I1RF55 · AURO_GIBZE
- ProteinFAD-linked oxidoreductase aurO
- GeneaurO
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids506 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin (PubMed:15809006, PubMed:15811992, PubMed:16879655).
The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 (PubMed:21296881, PubMed:23557488).
The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction (PubMed:21296881).
The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488).
Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ (PubMed:21296881, PubMed:23557488).
Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin (PubMed:21296881).
The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 (PubMed:21296881, PubMed:23557488).
The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction (PubMed:21296881).
The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488).
Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ (PubMed:21296881, PubMed:23557488).
Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin (PubMed:21296881).
Cofactor
Pathway
Pigment biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | FAD binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFAD-linked oxidoreductase aurO
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium
Accessions
- Primary accessionI1RF55
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Impairs the production of aurofusarin and leads to the accumulation of a light yellow pigment (PubMed:16879655).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000441091 | 1-506 | FAD-linked oxidoreductase aurO | |||
Sequence: MINSFSLFAHITPIIRSSLHSRYSVISSRKAMSSLAAAPYRHVMMPFSPAQDAQVHGNSALTKLTDAIPDLKIYTRSSPHYESLRGVYNKLITAQPLAICRPTSVAQVQAIVKTVSGLGIPLGVRGGGHDVFGRGCIADSVTIDMRELDTQELSQDKKTVKVGGGITSKNLVGFLGSHNLCTSNGFAGEAGWTSWASWGGYGPLGDYVGLGVDNIVGAKIVTASGDVVDAKGDSELLWALRGGGGNFGVIAETDVRVYPMSTIQAGFIVYPWPETADVLLRLQALLDSGVPDKLCLQAGFTKGEWGLGMAITYIWPEAETIGPESEEWLQKLKGLGTCIVDTVAETTFEAFQASISSAISNPVNVTSRHISISKFTSDTLNQLIGACESMPAEADCSITCTILHGKAAQANVLSAFGTRRPHIMLHINAVTEEAAHEHVAIAWADRLVDGVEATGDSIGSTYVSFMESDKDPKGCYGENWERLKAVKKEVDPNDVFRFVHGRIPAA |
Expression
Induction
Expression is regulated by the aurofusarin biosynthesis cluster-specific transcription factor aurR1/GIP2 (PubMed:16461721).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 92-260 | FAD-binding PCMH-type | ||||
Sequence: ITAQPLAICRPTSVAQVQAIVKTVSGLGIPLGVRGGGHDVFGRGCIADSVTIDMRELDTQELSQDKKTVKVGGGITSKNLVGFLGSHNLCTSNGFAGEAGWTSWASWGGYGPLGDYVGLGVDNIVGAKIVTASGDVVDAKGDSELLWALRGGGGNFGVIAETDVRVYPM |
Sequence similarities
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length506
- Mass (Da)54,117
- Last updated2012-06-13 v1
- ChecksumB009B842CBB45FF5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HG970332 EMBL· GenBank· DDBJ | CEF74598.1 EMBL· GenBank· DDBJ | Genomic DNA |