A7XRY6 · TDIC_EMENI
- ProteinProbable NADPH-dependent quinone reductase tdiC
- GenetdiC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids355 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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).
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
Pathway
Secondary metabolite biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | oxidoreductase activity | |
Biological Process | secondary metabolite biosynthetic process | |
Biological Process | terrequinone A biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable NADPH-dependent quinone reductase tdiC
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionA7XRY6
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000436366 | 1-355 | Probable NADPH-dependent quinone reductase tdiC | ||
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the zinc-containing alcohol dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length355
- Mass (Da)37,620
- Last updated2011-12-14 v1
- ChecksumA37DC0625A45FDB0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |