Dihydroxy-acid dehydratase (P05791)

Identification
Name:Dihydroxy-acid dehydratase
Synonyms:
  • DAD
Gene Name:ilvD
Enzyme Class:
Biological Properties
General Function:Involved in metabolic process
Specific Function:2,3-dihydroxy-3-methylbutanoate = 3-methyl-2- oxobutanoate + H(2)O
Cellular Location:Not Available
SMPDB Pathways:
  • Pantothenate and CoA biosynthesis PW000828
  • Secondary Metabolites: Valine and I-leucine biosynthesis from pyruvate PW000978
  • Valine Biosynthesis PW000812
  • isoleucine biosynthesis PW000818
KEGG Pathways:
KEGG Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0(R)-2,3-Dihydroxy-isovalerate → 1.0alpha-Ketoisovaleric acid + 1.0Water
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb
1.0(R) 2,3-Dihydroxy-3-methylvalerate → 1.03-Methyl-2-oxovaleric acid + 1.0Water
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.02,3-Dihydroxyisovaleric acid ↔ 1.0alpha-Ketoisovaleric acid + 1.0Water + 1.0a-Ketoisovaleric acid
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0(R)-2,3-Dihydroxy-isovalerate ↔ 1.0alpha-Ketoisovaleric acid + 1.0Water
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0(R) 2,3-Dihydroxy-3-methylvalerate ↔ 1.03-Methyl-2-oxovaleric acid + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0(R)-2,3-Dihydroxy-isovalerate → 1.0Water + 1.0Isovaleric acid
ReactionCard
1.0Thumb → 1.0Thumb+1.03-Methyl-2-oxovaleric acid+1.0Thumb
1.0(R) 2,3-Dihydroxy-3-methylvalerate → 1.0Water + 1.03-Methyl-2-oxovaleric acid + 1.03-Methyl-2-oxovaleric acid
ReactionCard
1.0Thumb ↔ 2.0Thumb+1.0Thumb
1.02,3-Dihydroxyisovaleric acid ↔ 2.0a-Ketoisovaleric acid + 1.0Water
ReactionCard
EcoCyc Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0(R)-2,3-Dihydroxy-isovalerate → 1.0alpha-Ketoisovaleric acid + 1.0Water
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb
1.0(R) 2,3-Dihydroxy-3-methylvalerate → 1.03-Methyl-2-oxovaleric acid + 1.0Water
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.02,3-Dihydroxyisovaleric acid → 1.0a-Ketoisovaleric acid + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB12140(R) 2,3-Dihydroxy-3-methylvalerateMetaboCard
ECMDB04059(R)-2,3-Dihydroxy-isovalerateMetaboCard
ECMDB214802,3-Dihydroxyisovaleric acidMetaboCard
ECMDB040912-Keto-3-methyl-valerateMetaboCard
ECMDB004913-Methyl-2-oxovaleric acidMetaboCard
ECMDB00019a-Ketoisovaleric acidMetaboCard
ECMDB04092alpha-Ketoisovaleric acidMetaboCard
ECMDB00718Isovaleric acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
carbon-oxygen lyase activity
catalytic activity
dihydroxy-acid dehydratase activity
hydro-lyase activity
lyase activity
Process
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
Gene Properties
Blattner:b3771
Gene OrientationClockwise
Centisome Percentage:85.17
Left Sequence End3951501
Right Sequence End3953351
Gene Sequence:
>1851 bp
ATGCCTAAGTACCGTTCCGCCACCACCACTCATGGTCGTAATATGGCGGGTGCTCGTGCG
CTGTGGCGCGCCACCGGAATGACCGACGCCGATTTCGGTAAGCCGATTATCGCGGTTGTG
AACTCGTTCACCCAATTTGTACCGGGTCACGTCCATCTGCGCGATCTCGGTAAACTGGTC
GCCGAACAAATTGAAGCGGCTGGCGGCGTTGCCAAAGAGTTCAACACCATTGCGGTGGAT
GATGGGATTGCCATGGGCCACGGGGGGATGCTTTATTCACTGCCATCTCGCGAACTGATC
GCTGATTCCGTTGAGTATATGGTCAACGCCCACTGCGCCGACGCCATGGTCTGCATCTCT
AACTGCGACAAAATCACCCCGGGGATGCTGATGGCTTCCCTGCGCCTGAATATTCCGGTG
ATCTTTGTTTCCGGCGGCCCGATGGAGGCCGGGAAAACCAAACTTTCCGATCAGATCATC
AAGCTCGATCTGGTTGATGCGATGATCCAGGGCGCAGACCCGAAAGTATCTGACTCCCAG
AGCGATCAGGTTGAACGTTCCGCGTGTCCGACCTGCGGTTCCTGCTCCGGGATGTTTACC
GCTAACTCAATGAACTGCCTGACCGAAGCGCTGGGCCTGTCGCAGCCGGGCAACGGCTCG
CTGCTGGCAACCCACGCCGACCGTAAGCAGCTGTTCCTTAATGCTGGTAAACGCATTGTT
GAATTGACCAAACGTTATTACGAGCAAAACGACGAAAGTGCACTGCCGCGTAATATCGCC
AGTAAGGCGGCGTTTGAAAACGCCATGACGCTGGATATCGCGATGGGTGGATCGACTAAC
