Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A949QG50 · A0A949QG50_CHLSQ

  • Protein
    2-isopropylmalate synthase
  • Gene
    leuA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site38Mg2+ (UniProtKB | ChEBI)
Binding site242Mg2+ (UniProtKB | ChEBI)
Binding site244Mg2+ (UniProtKB | ChEBI)
Binding site278Mg2+ (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
      JZU70_11140

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LaCa_MAG_11
  • Taxonomic lineage
    Bacteria > Chlorobiota > Chlorobiia > Chlorobiales > Chlorobiaceae > Chlorobium/Pelodictyon group > Chlorobium

Accessions

  • Primary accession
    A0A949QG50

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain29-303Pyruvate carboxyltransferase
Region437-558Regulatory domain

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    558
  • Mass (Da)
    61,970
  • Last updated
    2023-02-22 v1
  • MD5 Checksum
    3957E4B3D757A6F4C3D5C2293C53BAE7
MMNYKKYAPYPQVAISDRSWPDKSITKAPIWSSVDLRDGNQALPVPMSVDEKVAMFQLLVSIGFKEIEVGFPSASATEYAFARRLIESNLIPDDVTIQVLTQAREHLIRKTFDAVKGAKHAIIHLYNSTSTLQRDVVFRKNREEIKAIAIQGTELVRRLKEESGNTGIRFEYSPESFTGTELDYALDVCHAVMDSWGASVDNKIILNLPSTVEMSQPNIYADRIEWFCRNIKARDAVLISVHAHNDRGTAVATAELALLAGADRVEGALFGNGERCGNMDIVTMALNLFTQGVDPELDFSDLPRIREVYRRCTRMDIHPRHPYSGELVYTAFSGSHQDAISKGMKAQPTSPGGLWAVPYLPIDPQDVGCNYEAIVRINSQSGKGGVAYVLEKDYGIQIPKWMQPDFAEAVQGVADTTGNELAPDQIYELFHREYVKLMEPYAIKKCKIKWDDRDLERNEEEATAISCLVQSKEREFSFEAQGNGPLDAFVKGFSKESGLDFTIDEFSEHAIGRSAKALAAAYIKISCADGRISFGAGIDSNISLASIKATVSALNRLQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAFLKS010000168
EMBL· GenBank· DDBJ
MBV5304732.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help