3-isopropylmalate dehydratase large subunit (P0A6A6)

Identification
Name:3-isopropylmalate dehydratase large subunit
Synonyms:
  • Alpha-IPM isomerase
  • IPMI
  • Isopropylmalate isomerase
Gene Name:leuC
Enzyme Class:
Biological Properties
General Function:Involved in 3-isopropylmalate dehydratase activity
Specific Function:Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate
Cellular Location:Not Available
SMPDB Pathways:
  • Leucine Biosynthesis PW000811
  • Operon: leucine biosynthesis PW001880
  • Secondary Metabolite: Leucine biosynthesis PW000980
  • Secondary Metabolites: Valine and I-leucine biosynthesis from pyruvate PW000978
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.03-Isopropylmalate ↔ 1.0Isopropylmaleate + 1.0Water
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb
1.0Isopropylmaleate + 1.0Water ↔ 1.02-Isopropylmalic acid
ReactionCard
1.0(R)-2-Methylmalate ↔ 1.0Thumb+1.0Thumb
1.0(R)-2-Methylmalate ↔ 1.0Citraconic acid + 1.0Water
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1.0Thumb+1.0Thumb ↔ 1.0Thumb
1.0Citraconic acid + 1.0Water ↔ 1.0D-Erythro-3-Methylmalate
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Isopropylmalic acid ↔ 1.0Isopropylmaleate + 1.0Water
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb
1.03-Isopropylmalate + 1.0Isopropylmaleate + 1.0Water ↔ 1.02-Isopropylmalic acid
ReactionCard
SMPDB Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Isopropylmalic acid → 1.0Water + 1.0Isopropylmaleate
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1.0Thumb+1.0Thumb → 1.0Thumb
1.0Isopropylmaleate + 1.0Water → 1.03-Isopropylmalate
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1.0Thumb+1.0Thumb → 1.0Citramalic acid
1.0Citraconic acid + 1.0Water → 1.0Citramalic acid
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EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.03-Isopropylmalate ↔ 1.0Isopropylmaleate + 1.0Water
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.03-Isopropylmalate → 1.0Isopropylmaleate + 1.0Water
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb
1.0Isopropylmaleate + 1.0Water → 1.02-Isopropylmalic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB004022-Isopropylmalic acidMetaboCard
ECMDB041583-IsopropylmalateMetaboCard
ECMDB21397Citraconic acidMetaboCard
ECMDB20137D-Erythro-3-MethylmalateMetaboCard
ECMDB12241IsopropylmaleateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
3-isopropylmalate dehydratase activity
4 iron, 4 sulfur cluster binding
binding
carbon-oxygen lyase activity
catalytic activity
hydro-lyase activity
iron-sulfur cluster binding
lyase activity
metal cluster binding
Process
branched chain family amino acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
leucine biosynthetic process
leucine metabolic process
metabolic process
Gene Properties
Blattner:b0072
Gene OrientationCounterclockwise
Centisome Percentage:1.71
Left Sequence End79464
Right Sequence End80864
Gene Sequence:
>1401 bp
ATGGCTAAGACGTTATACGAAAAATTGTTCGACGCTCACGTTGTGTACGAAGCCGAAAAC
GAAACCCCACTGTTATATATCGACCGCCACCTGGTGCATGAAGTGACCTCACCGCAGGCG
TTCGATGGTCTGCGCGCCCACGGTCGCCCGGTACGTCAGCCGGGCAAAACCTTCGCTACC
