D7GCL9 · D7GCL9_PROFC

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 Functionlyase 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
      PFREUD_07490

Organism names

Accessions

  • Primary accession
    D7GCL9

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-26Disordered
Domain37-157Thiamine pyrophosphate enzyme N-terminal TPP-binding
Region216-241Disordered
Compositional bias218-236Pro residues

Sequence similarities

Belongs to the TPP enzyme family. MenD subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    551
  • Mass (Da)
    56,476
  • Last updated
    2010-08-10 v1
  • Checksum
    31772F627611F442
MSNTADPQNPPQARSGEPAAAVGQAVPGGPPVRSAALARALVTALVAHGLRDVVYCPGSRDAPFAYALDAAQHAGWLRVAVRLDERAAGFQALGLAKAAAAQGTARPVAVVTTSGTAVANLHPAVLEADAAGVALVVVSADRPHEMWRTGANQTTEQLGIFAHAVRQEADIPAGFPVDGRLSGLVRRAMTAALGNLNGNSGPVHLNVCLREPLKPDDQWLPGPAPAPEPHREAPGAPTELPMPDRTVVVAGDGAGDQAQQAATAGGWPLLAEPSSGARFGANALTDYQQLLGSPLAPQIEGVLVFGHPTLSRPVSALLARDDVRMVAVTCGSRWTDVAGLAQVVRGPVHIANNPQGEWLARWIGADEPAPRSTKDTAARLIWQAHGAPDAPALVLGASAVIRSFDRRAVPGDHAPLVIANRGLAGIDGTVSTAIGVAAGTGRPVRAVVGDLTLAHDGLGLLRGMNEAVPDVQVVVLADRGGAIFAGLEHGSAAPALLSRYFLTPQVLDVRQLAGAVGASYRHVTDVLELPQVLSEPISGASIVEVELPPVG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias218-236Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FN806773
EMBL· GenBank· DDBJ
CBL56280.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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