ID   SYE2_NOVAD              Reviewed;         487 AA.
AC   Q2G6Q3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-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=Saro_2031;
OS   Novosphingobium aromaticivorans (strain DSM 12444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
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; CP000248; ABD26470.1; -; Genomic_DNA.
DR   RefSeq; YP_497304.1; -.
DR   GeneID; 3917678; -.
DR   GenomeReviews; CP000248_GR; Saro_2031.
DR   KEGG; nar:Saro_2031; -.
DR   NMPDR; fig|48935.1.peg.2297; -.
DR   HOGENOM; Q2G6Q3; -.
DR   OMA; Q2G6Q3; MARYDAN.
DR   BioCyc; NARO279238:SARO_2031-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    487       Glutamyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000237381.
FT   MOTIF        24     34       "HIGH" region.
FT   MOTIF       258    262       "KMSKS" region.
FT   BINDING     261    261       ATP (By similarity).
SQ   SEQUENCE   487 AA;  53204 MW;  8DCC1B1CDBC397A2 CRC64;
     MASATDTVSA GSTPRDKVVT RFAPSPTGFL HIGGARTALF NWLYARHHGG TYLLRIEDTD
     RARSTDAAID AIFDGLEWLG LGGDEPAVFQ FARSDRHAEV AHKLLEAGHA YRCYLTQEEL
     AARRELAQAE RRPFRIDSEW RDATPDQWPA DQSYVVRMKA PREGETTIVD KVQGSITVQN
     SELDDFIILR SDGTPTYMLA VVVDDHDMGV THVIRGDDHI NNAFRQLVII RGMHAIEGGW
     PDPVYAHIPL IHGADGAKLS KRHGALGVDA YRDEMGLLPE AVFNYLLRLG WGHGDEEIIS
     REQAVAWFDI GDVNKGASRF DLKKLLNLNG HYIREADDAR LAALVAPRLA TLAPGFAPDK
     GLDLLTRAMP VLKVRAADIN ELAAGSVFLF AQRPLAMAEK AASLLTDDAR AILTKVAGVL
     EAENVWTTGV LEATVKQMAE ELGIGLGKIA QPLRASLTGQ TTSPGIFDVL ALLGKDESLS
     RIRDQAA
//