F0Q075 · F0Q075_PARA1

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 site41Mg2+ (UniProtKB | ChEBI)
Binding site245Mg2+ (UniProtKB | ChEBI)
Binding site247Mg2+ (UniProtKB | ChEBI)
Binding site281Mg2+ (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
    • Ordered locus names
      Acav_0030

Organism names

Accessions

  • Primary accession
    F0Q075

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain32-306Pyruvate carboxyltransferase
Region438-571Regulatory domain

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    571
  • Mass (Da)
    61,907
  • Last updated
    2011-05-03 v1
  • Checksum
    83717727DC4E4E4D
MMIAKPATKYQPTAIASLPDRTWPSRSITRAPIWLSTDLRDGNQALFEPMNGERKMRLFEELVRIGFKEIEVGFPAASQTDFDFVRRLIEENRIPDDVTIMVMTQSREDLIERTVQALQGAPRAIVHLYNATAPAWRRIVFGMNVSQVMAFIEHHVSLIKRLTDAQPATAWTLQYSPETFSATEPEVSLRACQTAITAWNAGPGRPIIINLPTTVENATPNVFADQIEWMHRRLAPREHIVLSVHPHNDRGTGVAAAELAMMAGADRVEGCLFGNGERCGNVDIVTLALNMYTQGVHPNLDFSDITHVARVAEECTSLPVHPRHPYAGDLVFTAFSGSHQDAIKKGFAAQDPAGLWEVPYLPIDPADLGRTYDSVIRVNSQSGKGGIAFLLERERGVVMPRRLQVEFSAVVQRATDTSEGEMDGDALWSLFSQTYIAAPAQGTPGALTLHGQRLDEDGQGIALDVTIDGVRQTLQGRGNGPIDATVDALGLPMRVDHYEERATGAGAGAQALAIVEAALEGVPGATFGVGLDHSIVNASVQAVVAVANRLIARRGAAAQAPAVREPAGTDF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002521
EMBL· GenBank· DDBJ
ADX43958.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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