3-isopropylmalate dehydrogenase
Details
- Name
- 3-isopropylmalate dehydrogenase
- Synonyms
- 1.1.1.85
- 3-IPM-DH
- Beta-IPM dehydrogenase
- IMDH
- Gene Name
- leuB
- Organism
- Acidithiobacillus ferrooxidans
- Amino acid sequence
>lcl|BSEQ0011210|3-isopropylmalate dehydrogenase MKKIAIFAGDGIGPEIVAAARQVLDAVDQAAHLGLRCTEGLVGGAALDASDDPLPAASLQ LAMAADAVILGAVGGPRWDAYPPAKRPEQGLLRLRKGLDLYANLRPAQIFPQLLDASPLR PELVRDVDILVVRELTGDIYFGQPRGLEVIDGKRRGFNTMVYDEDEIRRIAHVAFRAAQG RRKQLCSVDKANVLETTRLWREVVTEVARDYPDVRLSHMYVDNAAMQLIRAPAQFDVLLT GNMFGDILSDEASQLTGSIGMLPSASLGEGRAMYEPIHGSAPDIAGQDKANPLATILSVA MMLRHSLNAEPWAQRVEAAVQRVLDQGLRTADIAAPGTPVIGTKAMGAAVVNALNLKD
- Number of residues
- 358
- Molecular Weight
- 38461.785
- Theoretical pI
- 5.46
- GO Classification
- Functions3-isopropylmalate dehydrogenase activity / magnesium ion binding / NAD bindingProcessesleucine biosynthetic processComponentscytoplasm
- General Function
- Nad binding
- Specific Function
- Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Can also use D-malate and L-malate, with lower efficiency.
- Pfam Domain Function
- Iso_dh (PF00180)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0003368|1077 bp ATGAAAAAAATAGCCATCTTCGCCGGTGACGGCATCGGTCCGGAAATCGTGGCAGCCGCC CGGCAAGTGCTGGATGCAGTGGATCAGGCCGCCCACCTTGGCCTGCGTTGTACCGAAGGC CTGGTGGGCGGGGCCGCGCTGGATGCCAGCGATGATCCCTTGCCGGCGGCTTCTTTGCAG TTGGCCATGGCGGCGGATGCAGTCATTTTGGGTGCGGTGGGCGGCCCCCGCTGGGACGCG TATCCACCCGCCAAGCGCCCGGAACAGGGACTGCTGCGTCTGCGCAAAGGCCTGGACCTT TATGCGAACCTGCGTCCCGCACAGATTTTTCCGCAGTTGCTGGATGCCTCGCCCCTACGC CCGGAGCTGGTGCGCGACGTCGATATCCTGGTGGTGCGCGAGCTGACCGGGGATATCTAC TTCGGCCAGCCACGCGGTCTGGAGGTCATCGACGGCAAGCGCCGCGGCTTTAACACCATG GTCTATGACGAGGATGAAATTCGCCGTATCGCTCATGTGGCCTTCCGCGCTGCCCAGGGG CGTCGCAAGCAGTTGTGCTCGGTGGACAAGGCCAATGTCCTGGAGACCACGCGTCTGTGG CGCGAGGTGGTCACCGAGGTAGCGCGGGACTATCCCGATGTGCGGCTCAGCCACATGTAT GTGGATAATGCCGCCATGCAACTGATCCGCGCCCCGGCACAGTTCGACGTGCTGTTGACC GGCAATATGTTCGGCGACATTCTTTCCGACGAGGCCAGTCAATTGACTGGTTCCATCGGT ATGCTGCCCTCGGCCTCGCTGGGCGAGGGACGGGCGATGTATGAACCCATCCATGGCTCG GCGCCGGATATTGCCGGGCAGGACAAGGCGAATCCCCTGGCCACGATTCTATCCGTGGCG ATGATGCTGCGGCATTCCCTCAACGCCGAACCCTGGGCGCAACGGGTGGAGGCGGCAGTG CAGCGAGTGCTGGATCAGGGCCTGCGCACTGCGGATATTGCAGCGCCGGGAACGCCGGTA ATCGGCACCAAAGCCATGGGTGCCGCGGTGGTCAACGCCCTGAACCTGAAGGATTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q56268 UniProtKB Entry Name LEU3_ACIFR GenBank Protein ID 414355 GenBank Gene ID D14585 - General References
- Kawaguchi H, Inagaki K, Kuwata Y, Tanaka H, Tano T: 3-Isopropylmalate dehydrogenase from chemolithoautotroph Thiobacillus ferrooxidans: DNA sequence, enzyme purification, and characterization. J Biochem. 1993 Sep;114(3):370-7. [Article]
- Imada K, Inagaki K, Matsunami H, Kawaguchi H, Tanaka H, Tanaka N, Namba K: Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism. Structure. 1998 Aug 15;6(8):971-82. [Article]