A7XRY6 · TDIC_EMENI

Function

function

Probable NADPH-dependent quinone reductase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:16426969, PubMed:17291795, PubMed:17704773, PubMed:22083274).
The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD (PubMed:17704773).
The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773).
The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773).
TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206).
Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206).

Cofactor

NADPH (UniProtKB | Rhea| CHEBI:57783 )

Pathway

Secondary metabolite biosynthesis.

GO annotations

AspectTerm
Molecular Functionoxidoreductase activity
Biological Processsecondary metabolite biosynthetic process
Biological Processterrequinone A biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable NADPH-dependent quinone reductase tdiC
  • EC number
  • Alternative names
    • Terrequinone biosynthesis protein C

Gene names

    • Name
      tdiC
    • ORF names
      AN8515

Organism names

Accessions

  • Primary accession
    A7XRY6
  • Secondary accessions
    • C8VEN4
    • Q5AT62

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004363661-355Probable NADPH-dependent quinone reductase tdiC

Expression

Induction

Expressed during both sexual and asexual development (PubMed:26773375).
Expression is positively regulated by the secondary metabolism regulator laeA (PubMed:16426969, PubMed:17291795).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    355
  • Mass (Da)
    37,620
  • Last updated
    2011-12-14 v1
  • Checksum
    A37DC0625A45FDB0
MHAALVPTWSSPCPIYTEIPDPGPPPPEQLQLKVLAVGIPRVVRLRARGIHPTAKSASLPYDPSIDGVGIDEQTGIMYYILPLSASCLAEKVNVDRDNLVPLQPGAPKPQPRNGPENGYGIALGDAADHRAETLDPIAIAGLVNPVSSSWMALRTRVDGEITGKTVLVLGATSKSGRAAVLVARFLGANKVIGVARREEGLRSVEGLDGWVTSGDMLPGETGVRFALPDWVGPVHIVLDYVGGSVAAGVLGSAEIEEGRELQYVQVGNLALELGTGEKHMFETLPGHLISRKPICIRGSGMGSFSRRDLVREMPGLVAFLARMKAPFGIASAPMCEVASVWQDEDTKGSRVVIVP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EF550583
EMBL· GenBank· DDBJ
ABU51604.1
EMBL· GenBank· DDBJ
mRNA
BN001305
EMBL· GenBank· DDBJ
CBF80714.1
EMBL· GenBank· DDBJ
Genomic DNA
AACD01000154
EMBL· GenBank· DDBJ
EAA66859.1
EMBL· GenBank· DDBJ
Genomic DNA
AACD01000155
EMBL· GenBank· DDBJ
EAA66871.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help