| Identification |
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| Name: | Ketol-acid reductoisomerase |
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| Synonyms: | - Acetohydroxy-acid isomeroreductase
- Alpha-keto-beta-hydroxylacil reductoisomerase
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| Gene Name: | ilvC |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in oxidation-reduction process |
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| Specific Function: | (R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH |
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| Cellular Location: | Not Available |
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| SMPDB Pathways: | - Pantothenate and CoA biosynthesis PW000828
- Secondary Metabolites: Valine and I-leucine biosynthesis from pyruvate PW000978
- Valine Biosynthesis PW000812
- isoleucine biosynthesis PW000818
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| KEGG Pathways: | - Metabolic pathways eco01100
- Pantothenate and CoA biosynthesis ec00770
- Valine, leucine and isoleucine biosynthesis ec00290
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| KEGG Reactions: | |
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| SMPDB Reactions: | |
1.0 | + | 1.0 | + | 1.0NADPH | + | 1.0 | → | 1.0 | + | 1.0 |
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1.0 | + | 1.0NADPH | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 |
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1.02-dehydropantoate | + | 1.0NADPH | + | 1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0(R)-pantoate | + | 1.0 |
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1.0 | + | 1.0 | + | 1.0NADPH | + | 1.0 | → | 1.0 | + | 1.0 |
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| EcoCyc Reactions: | |
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| Complex Reactions: | |
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| Metabolites: | |
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| GO Classification: | | Function |
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| binding | | catalytic activity | | ketol-acid reductoisomerase activity | | NADP or NADPH binding | | nucleotide binding | | oxidoreductase activity | | oxidoreductase activity, acting on CH-OH group of donors | | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | | Process |
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| branched chain family amino acid biosynthetic process | | cellular amino acid and derivative metabolic process | | cellular amino acid biosynthetic process | | cellular amino acid metabolic process | | cellular metabolic process | | metabolic process | | oxidation reduction |
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| Gene Properties |
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| Blattner: | b3774 |
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| Gene Orientation | Clockwise |
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| Centisome Percentage: | 85.26 |
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| Left Sequence End | 3955993 |
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| Right Sequence End | 3957468 |
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| Gene Sequence: | >1476 bp
ATGAATACACAACAATTGGCAAAACTGCGTTCCATCGTGCCCGAAATGCGTCGCGTTCGG
CACATACATTTTGTCGGCATTGGTGGTGCCGGTATGGGCGGTATTGCCGAAGTTCTGGCC
AATGAAGGTTATCAGATCAGTGGTTCCGATTTAGCGCCAAATCCGGTCACGCAGCAGTTA
ATGAATCTGGGTGCGACGATTTATTTCAACCATCGCCCGGAAAACGTACGTGATGCCAGC
GTGGTCGTTGTTTCCAGCGCGATTTCTGCCGATAACCCGGAAATTGTCGCCGCTCATGAA
GCGCGTATTCCGGTGATCCGTCGTGCCGAAATGCTGGCTGAGTTAATGCGTTTTCGTCAT
GGCATCGCCATTGCCGGAACGCACGGCAAAACGACAACCACCGCGATGGTTTCCAGCATC
TACGCAGAAGCGGGGCTCGACCCAACCTTCGTTAACGGCGGGCTGGTAAAAGCGGCGGGG
GTTCATGCGCGTTTGGGGCATGGTCGGTACCTGATTGCCGAAGCAGATGAGAGTGATGCA
TCGTTCCTGCATCTGCAACCGATGGTGGCGATTGTCACCAATATCGAAGCCGACCACATG
GATACCTACCAGGGCGACTTTGAGAATTTAAAACAGACTTTTATTAATTTTCTGCACAAC
CTGCCGTTTTACGGTCGTGCGGTGATGTGTGTTGATGATCCGGTGATCCGCGAATTGTTA
CCGCGAGTGGGGCGTCAGACCACGACTTACGGCTTCAGCGAAGATGCCGACGTGCGTGTA
GAAGATTATCAGCAGATTGGCCCGCAGGGGCACTTTACGCTGCTGCGCCAGGACAAAGAG
CCGATGCGCGTCACCCTGAATGCGCCAGGTCGTCATAACGCGCTGAACGCCGCAGCTGCG
GTTGCGGTTGCTACGGAAGAGGGCATTGACGACGAGGCTATTTTGCGGGCGCTTGAAAGC
TTCCAGGGGACTGGTCGCCGTTTTGATTTCCTCGGTGAATTCCCGCTGGAGCCAGTGAAT
GGTAAAAGCGGTACGGCAATGCTGGTCGATGACTACGGCCACCACCCGACGGAAGTGGAC
GCCACCATTAAAGCGGCGCGCGCAGGCTGGCCGGATAAAAACCTGGTAATGCTGTTTCAG
CCGCACCGTTTTACCCGTACGCGCGACCTGTATGATGATTTCGCCAATGTGCTGACGCAG
GTTGATACCCTGTTGATGCTGGAAGTGTATCCGGCTGGCGAAGCGCCAATTCCGGGAGCG
GACAGCCGTTCGCTGTGTCGCACAATTCGTGGACGTGGGAAAATTGATCCCATTCTGGTG
CCGGATCCGGCGCGGGTAGCCGAGATGCTGGCACCGGTATTAACCGGTAACGACCTGATT
CTCGTTCAGGGGGCTGGTAATATTGGAAAAATTGCCCGTTCTTTAGCTGAAATCAAACTG
AAGCCGCAAACTCCGGAGGAAGAACAACATGACTGA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 491 |
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| Protein Molecular Weight: | 54069 |
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| Protein Theoretical pI: | 5 |
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| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Ketol-acid reductoisomerase
MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSG
LDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRTVQP
LMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPE
NDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKL
VEEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLF
QKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVL
MIAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYG
NYLFSYACVPLLKPFMAELQPGDLGKAIPEGAVDNGQLRDVNEAIRSHAIEQVGKKLRGY
MTDMKRIAVAG |
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| References |
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| External Links: | |
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| General Reference: | - Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
- Wek, R. C., Hatfield, G. W. (1986). "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. Pubmed: 3003115
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