A0A0D1E3S6 · MAC1_USTMA

Function

function

Acyl-CoA-dependent acyltransferase; part of the gene cluster that mediates the biosynthesis of mannosylerythritol lipids (MELs), surface-active substances that enhance the availability of water-insoluble substrates (PubMed:15932999, PubMed:16885300).
Mannosylerythritol lipid production is responsible for hemolytic activity of Ustilago maydis (PubMed:15932999).
Depending on the number of acetyl groups, mannosylerythritol lipids can be differentiated into MEL A (fully acetylated), MEL B and MEL C (monoacetylated at R-6 and R-4, respectively), and the fully deacetylated MEL D (PubMed:31103599).
The first step in the pathway is the generation of mannosylerythritol by the glycosyltransferase EMT1 which catalyzes the transfer of GDP-mannose to the C-4 atom of meso-erythritol (PubMed:15932999).
This reaction has to be stereospecific, since only mannosyl-D-erythritol is generated (PubMed:15932999).
The produced disaccharide is subsequently acylated with fatty acids of various lengths derived from the peroxisomal beta-oxidation by the peroxisomal acyltransferases MAC1 and MAC2 at positions C-2 and C-3, repectively (PubMed:16885300, PubMed:24835306, PubMed:31103599).
The existence of MEL derivatives which carry an acetyl group at C-2 implies that at least MAC1 also accepts acetyl-CoA as a donor (PubMed:15932999).
The final step of MEL biosynthesis is the acetylation of the fully acylated mannosylerythritol lipids catalyzed by the acetyl-CoA-dependent acetyltransferase MAT1 (PubMed:16885300).
MAT1 displays a relaxed regioselectivity and is able to transfer acetylgroups to both positions C-4 and C-6 of the mannosyl moiety (PubMed:15932999).

Biotechnology

MELs not only have high potential as eco-friendly biosurfactants due to their excellent surface activity, but also have attracted considerable recent interest because of thei runique properties, including self-assembly, anti-tumor and cell differentiation induction activities, and moisturizing and hair-repairing properties.

Pathway

Secondary metabolite biosynthesis.

GO annotations

AspectTerm
Cellular Componentperoxisome
Molecular Functionacetyltransferase activity
Biological Processmycotoxin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acyl-CoA-dependent acyltransferase MAC1
  • EC number
  • Alternative names
    • Mannosylerythritol lipids (MELs) biosynthesis cluster protein MAC1

Gene names

    • Name
      MAC1
    • ORF names
      UMAG_03116

Organism names

Accessions

  • Primary accession
    A0A0D1E3S6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Abolishes completely the production of mannosylerythritol lipids (MELs).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004495341-591Acyl-CoA-dependent acyltransferase MAC1

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region589-591Peroxisomal targeting signal type 1

Domain

The C-terminal PTS1-type tripeptide peroxisomal targeting signal is required for the import into peroxisomes.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    591
  • Mass (Da)
    66,282
  • Last updated
    2015-04-29 v1
  • Checksum
    6F84D9B60DC83D18
MINNALRTLISSATEQSLDDVLEHEFRTAVQLQQMDQFEWHQVEADLWKRTCLGHEASASFNQNIAHGHTELSLMTSWRVHQPSSSRITGSELELDQLVARVRQAWIQARYLRPEVGVELDTHTDPTVAQTMCYRLLRDEESIQEWLDETFVVKRLGDPGVATPAELCAYTYNRPLATKGKKSMLYLILPRLDDEQRTAYTIWNVSHAVTDGGSLAEVFNTLFQCVIDATPSEPYDSIYTPSAFELNVLPRMPRSVVMAYRQQYQPKPEEIAKAHKVAEVNMRMITEKMGESLALMPSTSWPERKHETVCLCRELEANEVRELLKFAKQVHSGITYLASAATILSAAETFPERKASSKGALVGMVRNARRWISATPLDASLGASTPLGSDAVFLWVPIDTHKTLEPSFSRMQELVTTARHIRHELDKHLTTPHCISSYPYVAESSIQGLNQQWSQIKAVQSPSSSSSQKEIAGIIGAQAPGFSSVGMMRIRPRFEPVSANARASGLWLERTDFTHTGRQINASPWISMFNVDGRIKLQLGFDTKFHEVEKMNQWLDRTVVWMRICAAAAATTSTSVSSTSVDATAPVFARL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM003146
EMBL· GenBank· DDBJ
KIS69145.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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