Sequence of AK3_ECOLI
EC Number:2.7.2.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + L-aspartate = ADP + 4-phospho-L-aspartate
Other sequences found for EC No. 2.7.2.4
General information:
Sequence
0 MSEIVVSKFG GTSVADFDAM NRSADIVLSD ANVRLVVLSA SAGITNLLVA LAEGLEPGER
60 FEKLDAIRNI QFAILERLRY PNVIREEIER LLENITVLAE AAALATSPAL TDELVSHGEL
120 MSTLLFVEIL RERDVQAQWF DVRKVMRTND RFGRAEPDIA ALAELAALQL LPRLNEGLVI
180 TQGFIGSENK GRTTTLGRGG SDYTAALLAE ALHASRVDIW TDVPGIYTTD PRVVSAAKRI
240 DEIAFAEAAE MATFGAKVLH PATLLPAVRS DIPVFVGSSK DPRAGGTLVC NKTENPPLFR
300 ALALRRNQTL LTLHSLNMLH SRGFLAEVFG ILARHNISVD LITTSEVSVA LTLDTTGSTS
360 TGDTLLTQSL LMELSALCRV EVEEGLALVA LIGNDLSKAC GVGKEVFGVL EPFNIRMICY
420 GASSHNLCFL VPGEDAEQVV QKLHSNLFE
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
388066
Cassan M.,Parsot C.,Cohen G.N.,Patte J.-C.
Nucleotide sequence of lysC gene encoding the lysine-sensitive aspartokinase III of Escherichia coli K12. Evolutionary pathway leading to three isofunctional enzymes.
J. Biol. Chem.
261
1052-1057
1986
388067
Blattner F.R.,Burland V.D.,Plunkett G. III,Sofia H.J.,Daniels D.L.
Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes.
Nucleic Acids Res.
21
5408-5417
1993
388068
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
388069
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
388070
Cassan M.,Ronceray J.,Patte J.-C.
Nucleotide sequence of the promoter region of the E. coli lysC gene.
Nucleic Acids Res.
11
6157-6166
1983
388071
Marco-Marin C.,Ramon-Maiques S.,Tavarez S.,Rubio V.
Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase.
J. Mol. Biol.
334
459-476
2003
388072
Kotaka M.,Ren J.,Lockyer M.,Hawkins A.R.,Stammers D.K.
Structures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine.
J. Biol. Chem.
281
31544-31552
2006
