A0A0D1DT68 · AHD1_USTMA
- ProteinFatty acid hydroxylase ahd1
- Geneahd1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids383 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Fatty acid hydroxylase; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA) (PubMed:15932999, PubMed:17850255).
UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis (PubMed:15932999, PubMed:17850255).
UA consists of 15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose at its terminal hydroxyl group (PubMed:17850255).
In addition, the cellobiose moiety is acetylated and acylated with a short-chain hydroxy fatty acid (PubMed:17850255).
UA biosynthesis starts with omega-hydroxylation of palmitic acid catalyzed by the cytochrome P450 monooxygenase cyp1 (PubMed:17850255).
Terminal hydroxylation of palmitic acid precedes subterminal hydroxylation catalyzed by the cytochrome P450 monooxygenase cyp2 (PubMed:17850255).
Sequential glucosylation of the hydroxy fatty acid is probably catalyzed by the glycosyltransferase ugt1 (Probable). The cellobiose lipid is further decorated by acetylation of the proximal glucose residue and by acylation with a short-chain beta-hydroxy fatty acid at the distal glucose residue (Probable). The acyltransferase uat1 may be a good candidate for catalyzing either acetylation or acylation of the cellobiose lipid (Probable). The fatty acid synthase fas2 may be involved in synthesis of the carbon backbone of the short-chain beta-hydroxy fatty acid esterified to the cellobiose disaccharide (Probable). The secreted UA consists of a mixture of both alpha-hydroxylated and non-hydroxylated glycolipids; therefore, alpha-hydroxylation of the long-chain fatty, catalyzed by the fatty acid hydroxylase ahd1, occurs late in UA biosynthesis and may be the last step before secretion (PubMed:17850255).
UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis (PubMed:15932999, PubMed:17850255).
UA consists of 15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose at its terminal hydroxyl group (PubMed:17850255).
In addition, the cellobiose moiety is acetylated and acylated with a short-chain hydroxy fatty acid (PubMed:17850255).
UA biosynthesis starts with omega-hydroxylation of palmitic acid catalyzed by the cytochrome P450 monooxygenase cyp1 (PubMed:17850255).
Terminal hydroxylation of palmitic acid precedes subterminal hydroxylation catalyzed by the cytochrome P450 monooxygenase cyp2 (PubMed:17850255).
Sequential glucosylation of the hydroxy fatty acid is probably catalyzed by the glycosyltransferase ugt1 (Probable). The cellobiose lipid is further decorated by acetylation of the proximal glucose residue and by acylation with a short-chain beta-hydroxy fatty acid at the distal glucose residue (Probable). The acyltransferase uat1 may be a good candidate for catalyzing either acetylation or acylation of the cellobiose lipid (Probable). The fatty acid synthase fas2 may be involved in synthesis of the carbon backbone of the short-chain beta-hydroxy fatty acid esterified to the cellobiose disaccharide (Probable). The secreted UA consists of a mixture of both alpha-hydroxylated and non-hydroxylated glycolipids; therefore, alpha-hydroxylation of the long-chain fatty, catalyzed by the fatty acid hydroxylase ahd1, occurs late in UA biosynthesis and may be the last step before secretion (PubMed:17850255).
Pathway
Secondary metabolite biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | C-4 methylsterol oxidase activity | |
Molecular Function | iron ion binding | |
Biological Process | ergosterol biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFatty acid hydroxylase ahd1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Ustilaginaceae > Ustilago
Accessions
- Primary accessionA0A0D1DT68
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 84-104 | Helical | |||
Transmembrane | 123-143 | Helical | |||
Transmembrane | 172-192 | Helical | |||
Transmembrane | 214-236 | Helical | |||
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Leads to the production of UA derivatives that lack the alpha-hydroxyl group.
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000452764 | 1-383 | Fatty acid hydroxylase ahd1 | ||
Glycosylation | 342 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
PTM databases
Expression
Induction
Expression is strongly induced under conditions of nitrogen starvation (PubMed:17850255).
Expression is positively regulated by the cluster-specific transcription factor rua1 that recognizes and binds to the specific 5'-T/G-G/T-C-G-C-A-T-A/T-C/T-C/T-G/A-3' upstream activating sequence found in all promoters of the UA biosynthesis genes (PubMed:20173069).
Expression is positively regulated by the cluster-specific transcription factor rua1 that recognizes and binds to the specific 5'-T/G-G/T-C-G-C-A-T-A/T-C/T-C/T-G/A-3' upstream activating sequence found in all promoters of the UA biosynthesis genes (PubMed:20173069).
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 217-341 | Fatty acid hydroxylase | |||
Sequence similarities
Belongs to the sterol desaturase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length383
- Mass (Da)43,603
- Last updated2015-04-29 v1
- Checksum449B7008B1729EEC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM003162 EMBL· GenBank· DDBJ | KIS65765.1 EMBL· GenBank· DDBJ | Genomic DNA |