ID   SYE1_COXBU              Reviewed;         469 AA.
AC   Q83EV3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 42.
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; Synonyms=gltX-1; OrderedLocusNames=CBU_0205;
OS   Coxiella burnetii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=777;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nine Mile phase I / RSA 493;
RX   MEDLINE=22608657; PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E.,
RA   Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J.,
RA   DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J.,
RA   Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A.,
RA   Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella
RT   burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO89765.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_819251.2; -.
DR   HSSP; P27000; 1J09.
DR   GeneID; 1208081; -.
DR   GenomeReviews; AE016828_GR; CBU_0205.
DR   KEGG; cbu:CBU_0205; -.
DR   NMPDR; fig|227377.1.peg.195; -.
DR   TIGR; CBU_0205; -.
DR   HOGENOM; Q83EV3; -.
DR   OMA; Q83EV3; MAHIPLI.
DR   BioCyc; CBUR227377:CBU_0205-MON; -.
DR   BRENDA; 6.1.1.17; 256353.
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    469       Glutamyl-tRNA synthetase 1.
FT                                /FTId=PRO_0000119550.
FT   MOTIF        10     20       "HIGH" region.
FT   MOTIF       237    241       "KMSKS" region.
FT   METAL        99     99       Zinc (By similarity).
FT   METAL       101    101       Zinc (By similarity).
FT   METAL       126    126       Zinc (By similarity).
FT   METAL       128    128       Zinc (By similarity).
FT   BINDING     240    240       ATP (By similarity).
SQ   SEQUENCE   469 AA;  53697 MW;  E6C2E5C22060D888 CRC64;
     MKHIRTRFAP SPTGYLHIGG VRTALFSWLF ARQNNGAFIL RIEDTDVARS TQASVDAILE
     GLRWLQIDWN EGPYYQSQRM DRYREVIEQL VKSDDAYRCY CSKERLIELR NTQLKNKQKP
     RYDGFCRDKA PRQSNEPFVI RFRNPVEGAV VFDDLIRGTI SIDNRELDDL IIARSDGGPT
     YNLTVVVDDW DMKITHVIRG DDHINNTPRQ INILHALGAE LPHYGHVPMI LGPDGKRLSK
     RHGAVSVLQY RDEGYLPEAL MNYLIRLGWA HGDQEIFSRE EMVQLFDISA VSRSPAAFNP
     EKLLWLNQHY LKTVSPTIIA EAFATQLEKA GTDLRNGPSL EQVIALQAER TKTLKEMAQR
     SLYFYQEVRS YDEKAARKHL LATIVEPLQR VRERLASLPS WEKEAIHEVI VETAQLHQLK
     LGQLAQPIRV ALTGDTVSPP IDATLYLIGR DSALKRLDHA IRFIHQGMG
//