A0A377DXM2 · A0A377DXM2_ECOLX

  • Protein
    Multifunctional fusion protein
  • Gene
    leuA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
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.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 1 Mg2+ or Mn2+ ion per subunit.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site14Mn2+ (UniProtKB | ChEBI)
Binding site202Mn2+ (UniProtKB | ChEBI)
Binding site204Mn2+ (UniProtKB | ChEBI)
Binding site238Mn2+ (UniProtKB | ChEBI)
Binding site602-615NAD+ (UniProtKB | ChEBI)
Binding site623substrate
Binding site633substrate
Binding site662substrate
Site669Important for catalysis
Site719Important for catalysis
Binding site751Mg2+ (UniProtKB | ChEBI)
Binding site751substrate
Binding site775Mg2+ (UniProtKB | ChEBI)
Binding site779Mg2+ (UniProtKB | ChEBI)
Binding site809-821NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function2-isopropylmalate synthase activity
Molecular Function3-isopropylmalate dehydrogenase activity
Molecular Functionacetyl-CoA C-acetyltransferase activity
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular FunctionNAD binding
Biological ProcessL-leucine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    3-isopropylmalate dehydrogenase
  • EC number
  • Alternative names
    • 3-IPM-DH
    • Beta-IPM dehydrogenase
      (IMDH
      )
  • Recommended name
    2-isopropylmalate synthase
  • EC number
  • Alternative names
    • Alpha-IPM synthase
    • Alpha-isopropylmalate synthase

Gene names

    • Name
      leuA
    • Synonyms
      leuB
    • ORF names
      NCTC8500_04662

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NCTC8500
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A377DXM2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain5-267Pyruvate carboxyltransferase
Region392-887Regulatory domain

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    887
  • Mass (Da)
    96,857
  • Last updated
    2018-11-07 v1
  • MD5 Checksum
    4FCED1B17EDE6649D112B4ABD24206F7
MSQQVIIFDTTLRDGEQALQASLSVKEKLQIALALERMGVDVMEVGFPVSSPGDFESVQTIARQVKNSRVCALARCVEKDIDVAAESLKVAEAFRIHTFIATSPMHIATKLRSTLDEVIERAIYMVKRARNYTDDVEFSCEDAGRTPIADLARVVEAAINAGATTINIPDTVGYTMPFEFAGIISGLYERVPNIDKAIISVHTHDDLGLAVGNSLAAVHAGARQVEGAMNGIGERAGNCSLEEVIMAIKVRKDILNVHTAINHQEIWRTSQLVSQICNMPIPANKAIVGSGAFAHSSGIHQDGVLKNRENYEIMTPESIGLNQIQLNLTSRSGRAAVKHRMDEMGYKESEYNLDNLYDAFLKLADKKGQVFDYDLEALAFIGKQQEEPEHFRLDYFSVQSGSNDIATAAVKLACGEEVKAEAANGNGPVDAVYQAINRITEYNVELVKYSLTAKGHGKDALGQVDIVANYNGRRFHGVGLATDIVESSAKAMVHVSEQYLACRRSRKRVATQSSTQRKQQGNRVMSKNYHIAVLPGDGIGPEVMTQALKVLDAVRNRFAMRITTSHYDVGGAAIDNHGQPLPPATVEGCEQADAVLFGSVGGPKWEHLPPDQQPERGALLPLRKHFKLFSNLRPAKLYQGLEAFCPLRADIAANGFDILCVRELTGGIYFGQPKGREGSGQYEKAFDTEVYHRFEIERIARIAFESARKRRHKVTSIDKANVLQSSILWREIVNEIATEYPDVELAHMYIDNATMQLIKDPSQFDVLLCSNLFGDILSDECAMITGSMGMLPSASLNEQGFGLYEPAGGSAPDIAGKNIANPIAQILSLALLLRYSLDADDAACAIERAINRALEEGIRTGDLARGAAAVSTDEMGDIIARYVAEGV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UGFG01000001
EMBL· GenBank· DDBJ
STM40795.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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