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Sequence of ILVC_ECOLI

EC Number:1.1.1.86

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
ketol-acid reductoisomerase (NADP+)
P05793
Escherichia coli (strain K12)
491
54069
Reaction
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
Other sequences found for EC No. 1.1.1.86

EC Number:1.1.1.383

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
ketol-acid reductoisomerase [NAD(P)+]
P05793
Escherichia coli (strain K12)
491
54069
Reaction
(2R)-2,3-dihydroxy-3-methylbutanoate + NAD(P)+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.383

General information:

Sequence
show sequence in fasta format
  0 MANYFNTLNL RQQLAQLGKC RFMGRDEFAD GASYLQGKKV VIVGCGAQGL NQGLNMRDSG
 60 LDISYALRKE AIAEKRASWR KATENGFKVG TYEELIPQAD LVINLTPDKQ HSDVVRTVQP
120 LMKDGAALGY SHGFNIVEVG EQIRKDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE
180 NDPKGEGMAI AKAWAAATGG HRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCFDKL
240 VEEGTDPAYA EKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYALSE QLKEIMAPLF
300 QKHMDDIISG EFSSGMMADW ANDDKKLLTW REETGKTAFE TAPQYEGKIG EQEYFDKGVL
360 MIAMVKAGVE LAFETMVDSG IIEESAYYES LHELPLIANT IARKRLYEMN VVISDTAEYG
420 NYLFSYACVP LLKPFMAELQ PGDLGKAIPE GAVDNGQLRD VNEAIRSHAI EQVGKKLRGY
480 MTDMKRIAVA G
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
306703
Wek R.C.,Hatfield G.W.
Nucleotide sequence and in vivo expression of the ilvY and ilvC genes in Escherichia coli K12. Transcription from divergent overlapping promoters.
J. Biol. Chem.
261
2441-2450
1986
306704
Daniels D.L.,Plunkett G. III,Burland V.D.,Blattner F.R.
Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes.
Science
257
771-778
1992
306705
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
306706
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
306707
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
306708
Wek R.C.,Hatfield G.W.
Transcriptional activation at adjacent operators in the divergent-overlapping ilvY and ilvC promoters of Escherichia coli.
J. Mol. Biol.
203
643-663
1988
306709
Chunduru S.K.,Mrachko G.T.,Calvo K.C.
Mechanism of ketol acid reductoisomerase--steady-state analysis and metal ion requirement.
Biochemistry
28
486-493
1989
306710
Aulabaugh A.,Schloss J.V.
Oxalyl hydroxamates as reaction-intermediate analogues for ketol-acid reductoisomerase.
Biochemistry
29
2824-2830
1990
306711
Rane M.J.,Calvo K.C.
Reversal of the nucleotide specificity of ketol acid reductoisomerase by site-directed mutagenesis identifies the NADPH binding site.
Arch. Biochem. Biophys.
338
83-89
1997
306712
Tyagi R.,Lee Y.T.,Guddat L.W.,Duggleby R.G.
Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site.
FEBS J.
272
593-602
2005
306713
Bastian S.,Liu X.,Meyerowitz J.T.,Snow C.D.,Chen M.M.,Arnold F.H.
Engineered ketol-acid reductoisomerase and alcohol dehydrogenase enable anaerobic 2-methylpropan-1-ol production at theoretical yield in Escherichia coli.
Metab. Eng.
13
345-352
2011
306714
Tyagi R.,Duquerroy S.,Navaza J.,Guddat L.W.,Duggleby R.G.
The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution.
Protein Sci.
14
3089-3100
2005
306715
Wong S.H.,Lonhienne T.G.,Winzor D.J.,Schenk G.,Guddat L.W.
Bacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycle.
J. Mol. Biol.
424
168-179
2012