Q1QUJ6 · Q1QUJ6_CHRSD

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 site40Mg2+ (UniProtKB | ChEBI)
Binding site244Mg2+ (UniProtKB | ChEBI)
Binding site246Mg2+ (UniProtKB | ChEBI)
Binding site280Mg2+ (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
      Csal_2515

Organism names

Accessions

  • Primary accession
    Q1QUJ6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain31-305Pyruvate carboxyltransferase
Region437-563Regulatory domain

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    563
  • Mass (Da)
    62,357
  • Last updated
    2006-05-16 v1
  • Checksum
    392F54A7AD118F45
MSRFDHRKYRPAPRVPAFDRQWPDRDLVAAPTWVSEDLRDGNQALLEPMSVEQKQRFWHQIIKVGIKEVMVGFPSASQPDYDFVRWLIEEDQIPDDVTIAVLVQCREHLIERTFESLVGAKRAIVHLYNSTSTVQRERVFEMDRAGIVDIAVQGASWVKERAARYPDVDWRFEYTPESFSSTEIDFSLDICEAVMDVWQPTPDNKCILNLPTTVEVAGPHHHADQIDYFCQHISRRDSVIISVHTHNDRGGAVAAAELAMLAGAERVEGTLLGNGERTGNMDIVTLAMNLYSQGIDPELDLSRPDEIIQVVQECTGIPMHPRHPWVGEMVYTAFSGSHQDAIRKSLKKQQDDEPWQVAYLPIDPRDIGRDYQAVIRVNSQSGKGGMAFLLERDYGISLPRWMALELAPAVQAVSETVNGELSSARIRDVLVETFTQCAPLTLSGYRLDREASEHLTVSLDDNGQALRLSGQGNGVISAFMAAWQQHTGRSVSVVDYSEHALGEGSDAVAIAFVQLNVDGQRVSGMAEDGDTVGASLKAVLSALNRAGHEAVSTGLASEASALA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000285
EMBL· GenBank· DDBJ
ABE59862.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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