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Sequence of DHAS_ECOLI

EC Number:1.2.1.11

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
aspartate-semialdehyde dehydrogenase
P0A9Q9
Escherichia coli (strain K12)
367
40018
Reaction
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
Other sequences found for EC No. 1.2.1.11

General information:

Sequence
show sequence in fasta format
  0 MKNVGFIGWR GMVGSVLMQR MVEERDFDAI RPVFFSTSQL GQAAPSFGGT TGTLQDAFDL
 60 EALKALDIIV TCQGGDYTNE IYPKLRESGW QGYWIDAASS LRMKDDAIII LDPVNQDVIT
120 DGLNNGIRTF VGGNCTVSLM LMSLGGLFAN DLVDWVSVAT YQAASGGGAR HMRELLTQMG
180 HLYGHVADEL ATPSSAILDI ERKVTTLTRS GELPVDNFGV PLAGSLIPWI DKQLDNGQSR
240 EEWKGQAETN KILNTSSVIP VDGLCVRVGA LRCHSQAFTI KLKKDVSIPT VEELLAAHNP
300 WAKVVPNDRE ITMRELTPAA VTGTLTTPVG RLRKLNMGPE FLSAFTVGDQ LLWGAAEPLR
360 RMLRQLA
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
152748
Haziza C.,Stragier P.,Patte J.-C.
Nucleotide sequence of the asd gene of Escherichia coli: absence of a typical attenuation signal.
EMBO J.
1
379-384
1982
152749
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
152750
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
152751
Biellmann J.F.,Eid P.,Hirth C.,Jornvall H.
Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Purification and general properties.
Eur. J. Biochem.
104
53-58
1980
152752
Link A.J.,Robison K.,Church G.M.
Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
Electrophoresis
18
1259-1313
1997
152753
Karsten W.E.,Viola R.E.
Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli.
Biochim. Biophys. Acta
1121
234-238
1992
152754
Chassagnole C.,Rais B.,Quentin E.,Fell D.A.,Mazat J.P.
An integrated study of threonine-pathway enzyme kinetics in Escherichia coli.
Biochem. J.
356
415-423
2001
152755
Alvarez E.,Ramon F.,Magan C.,Diez E.
L-cystine inhibits aspartate-beta-semialdehyde dehydrogenase by covalently binding to the essential 135Cys of the enzyme.
Biochim. Biophys. Acta
1696
23-29
2004
152756
Hadfield A.,Kryger G.,Ouyang J.,Petsko G.A.,Ringe D.,Viola R.
Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.
J. Mol. Biol.
289
991-1002
1999
152757
Hadfield A.,Shammas C.,Kryger G.,Ringe D.,Petsko G.A.,Ouyang J.,Viola R.E.
Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase.
Biochemistry
40
14475-14483
2001
152758
Nichols C.E.,Dhaliwal B.,Lockyer M.,Hawkins A.R.,Stammers D.K.
High-resolution structures reveal details of domain closure and 'half-of-sites-reactivity' in Escherichia coli aspartate beta-semialdehyde dehydrogenase.
J. Mol. Biol.
341
797-806
2004