P9WEV9 · MDPH2_EMENI
- ProteinAnthrone oxygenase
- GenemdpH-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids192 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213).
The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316).
The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316).
The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone by mdpH-1 and mdpH-2 (PubMed:20139316).
Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751).
These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213).
Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213).
The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316).
The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316).
The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone by mdpH-1 and mdpH-2 (PubMed:20139316).
Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751).
These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213).
Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213).
Catalytic activity
- emodin anthrone + O2 = emodin + H+ + H2OThis reaction proceeds in the forward direction.
Pathway
Secondary metabolite biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | monooxygenase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAnthrone oxygenase
- 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 accessionP9WEV9
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 12-32 | Helical | ||||
Sequence: IVTGSFLSGAMITLSTITVPV | ||||||
Transmembrane | 54-74 | Helical | ||||
Sequence: GHISLPTISIATAILYFYIAA | ||||||
Transmembrane | 86-106 | Helical | ||||
Sequence: AALVGFLTIVMVPFTWIVMSS | ||||||
Transmembrane | 172-192 | Helical | ||||
Sequence: MHLVRSLFPLMAAVLGVGICV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450871 | 1-192 | Anthrone oxygenase | |||
Sequence: MASLTTLKNTAIVTGSFLSGAMITLSTITVPVLLETSTHPPQLLHQWVRTYHYGHISLPTISIATAILYFYIAAYQGAREQPWRKAALVGFLTIVMVPFTWIVMSSTNGMLFGLEAGNRDHSQFFEQGANRSGLKGANSSQSHGLGNVSVGIGVEMATLEGVRELLVRWKWMHLVRSLFPLMAAVLGVGICV | ||||||
Glycosylation | 130 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 138 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 147 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Structure
Family & Domains
Sequence similarities
Belongs to the anthrone oxygenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length192
- Mass (Da)20,918
- Last updated2020-10-07 v1
- Checksum2814E86A18EA220E
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BN001308 EMBL· GenBank· DDBJ | CBF90095.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AACD01000005 EMBL· GenBank· DDBJ | EAA66024.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |