Sequence of Q9LCC6_9BACI
EC Number:4.3.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-aspartate = fumarate + NH3
Other sequences found for EC No. 4.3.1.1
General information:
Sequence
0 MNTDVRIEKD FLGEKEIPKD AYYGVQTIRA TENFPITGYR IHPELIKSLG IVKKSAALAN
60 MEVGLLDKEV GQYIVKAADE VIEGKWNDQF IVDPIQGGAG TSINMNANEV IANRALELMG
120 EEKGNYSKIS PNSHVNMSQS TNDAFPTATH IAVLSLLNQL IETTKYMQQE FMKKADEFAG
180 VIKMGRTHLQ DAVPILLGQE FEAYARVIAR DIERIANTRN NLYDINMGAT AVGTGLNADP
240 EYISIVTEHL AKFSGHPLRS AQHLVDATQN TDCYTEVSSA LKVCMINMSK IANDLRLMAS
300 GPRAGLSEIV LPARQPGSSI MPGKVNPVMP EVMNQVAFQV FGNDLTITSA SEAGQFELNV
360 MEPVLFFNLI QSISIMTNVF KSFTENCLKG IKANEERMKE YVEKSIGIIT AINPHVGYET
420 AAKLAREAYL TGESIRELCI KYGVLTEEQL NEILNPYEMT HPGIAGRK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
241218627
Kawata Y.,Tamura K.,Yano S.,Mizobata T.,Nagai J.,Esaki N.,Soda K.,Tokushige M.,Yumoto N.
Purification and characterization of thermostable aspartase from Bacillus sp. YM55-1.
Arch. Biochem. Biophys.
366
40-46
1999
241218628
Kawata Y.,Tamura K.,Kawamura M.,Ikei K.,Mizobata T.,Nagai J.,Fujita M.,Yano S.,Tokushige M.,Yumoto N.
Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue.
Eur. J. Biochem.
267
1847-1857
2000
241218629
Fujii T.,Sakai H.,Kawata Y.,Hata Y.
Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family.
J. Mol. Biol.
328
635-654
2003
241218630
Fibriansah G.,Veetil V.P.,Poelarends G.J.,Thunnissen A.M.
Structural basis for the catalytic mechanism of aspartate ammonia lyase.
Biochemistry
50
6053-6062
2011
