Q6AHC2 · MEND_LEIXX

Function

function

Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

thiamine diphosphate (UniProtKB | Rhea| CHEBI:58937 )

Note: Binds 1 thiamine pyrophosphate per subunit.

Pathway

Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Quinol/quinone metabolism; menaquinone biosynthesis.

GO annotations

AspectTerm
Molecular Function2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular Functionthiamine pyrophosphate binding
Biological Processmenaquinone biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
  • EC number
  • Short names
    SEPHCHC synthase
  • Alternative names
    • Menaquinone biosynthesis protein MenD

Gene names

    • Name
      menD
    • Ordered locus names
      Lxx01490

Organism names

Accessions

  • Primary accession
    Q6AHC2

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003417641-5922-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the TPP enzyme family. MenD subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    592
  • Mass (Da)
    61,513
  • Last updated
    2004-09-13 v1
  • Checksum
    D331DF15A4332D6E
MPDARAADEPAQRLPRTGNPATDYALALLAHLIGAGVRDIVVSPGSRSQALALAAAELERAGAVRLHVRLDERVGGFLALGIGRETGAPAAVVTTSGTATANLHPAVLEAHESGVPLIVITADRPPELRGIRSSQTTHQDGLYGVAVRLAKDVPAPSGEEEDVATAARLAVESVRAAVGAETADPGPVHLNLAFREPLSVAVPPLPVVERGALPALAGAQKLGRETVVPGIGPSTVVIAGADAGPEAEEYARSAGFPLLAEVSSGSRFGPNLVVAYRELLREPEFGGRVRRAVVFGHPTLSREVPALLLRDDVETVVVAPRGRQAYNPGRRAVIVGAVRPAVEADPRSPEARAWVGLWVSASRRLVEAAERVASPDATAPDLAKARSLDPSDALAFARMELAAVRAPITRPLLAEALWRHTWPHDRLVLGASRLIRDADRIVPGKRLRVHSNRGLAGIDGTIATAIGVALASQAVAVETGTLPGITRVLLGDLALLHDAGALLGGSGEAWPNVQVIVGNDGGGTIFDGLEVATIASPAAFDRVLYTPQRGDIAALSTAYGWAHRVVRTKGELDQALSAPPAGASVLEVPLER

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE016822
EMBL· GenBank· DDBJ
AAT88223.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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