Q4J989 · HOSA_SULAC

Function

function

Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway. Does not display 2-isopropylmalate synthase and citramalate synthase activities since it cannot use 2-oxoisovalerate or pyruvate as substrate.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Activity regulation

Inhibited by lysine.

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site192-oxoglutarate (UniProtKB | ChEBI)
Binding site20Mg2+ (UniProtKB | ChEBI)
Binding site832-oxoglutarate (UniProtKB | ChEBI)
Binding site1432-oxoglutarate (UniProtKB | ChEBI)
Binding site1772-oxoglutarate (UniProtKB | ChEBI)
Binding site205Mg2+ (UniProtKB | ChEBI)
Binding site207Mg2+ (UniProtKB | ChEBI)
Active site299Proton acceptor

GO annotations

AspectTerm
Molecular Functionhomocitrate synthase activity
Molecular Functionmetal ion binding
Biological Processlysine biosynthetic process via aminoadipic acid

Keywords

Enzyme and pathway databases

Community curation (1)

Synthesis of homocitrate from acetyl-CoA and 2-oxoglutarate, the first (committed) step of lysine biosynthesis via the alpha-aminoadipate pathway. The enzyme is inhibited by lysine via its C-terminal RAM (Regulation of Amino acid Metabolism) domain.

Names & Taxonomy

Protein names

  • Recommended name
    Homocitrate synthase
  • EC number
  • Short names
    HCS

Gene names

    • Ordered locus names
      Saci_1304
Community curation (1)

Organism names

Accessions

  • Primary accession
    Q4J989

Proteomes

Phenotypes & Variants

Disruption phenotype

Cells lacking this gene do not grow in MM without or even with lysine, but grow in MM with the simultaneous supplementation of lysine and arginine to the medium. Furthermore, the mutant strain does not grow on MM supplemented with lysine and glutamate, but grows with lysine and ornithine.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004480521-468Homocitrate synthase

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-266Pyruvate carboxyltransferase

Domain

Contains an N-terminal catalytic domain fused with a RAM (Regulation of Amino acid Metabolism) domain at the C-terminus. The mutant enzyme lacking the RAM domain is insensitive to inhibition by lysine, indicating that the RAM domain is responsible for enzyme allosteric regulation.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    468
  • Mass (Da)
    51,732
  • Last updated
    2005-08-02 v1
  • Checksum
    B1C66520DDDCFBDE
MLPKKKLHMKVGILDSTLREGEQTPGVVFTTDQRVEIAKALSDIGVQMIEAGHPAVSPDIYEGIRRIIKLKREGVIKSEIVAHSRAVKRDIEVGAEIEADRIAIFYGISDTHLKAKHHTTRDEALRSIAETVSYAKSHGVKVRFTAEDATRADYQYLLEVIKTVRDAGADRVSIADTVGVLYPSRTRELFKDLTSRFPDIEFDIHAHNDLGMAVANVLAAAEGGATIIHTTLNGLGERVGIAPLQVVAAALKYHFGIEVVDLKKLSEVASLVEKYSGIALPPNFPITGDYAFVHKAGVHVAGVLNDPKTYEFLPPETFGRSRDYVIDKYTGKHAVKDRFDRLGVKLTDSEIDQVLAKIKSNPNVRFYRDVDLLELAESVTGRILKPRPPENIMALISVKCDSNVYTTSVTRRIVLIEGVREVMEISGDYDILVKVEAKDSTELNQIIESIRAVKGVKSTLTSLILKKM

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000077
EMBL· GenBank· DDBJ
AAY80642.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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