ACCGTACTTCACCTGCTGGCGGCGGCGCAGGAAGCGGAAATCGACTTCACCATGAGTGAT
ATCGATAAGCTTTCCCGCAAGGTTCCACAGCTGTGTAAAGTTGCGCCGAGCACCCAGAAA
TACCATATGGAAGATGTTCACCGTGCTGGTGGTGTTATCGGTATTCTCGGCGAACTGGAT
CGCGCGGGGTTACTGAACCGTGATGTGAAAAACGTACTTGGCCTGACGTTGCCGCAAACG
CTGGAACAATACGACGTTATGCTGACCCAGGATGACGCGGTAAAAAATATGTTCCGCGCA
GGTCCTGCAGGCATTCGTACCACACAGGCATTCTCGCAAGATTGCCGTTGGGATACGCTG
GACGACGATCGCGCCAATGGCTGTATCCGCTCGCTGGAACACGCCTACAGCAAAGACGGC
GGCCTGGCGGTGCTCTACGGTAACTTTGCGGAAAACGGCTGCATCGTGAAAACGGCAGGC
GTCGATGACAGCATCCTCAAATTCACCGGCCCGGCGAAAGTGTACGAAAGCCAGGACGAT
GCGGTAGAAGCGATTCTCGGCGGTAAAGTTGTCGCCGGAGATGTGGTAGTAATTCGCTAT
GAAGGCCCGAAAGGCGGTCCGGGGATGCAGGAAATGCTCTACCCAACCAGCTTCCTGAAA
TCAATGGGTCTCGGCAAAGCCTGTGCGCTGATCACCGACGGTCGTTTCTCTGGTGGCACC
TCTGGTCTTTCCATCGGCCACGTCTCACCGGAAGCGGCAAGCGGCGGCAGCATTGGCCTG
ATTGAAGATGGTGACCTGATCGCTATCGACATCCCGAACCGTGGCATTCAGTTACAGGTA
AGCGATGCCGAACTGGCGGCGCGTCGTGAAGCGCAGGACGCTCGAGGTGACAAAGCCTGG
ACGCCGAAAAATCGTGAACGTCAGGTCTCCTTTGCCCTGCGTGCTTATGCCAGCCTGGCA
ACCAGCGCCGACAAAGGCGCGGTGCGCGATAAATCGAAACTGGGGGGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:616
Protein Molecular Weight:65531
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Dihydroxy-acid dehydratase
MPKYRSATTTHGRNMAGARALWRATGMTDADFGKPIIAVVNSFTQFVPGHVHLRDLGKLV
AEQIEAAGGVAKEFNTIAVDDGIAMGHGGMLYSLPSRELIADSVEYMVNAHCADAMVCIS
NCDKITPGMLMASLRLNIPVIFVSGGPMEAGKTKLSDQIIKLDLVDAMIQGADPKVSDSQ
SDQVERSACPTCGSCSGMFTANSMNCLTEALGLSQPGNGSLLATHADRKQLFLNAGKRIV
ELTKRYYEQNDESALPRNIASKAAFENAMTLDIAMGGSTNTVLHLLAAAQEAEIDFTMSD
IDKLSRKVPQLCKVAPSTQKYHMEDVHRAGGVIGILGELDRAGLLNRDVKNVLGLTLPQT
LEQYDVMLTQDDAVKNMFRAGPAGIRTTQAFSQDCRWDTLDDDRANGCIRSLEHAYSKDG
GLAVLYGNFAENGCIVKTAGVDDSILKFTGPAKVYESQDDAVEAILGGKVVAGDVVVIRY
EGPKGGPGMQEMLYPTSFLKSMGLGKACALITDGRFSGGTSGLSIGHVSPEAASGGSIGL
IEDGDLIAIDIPNRGIQLQVSDAELAARREAQDARGDKAWTPKNRERQVSFALRAYASLA
TSADKGAVRDKSKLGG
References
External Links:
ResourceLink
Uniprot ID:P05791
Uniprot Name:ILVD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676276
Ecogene ID:EG10496
Ecocyc:EG10496
ColiBase:b3771
Kegg Gene:b3771
EchoBASE ID:EB0491
CCDB:ILVD_ECOLI
BacMap:49176404
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
  • Brown, O. R., Smyk-Randall, E., Draczynska-Lusiak, B., Fee, J. A. (1995). "Dihydroxy-acid dehydratase, a [4Fe-4S] cluster-containing enzyme in Escherichia coli: effects of intracellular superoxide dismutase on its inactivation by oxidant stress." Arch Biochem Biophys 319:10-22. Pubmed: 7771772
  • Cox, J. L., Cox, B. J., Fidanza, V., Calhoun, D. H. (1987). "The complete nucleotide sequence of the ilvGMEDA cluster of Escherichia coli K-12." Gene 56:185-198. Pubmed: 3315862
  • 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
  • Flint, D. H., Emptage, M. H., Finnegan, M. G., Fu, W., Johnson, M. K. (1993). "The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase." J Biol Chem 268:14732-14742. Pubmed: 8325851
  • 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
  • Kuramitsu, S., Ogawa, T., Ogawa, H., Kagamiyama, H. (1985). "Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence." J Biochem 97:993-999. Pubmed: 3897211
  • Lawther, R. P., Wek, R. C., Lopes, J. M., Pereira, R., Taillon, B. E., Hatfield, G. W. (1987). "The complete nucleotide sequence of the ilvGMEDA operon of Escherichia coli K-12." Nucleic Acids Res 15:2137-2155. Pubmed: 3550695
  • Riley, M., Abe, T., Arnaud, M. B., Berlyn, M. K., Blattner, F. R., Chaudhuri, R. R., Glasner, J. D., Horiuchi, T., Keseler, I. M., Kosuge, T., Mori, H., Perna, N. T., Plunkett, G. 3rd, Rudd, K. E., Serres, M. H., Thomas, G. H., Thomson, N. R., Wishart, D., Wanner, B. L. (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34:1-9. Pubmed: 16397293