW;  4A1ED73395B51DE3 CRC64;
     MQKLKEIRTR FAPSPTGYLH IGGARTALFS WLYARHHQGK FVLRIEDTDQ LRSTEESTRA
     ILDAMTWLGL NWDEGPVFQA ERVDIHRAMI RKLVDEDKAY YCTCTPDELE EKRKRALAEG
     RKPKYDGTCR EKKLPPSPGT VVRFRCPQTG ITVVDDLIKG KISFNNEELD DLIIQRSDGY
     PTYNFAVVVD DAQMGISHVI RGDDHVNNTP RQILLYQALG YDIPHFGHVP MILGADKARL
     SKRHGATSVM AYKDMGYLPE ALVNYLVRLG WSHGDQEIFS LDELIALFGL ESIGKSAAVF
     NPEKLLWLNQ HYIKTYPEDR LLEVLQPFWK QLGIEAPDPD YGRSIVRDLR ARAKTLVDMA
     ESSTFYFNDE PAIDADAAKK FLTPEIAGHL EAIAEALATL GDYSKEGIEI FLRSLVEARA
     IKLKTIAQPL RIALTGKTVS PGLDDIMLTL GKERVIARIQ RTVAYIRSGM AS
//