ATGGATCACAACGTCTCTACCCAGACCAAAGACATTAATGCCTGCGGTGAAATGGCGCGT
ATCCAGATGCAGGAACTGATCAAAAACTGCAAAGAATTTGGCGTCGAACTGTATGACCTG
AATCACCCGTATCAGGGGATCGTCCACGTAATGGGGCCGGAACAGGGCGTCACCTTGCCG
GGGATGACCATTGTCTGCGGCGACTCGCATACCGCCACCCACGGCGCGTTTGGCGCACTG
GCCTTTGGTATCGGCACTTCCGAAGTTGAACACGTACTGGCAACGCAAACCCTGAAACAG
GGCCGCGCAAAAACCATGAAAATTGAAGTCCAGGGCAAAGCCGCGCCGGGCATTACCGCA
AAAGATATCGTGCTGGCAATTATCGGTAAAACCGGTAGCGCAGGCGGCACCGGGCATGTG
GTGGAGTTTTGCGGCGAAGCAATCCGTGATTTAAGCATGGAAGGTCGTATGACCCTGTGC
AATATGGCAATCGAAATGGGCGCAAAAGCCGGTCTGGTTGCACCGGACGAAACCACCTTT
AACTATGTCAAAGGCCGTCTGCATGCGCCGAAAGGCAAAGATTTCGACGACGCCGTTGCC
TACTGGAAAACCCTGCAAACCGACGAAGGCGCAACTTTCGATACCGTTGTCACTCTGCAA
GCAGAAGAAATTTCACCGCAGGTCACCTGGGGCACCAATCCCGGCCAGGTGATTTCCGTG
AACGACAATATTCCCGATCCGGCTTCGTTTGCCGATCCGGTTGAACGCGCGTCGGCAGAA
AAAGCGCTGGCCTATATGGGGCTGAAACCGGGTATTCCGCTGACCGAAGTGGCTATCGAC
AAAGTGTTTATCGGTTCCTGTACCAACTCGCGCATTGAAGATTTACGCGCGGCAGCGGAG
ATCGCCAAAGGGCGAAAAGTCGCGCCAGGCGTGCAGGCACTGGTGGTTCCCGGCTCTGGC
CCGGTAAAAGCCCAGGCGGAAGCGGAAGGTCTGGATAAAATCTTTATTGAAGCCGGTTTT
GAATGGCGCTTGCCTGGCTGCTCAATGTGTCTGGCGATGAACAACGACCGTCTGAATCCG
GGCGAACGTTGTGCCTCCACCAGCAACCGTAACTTTGAAGGCCGCCAGGGGCGCGGCGGG
CGCACGCATCTGGTCAGCCCGGCAATGGCTGCCGCTGCTGCTGTGACCGGACATTTCGCC
GACATTCGCAACATTAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:466
Protein Molecular Weight:49882
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>3-isopropylmalate dehydratase large subunit
MAKTLYEKLFDAHVVYEAENETPLLYIDRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFAT
MDHNVSTQTKDINACGEMARIQMQELIKNCKEFGVELYDLNHPYQGIVHVMGPEQGVTLP
GMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGKAAPGITA
KDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTF
NYVKGRLHAPKGKDFDDAVAYWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISV
NDNIPDPASFADPVERASAEKALAYMGLKPGIPLTEVAIDKVFIGSCTNSRIEDLRAAAE
IAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNP
GERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRNIK
References
External Links:
ResourceLink
Uniprot ID:P0A6A6
Uniprot Name:LEUC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674316
Ecogene ID:EG11576
Ecocyc:EG11576
ColiBase:b0072
Kegg Gene:b0072
EchoBASE ID:EB1536
CCDB:LEUC_ECOLI
BacMap:16128066
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
  • Chen, H., Lawrence, C. B., Bryan, S. K., Moses, R. E. (1990). "Aphidicolin inhibits DNA polymerase II of Escherichia coli, an alpha-like DNA polymerase." Nucleic Acids Res 18:7185-7186. Pubmed: 2124684
  • 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
  • Kirino, H., Aoki, M., Aoshima, M., Hayashi, Y., Ohba, M., Yamagishi, A., Wakagi, T., Oshima, T. (1994). "Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus." Eur J Biochem 220:275-281. Pubmed: 8119295
  • 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
  • Tonella, L., Walsh, B. J., Sanchez, J. C., Ou, K., Wilkins, M. R., Tyler, M., Frutiger, S., Gooley, A. A., Pescaru, I., Appel, R. D., Yan, J. X., Bairoch, A., Hoogland, C., Morch, F. S., Hughes, G. J., Williams, K. L., Hochstrasser, D. F. (1998). "'98 Escherichia coli SWISS-2DPAGE database update." Electrophoresis 19:1960-1971. Pubmed: 9740056
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901