A0A068MT64 · A0A068MT64_SYNY4

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

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

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
Biological Processphylloquinone 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

Gene names

    • Name
      menD
    • ORF names
      D082_06200

Organism names

Accessions

  • Primary accession
    A0A068MT64

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-125Thiamine pyrophosphate enzyme N-terminal TPP-binding
Domain424-554Thiamine pyrophosphate enzyme TPP-binding

Sequence similarities

Belongs to the TPP enzyme family. MenD subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    596
  • Mass (Da)
    66,097
  • Last updated
    2014-10-01 v1
  • Checksum
    2AE0837D6143F6D4
MVDFTNLNGLAASLLVETLFRLGLRQAVICPGSRSSPLTVALARHGEIDCVVSLDERSASFFALGYGKRTGKPALLVCTSGTAAANFLPAIIEAHYSQVPLLVLTGDRPPKLRHCRAGQTIDQTKLYGHYPQWQTELALPEASLDFCHYLRQTVLHGWQKCFWPRLGVVHLNCPFDEPLAPLADDSVQVLAQKFDANSFYWGITEFNQLWPALPINFSSPVVPLLPWDFPKIGLILVGVIPGGEAHALLTDILAIAKALHYPVLCDALCSLRNYDDGETVLITNYDFLVRCQSWAEQLVPEQIIQIGELPTSKALRNWLSIINCPRYVFNCNGENLDPLQGQTVYSFATIGQLADYLHTNILPIDSIQKEYTHNWQEKQAKSQAIIASAFINPGGNTPSMVSQLVHCLPPQTNLLVANSLPVRWLEFFWPANGDRHRIFVNRGANGIDGTLSTAMGISHRSIHQTVLLTGDLSLLHDSNGFLNQSQMRGNLTIILLNNNGGGIFQTLPIAQCEDVFETYFATPQSVDFAQLCGTYGVDHHVITDLGSLKEQLETISPTPIRVLEIIGDRHQEAQWLKSLQTQFCHADEPFQELGFL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP007542
EMBL· GenBank· DDBJ
AIE73149.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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