A0A4P6X211 · A0A4P6X211_HYDPS

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

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

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 site14Mn2+ (UniProtKB | ChEBI)
Binding site202Mn2+ (UniProtKB | ChEBI)
Binding site204Mn2+ (UniProtKB | ChEBI)
Binding site239Mn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function2-isopropylmalate synthase activity
Molecular Functionacetyl-CoA C-acetyltransferase activity
Molecular Functionmanganese 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
      HPF_14130

Organism names

Accessions

  • Primary accession
    A0A4P6X211

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain5-268Pyruvate carboxyltransferase
Region394-513Regulatory domain

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    513
  • Mass (Da)
    55,469
  • Last updated
    2019-07-31 v1
  • Checksum
    F4AC0AEA50F077E7
MSDKLIIFDTTLRDGEQSPGASMTKDEKLRIARQLERLKVDVIEAGFAASSNGDFDCVQAIANTIKDSTVCSLARANDRDISRAAEALKGASRARIHTFIATSPLHMEKKLRMTPDQVFEQAKQSVRFARNLVDDIEFSPEDGYRSDIDFLCRVLEAVINEGATTLNIPDTVGYAVPELYGNFIHTLRERVPNSDKAIWSVHCHNDLGMAVANSLAGVKIGGARQVECTINGLGERAGNCSLEEIVMAVKTRRDYFNLDIGIDTTQIVPASRMVSQTTGFVVQPNKAVVGANAFAHASGIHQDGVLKARDTYEIMRAEDVGWSANKIVLGKLSGRNAFKQRLQDLGIEMASESEINTAFAAFKELADRKSEIFDEDILALCSDESVTAEKERYGLVSLSQRSETGERPHAEVVFTVEGKEIRGSSDGNGPVDASLKAIESHVKSGAELVLYSVNAITSGSTESQGEVTVRLQLGGRVVNGVGADPDIVVASAKAYLSALNKLESQAERVAAQG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP037867
EMBL· GenBank· DDBJ
QBM28835.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
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