A0A076JGB7 · A0A076JGB7_BIFAD

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).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site81Mg2+ (UniProtKB | ChEBI)
Binding site285Mg2+ (UniProtKB | ChEBI)
Binding site287Mg2+ (UniProtKB | ChEBI)
Binding site321Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function2-isopropylmalate synthase activity
Molecular Functionacetyl-CoA C-acetyltransferase activity
Molecular Functionmagnesium ion binding
Biological ProcessL-leucine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    2-isopropylmalate synthase
  • EC number
  • Alternative names
    • Alpha-IPM synthase
    • Alpha-isopropylmalate synthase

Gene names

    • Name
      leuA
    • ORF names
      AL0462_0144
      , BIFAD42_07280
      , DWX79_00235
      , ERS852382_01180
      , F3K97_00785
      , QEP23_01210

Organism names

  • Taxonomic identifier
  • Strains
    • 2789STDY5608824
    • AL46-2
    • AF21-27
    • ZJ2
    • 4-2
    • IVS-1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A076JGB7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain72-346Pyruvate carboxyltransferase
Region488-636Regulatory domain

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    636
  • Mass (Da)
    70,147
  • Last updated
    2014-10-29 v1
  • Checksum
    DA363EABDA1C181C
MGQDQSSVFDLAAVAAASNGGNNDPLLPPARYIGAPQKPSKMPYNKYVAYDKQVPFDFPERTWPGKRLQRAPRWCSVDLRDGNQALVNPMDSERKLRFWNLLVSMGFKEIEVGFPSASETDYDFIRMLIERELIPDDVTIVVLTQAREHLIRKTYECLKGAKRAVVHFYNSVSVLQREVVFRKDKAGIKKLATDAATLCKELEGEAKGIDLYYEYSPESFTGTEPEYAVEVCNAVIDVIKPTPEHPMIINLPATVEMTTPNVFADEVEYVSNHLVPRDAVVLSLHPHNDEGMGVAATELAVLAGADRVEGCLLGNGERTGNVDLVTLGLNFLTQGIDPQIDYSNVPEIRKTVEYCNQIKISERHPYAGNFVFTAFSGSHQDAIKKGLEARQVAADRAGADLDSFVWLVPYLPIDPKDIGRSYEAIIRVNSQSGKGGMAYLLKTNHNLDLPKRLQVEFEKVVQNYADETKKEVKDEDIWRLFKDEYLPVEESGATAAGVVVGDSKDETLKQWGRLKLLKVSVSSGEDGSDTVLKARILDRGVNVGVDEPVEREVSGIGNGPIAAFLNAVSNFGIEASVMDYVEHTMSVGTDAMAASYVECQIGEEDNTSIVWGVGIDTSIVTSSLKAIISAINRSER

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CYYI01000003
EMBL· GenBank· DDBJ
CUN71063.1
EMBL· GenBank· DDBJ
Genomic DNA
BPPZ01000003
EMBL· GenBank· DDBJ
GJD13744.1
EMBL· GenBank· DDBJ
Genomic DNA
LNKH01000003
EMBL· GenBank· DDBJ
OSG97601.1
EMBL· GenBank· DDBJ
Genomic DNA
CP047129
EMBL· GenBank· DDBJ
QHB61944.1
EMBL· GenBank· DDBJ
Genomic DNA
QRVT01000001
EMBL· GenBank· DDBJ
RGS65581.1
EMBL· GenBank· DDBJ
Genomic DNA
CP123050
EMBL· GenBank· DDBJ
WGJ17736.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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