A0A1S2MYR4 · A0A1S2MYR4_9MICC

  • Protein
    2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
  • Gene
    menD
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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
    • ORF names
      BK826_08180

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LCT-H5
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Rothia

Accessions

  • Primary accession
    A0A1S2MYR4

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-104Thiamine pyrophosphate enzyme N-terminal TPP-binding

Sequence similarities

Belongs to the TPP enzyme family. MenD subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    558
  • Mass (Da)
    58,255
  • Last updated
    2017-04-12 v1
  • Checksum
    77285C6F0E2DCB35
MRHAVIAPGSRSAPLAYALAAAADAGALQVHVRIDERTAGFTALGLAKATGAPAAVVTTSGTAVGELLPAVMEAHHAEVPLAVLSADRPPRLRGTGANQTTDQPGIFGTHVRVGVDLTDYPEQTPGPQTAGFTNALAALTGRDPDDWTQPSLRPLGPVQINCAFDEPLHPDQRMRQILRAWADGVAGLDPEPAPTLPDPTLEAVLADAAGPPADGIPRRSVVIAGDGAGPLARDFAEARGLPLLAEPSSGARSGEHAIGGYRVLLGEESLGGRIERVVLFGRPTLSRPVTRLLADPQTDAVIYLPRPVAWADPRRRPEMPVRTLAEAAAFAGTGERGWLRAWREADAALAARIERLAAAGEHPTGPAVAAAAVRACERDGSALILGSSNLVRDADLAPVPALPLTGVWANRGLAGIDGTLATATGIGLGLGVPARLLVGDLTFLHDLGSLNLGPGEARPRLQIVVFNDDGGGIFTTLEHGQVAEDRGWSDAVERFFSTPHGADLEHLVRGFGHRYLRADDVAALRAALREPAEGIEVIEVRGSRADLRPFHDALTRPA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MODZ01000009
EMBL· GenBank· DDBJ
OIJ35468.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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