P0DOB2 · GEDH_ASPTN
- ProteinAnthrone oxygenase gedH
- GenegedH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids150 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of geodin, an intermediate in the biosynthesis of other natural products (PubMed:19549600, PubMed:24009710, PubMed:7665560).
The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) gedC (PubMed:12536215, PubMed:19549600).
The atrochrysone carboxyl ACP thioesterase gedB then breaks the thioester bond and releases the atrochrysone carboxylic acid from gedC (PubMed:19549600).
The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:24009710).
The next step is performed by the emodin anthrone oxygenase gedH that catalyzes the oxidation of emodinanthrone to emodin (PubMed:1810248).
Emodin O-methyltransferase encoded probably by gedA then catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:1444712).
Ring cleavage of questin by questin oxidase gedK leads to desmethylsulochrin via several intermediates including questin epoxide (PubMed:3182756).
Another methylation step probably catalyzed by methyltransferase gedG leads to the formation of sulochrin which is further converted to dihydrogeodin by the sulochrin halogenase gedL (PubMed:24009710).
Finally, the dihydrogeodin oxidase gedJ catalyzes the stereospecific phenol oxidative coupling reaction converting dihydrogeodin to geodin (PubMed:7665560).
The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) gedC (PubMed:12536215, PubMed:19549600).
The atrochrysone carboxyl ACP thioesterase gedB then breaks the thioester bond and releases the atrochrysone carboxylic acid from gedC (PubMed:19549600).
The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:24009710).
The next step is performed by the emodin anthrone oxygenase gedH that catalyzes the oxidation of emodinanthrone to emodin (PubMed:1810248).
Emodin O-methyltransferase encoded probably by gedA then catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:1444712).
Ring cleavage of questin by questin oxidase gedK leads to desmethylsulochrin via several intermediates including questin epoxide (PubMed:3182756).
Another methylation step probably catalyzed by methyltransferase gedG leads to the formation of sulochrin which is further converted to dihydrogeodin by the sulochrin halogenase gedL (PubMed:24009710).
Finally, the dihydrogeodin oxidase gedJ catalyzes the stereospecific phenol oxidative coupling reaction converting dihydrogeodin to geodin (PubMed:7665560).
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 gedH
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionP0DOB2
- 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 | 1-21 | Helical | ||||
Sequence: MANPAVGAMMGLSLVAVPVFL | ||||||
Transmembrane | 41-61 | Helical | ||||
Sequence: GHKLMPTIAVATCALHGWVAA | ||||||
Transmembrane | 73-93 | Helical | ||||
Sequence: PVLAAVTTITMVPFTWVCMVS | ||||||
Transmembrane | 128-148 | Helical | ||||
Sequence: LFPLAGAIVACQTLLKELVGG |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000437096 | 1-150 | Anthrone oxygenase gedH | |||
Sequence: MANPAVGAMMGLSLVAVPVFLDTNTQSEQLLAQFASLYDYGHKLMPTIAVATCALHGWVAARKRAAHQPWGRPVLAAVTTITMVPFTWVCMVSTNNALFQLHKGADANMEMVRALIARWQWLHVARSLFPLAGAIVACQTLLKELVGGSR |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the anthrone oxygenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length150
- Mass (Da)16,271
- Last updated2016-09-07 v1
- Checksum6036551E65A78341
Sequence caution
Keywords
- Technical term