I1RF60 · AURJ_GIBZE
- ProteinO-methyltransferase aurJ
- GeneaurJ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids439 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
O-methyltransferase; 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).
Catalytic activity
- norrubrofusarin + S-adenosyl-L-methionine = H+ + rubrofusarin + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Pathway
Pigment biosynthesis.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | O-methyltransferase activity | |
Biological Process | methylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameO-methyltransferase aurJ
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium
Accessions
- Primary accessionI1RF60
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000441088 | 1-439 | O-methyltransferase aurJ | |||
Sequence: MGSISSPSLIIDLANAVSSAAKNLDTQLQSQGFPQPSFEADGPTYVVPKDAPKAAHEARVATAEAALKLFNLVSGPSELLPNMTASYHTIFALQWLHHFDVFSHIPLDGSLSYEKLATKANVPESLLKSVARMAMTSNILAEPTTGQVAHSANSAMFVKFPNMRDWASYMFTASIPTAAAMVQATEKWPGSVKKTETAYNIAFNHDLPFFDHLSQSPVMTKQFSGYMRSVTDGQGMDLSHLVNGFDWASLPDKSLIVDIGGSAGHASYALAAAYPHLRFEVQDLDTVVNGEKAAKEHEEAVSKHVIGTDNRVTFKAHNFFEAQPTKDATVYMLRMIIHDWPDAEAKTILGNLVPALESAKATLLIMDTVLPSPGSIPSVRERVIRTRDLTMRQVFNAKERGVDDWEAILRETDSRLTLKNLRQPEGSNMCLLTISLQDD |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length439
- Mass (Da)48,089
- Last updated2012-06-13 v1
- ChecksumF4C18EEAE425AE18
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HG970332 EMBL· GenBank· DDBJ | CEF74603.1 EMBL· GenBank· DDBJ | Genomic DNA |