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Sequence of SYD_THETH

EC Number:6.1.1.12

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
aspartate-tRNA ligase
P36419
Thermus thermophilus
580
66030
Reaction
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp
Other sequences found for EC No. 6.1.1.12

General information:

Sequence
show sequence in fasta format
  0 MRRTHYAGSL RETHVGEEVV LEGWVNRRRD LGGLIFLDLR DREGLVQLVA HPASPAYATA
 60 ERVRPEWVVR AKGLVRLRPE PNPRLATGRV EVELSALEVL AEAKTPPFPV DAGWRGEEEK
120 EASEELRLKY RYLDLRRRRM QENLRLRHRV IKAIWDFLDR EGFVQVETPF LTKSTPEGAR
180 DFLVPYRHEP GLFYALPQSP QLFKQMLMVA GLDRYFQIAR CFRDEDLRAD RQPDFTQLDL
240 EMSFVEVEDV LELNERLMAH VFREALGVEL PLPFPRLSYE EAMERYGSDK PDLRFGLELK
300 EVGPLFRQSG FRVFQEAESV KALALPKALS RKEVAELEEV AKRHKAQGLA WARVEEGGFS
360 GGVAKFLEPV REALLQATEA RPGDTLLFVA GPRKVAATAL GAVRLRAADL LGLKREGFRF
420 LWVVDFPLLE WDEEEEAWTY MHHPFTSPHP EDLPLLEKDP GRVRALAYDL VLNGVEVGGG
480 SIRIHDPRLQ ARVFRLLGIG EEEQREKFGF FLEALEYGAP PHGGIAWGLD RLLALMTGSP
540 SIREVIAFPK NKEGKDPLTG APSPVPEEQL RELGLMVVRP
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
870563
Poterszman A.,Plateau P.,Moras D.,Blanquet S.,Mazuric M.-H.,Kreutzer R.,Kern D.
Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases.
FEBS Lett.
325
183-186
1993
870564
Delarue M.,Poterszman A.,Nikonov S.,Garber M.,Moras D.,Thierry J.-C.
Crystal structure of a prokaryotic aspartyl tRNA-synthetase.
EMBO J.
13
3219-3229
1994
870565
Poterszman A.,Delarue M.,Thierry J.C.,Moras D.
Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase.
J. Mol. Biol.
244
158-167
1994
870566
Briand C.,Poterszman A.,Eiler S.,Webster G.,Thierry J.-C.,Moras D.
An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase.
J. Mol. Biol.
299
1051-1060
2000
870567
Ng J.D.,Sauter C.,Lorber B.,Kirkland N.,Arnez J.,Giege R.
Comparative analysis of space-grown and earth-grown crystals of an aminoacyl-tRNA synthetase: space-grown crystals are more useful for structural determination.
Acta Crystallogr. D
58
645-652
2002