A0A0D1CFF0 · UGT1_USTMA

Function

function

Glycosyltransferase; 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
Molecular FunctionUDP-glycosyltransferase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycosyltransferase ugt1
  • EC number
  • Alternative names
    • Ustilagic acid biosynthesis cluster protein ugt1

Gene names

    • Name
      ugt1
    • ORF names
      UMAG_06467

Organism names

Accessions

  • Primary accession
    A0A0D1CFF0

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004527631-578Glycosyltransferase ugt1

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).

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region81-106Disordered
Region342-375Disordered
Compositional bias360-375Basic and acidic residues

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    578
  • Mass (Da)
    64,072
  • Last updated
    2015-04-29 v1
  • Checksum
    5DBD21779098B493
MATEHILLVCWPAVGHARPMLDYAAAQLKQNPGLIITFICSKMQIALLEGLAISEHLADKKFGDRLRLLGTGRPAQEVLKEFGDREDAKNAANSASKAPNTTANGPEPEVILTMQAATLIQKRFAEIFPTILANDDLFDEQDNSLLLPACVAGKPTTIVVNWMLPGMVETVRKHSSDLKMVTFFDNSCTFVTRMLGPRSIGGFGGIERLWSQYCNSNPEVDPNDSTLKEKLLGRRWTGKFYIPGSRMGAIEEQEMAALAKDWLLSVPLTPSLIEIQKLVDASHTILINTHLAVEERELDYLRMVYPFKKIGILGPAMFSGFVEKGEKLAAKLLDKHINVKPAASRPLTPPETPPPGSPDTDSHGEEEDPKQKSVKQVEKFLAESATGSVVYISFGTMFRPQPTHLIKMLEIIIYEMSLSSQFRLLFTFGGSKDLASSCPPSFAPQISALESQLFKSGNTLFVNWVDQHYVLQHPSVGWFLSHGGWNSCQESMLAGTPLLILPFFGDQLFNAYFLESIQIAYRFNTAANMSVADFVASFREGITCTRPESERGSQLTKNAKELQLRLKGERALAEVRLF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias360-375Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM003162
EMBL· GenBank· DDBJ
KIS65763.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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