ilvD [2017-8-11 16:0:3]

dihydroxy-acid dehydratase (2,3-dihydroxy-3-methylbutanoate, 2,3-dihydroxy-3-methylpentanoate)

locus: BSU21870

pI: 5.32

mw: 59.38 kDa

protein length: 558 aa

gene length: 1674 bp

function: biosynthesis of branched-chain amino acids

product: dihydroxy-acid dehydratase (2,3-dihydroxy-3-methylbutanoate, 2,3-dihydroxy-3-methylpentanoate)

essential: no

ec: 4.2.1.9

synonyms

Genomic Context

categories

• [category|SW 2|Metabolism] → [category|SW 2.3|Amino acid/ nitrogen metabolism] → [category|SW 2.3.1|Biosynthesis/ acquisition of amino acids] → [category|SW 2.3.1.12|Biosynthesis/ acquisition of branched-chain amino acids]

Gene

Coordinates: 2,300,762 → 2,302,438

The protein

Catalyzed reaction/ biological activity

• 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H₂O (according to Swiss-Prot)

Structure

• [PDB|2GP4] (apo form of 6-phosphogluconate dehydratase from ''Shewanella oneidensis'', 33% identity)

additional information

• belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]

Expression and Regulation

Operons

• genes: [gene|8D08E5F1EC57A9B3EFFCD7D12D8F16B3B28AEFF0|ilvD]
  description: [Pubmed|15060025]

  regulatory mechanism

  • [protein|90ACE0DECA58D3C1A55E135120F7A0C1C920571C|CodY]: repression, [pubmed|12618455] [pubmed|18083814], in [regulon|90ACE0DECA58D3C1A55E135120F7A0C1C920571C|CodY regulon]

  regulation

  • repressed by casamino acids [Pubmed|12107147]

Biological materials

lacZ fusion

• pGP522 (in [protein|search|pAC5]), pGP235 (in [protein|search|pAC5]), both available in [SW|Jörg Stülke]'s lab; a series of promoter deletions in [protein|search|pAC6] is available in [SW|Jörg Stülke]'s lab

References

• 18083814,12618455,15060025,12107147,24163341,15378759,26220295