A0A0D1DT68 · AHD1_USTMA

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).

Pathway

Secondary metabolite biosynthesis.

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular FunctionC-4 methylsterol oxidase activity
Molecular Functioniron ion binding
Biological Processergosterol biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fatty acid hydroxylase ahd1
  • EC number
  • Alternative names
    • Ustilagic acid biosynthesis cluster protein ahd1

Gene names

    • Name
      ahd1
    • ORF names
      UMAG_12340

Organism names

Accessions

  • Primary accession
    A0A0D1DT68

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane84-104Helical
Transmembrane123-143Helical
Transmembrane172-192Helical
Transmembrane214-236Helical

Keywords

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
IDPosition(s)Description
ChainPRO_00004527641-383Fatty acid hydroxylase ahd1
Glycosylation342N-linked (GlcNAc...) asparagine

Keywords

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).

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain217-341Fatty acid hydroxylase

Sequence similarities

Belongs to the sterol desaturase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    383
  • Mass (Da)
    43,603
  • Last updated
    2015-04-29 v1
  • Checksum
    449B7008B1729EEC
MTTRTATSTSTTVHGHLGDLKLRNAAITGPHLQPKAAKQDLADTKPDSARTFPGLGFKLSPTEERLRAKRNWGFLETAYDNSKVMGLTTHFVTITMAIVFNKSWLAKPVYDWLNTYDRFTIHTVHTWILLSTCQLLVIGLFALTDLSGRPSWLARYRMQPHKPPTLAQYKKLIPVVLFNLVVVNTISNIIYYPLAEWRGIQTTYETLPSGKKLVAQWLVCLLMEDIGFYTVHRALHHPRIYKYIHKKHHEFSAPIAGASTYAHPLEHYFSNLVPILVGLLITRAHISVQYLFFTGLMIGSHVQHSGYNIPFLTCALVHDWHHYFNTENYGPVGLLDAIFKTNKTFKAWTSETVAAFHGDRAKARQAALEKLAQIEAEEQERIR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM003162
EMBL· GenBank· DDBJ
KIS65765.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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