A8NCK4 · COX1_COPC7
- ProteinCytochrome P450 monooxygenase COX1
- GeneCOX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids518 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of alpha-cuprenene and oxidized derivatives (PubMed:19400802).
The alpha-cuprenene synthase COP6 is the only sesquiterpene synthase identified in C.cinereus that appears to be part of a biosynthetic gene cluster and is highly specific since it catalyzes the cyclization of (2E,6E)-farnesyl diphosphate into only one product, alpha-cuprenene (PubMed:19400802, PubMed:20419721).
The cytochrome P450 monooxygenase COX2 then oxidizes the cyclohexadiene ring of alpha-cuprenene at positions 1 and 4, yielding first alpha-cuparene, followed by alpha-cuparophenol and a further yet unidentified compound resulting from one additional oxidation step (PubMed:19400802).
The cytochrome P450 monooxygenase COX1 then likely catalyzes the oxidation at position 9 of the pentane ring of alpha-cuprenene to give the corresponding hydroxy or ketone derivatives (PubMed:19400802).
The alpha-cuprenene synthase COP6 is the only sesquiterpene synthase identified in C.cinereus that appears to be part of a biosynthetic gene cluster and is highly specific since it catalyzes the cyclization of (2E,6E)-farnesyl diphosphate into only one product, alpha-cuprenene (PubMed:19400802, PubMed:20419721).
The cytochrome P450 monooxygenase COX2 then oxidizes the cyclohexadiene ring of alpha-cuprenene at positions 1 and 4, yielding first alpha-cuparene, followed by alpha-cuparophenol and a further yet unidentified compound resulting from one additional oxidation step (PubMed:19400802).
The cytochrome P450 monooxygenase COX1 then likely catalyzes the oxidation at position 9 of the pentane ring of alpha-cuprenene to give the corresponding hydroxy or ketone derivatives (PubMed:19400802).
Cofactor
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 450 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Molecular Function | monooxygenase activity | |
Molecular Function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome P450 monooxygenase COX1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Agaricineae > Psathyrellaceae > Coprinopsis
Accessions
- Primary accessionA8NCK4
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 7-25 | Helical | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000444637 | 1-518 | Cytochrome P450 monooxygenase COX1 | ||
Glycosylation | 48 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 100 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 292 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 302 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 351 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 457 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
PTM databases
Structure
Sequence
- Sequence statusComplete
- Length518
- Mass (Da)58,438
- Last updated2010-08-10 v2
- MD5 ChecksumE8022F80892C182515D73207C77D1355
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AACS02000009 EMBL· GenBank· DDBJ | EAU89297.2 EMBL· GenBank· DDBJ | Genomic DNA |