G0R6T3 · SORD_HYPJQ

Function

function

FAD-linked oxidoreductase; part of the SOR gene cluster that mediates the biosynthesis of sorbicillinoids, a diverse group of yellow secondary metabolites that restrict growth of competing pathogenic fungi but not of bacteria (PubMed:29104566).
Sorbicillinoids biosynthesis requires the action of two PKSs (PubMed:28809958).
The SOR cluster is required for the production of trichodimerol and dihydrotrichotetronin, with sor2 being sufficient for production of trichodimerol, but not dihydrotrichotetronin in the light (PubMed:28809958).
Sor1 iteratively combines three acetyl units and the growing chain is modified by the ketoacyl reductase subunit, and optional by the enoyl reductase subunit in the second cycle (By similarity).
The polyketide is then handed over to the PKS sor2, which adds three more acetyl units, and two methyl groups (By similarity).
Sor2 releases an aldehyde, which undergoes spontaneous cyclization resulting in the formation of sorbicillin or 2',3'-dihydrosorbicillin (By similarity).
The monooxygenase sor5 oxidizes sorbicillin and 2',3'-dihydrosorbicillin to 2',3'-dihydrosorbicillinol and sorbicillinol, respectively (PubMed:29104566).
The oxidoreductase sor8 further converts sorbicillinol into oxosorbicillinol (PubMed:29104566).
Sorbicillinol is the building block for the other sorbicillinoids such as disorbicillinol, bisvertinolon, dihydrobisvertinolone, and dihydrotrichotetronine (PubMed:28809958, PubMed:29104566).

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Pathway

Secondary metabolite biosynthesis.

GO annotations

AspectTerm
Molecular FunctionFAD binding
Molecular Functionoxidoreductase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    FAD-linked oxidoreductase sor8
  • EC number
  • Alternative names
    • Sorbicillinoid biosynthetic cluster protein 8

Gene names

    • Name
      sor8
    • Synonyms
      sor4
    • ORF names
      TRIREDRAFT_73631

Organism names

Accessions

  • Primary accession
    G0R6T3

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Leads to the accumulation of dihydrosorbicillinol as well as to higher amounts of oxosorbicillinol (PubMed:29104566).

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-27
ChainPRO_500340846828-574FAD-linked oxidoreductase sor8
Glycosylation58N-linked (GlcNAc...) asparagine
Glycosylation112N-linked (GlcNAc...) asparagine
Glycosylation136N-linked (GlcNAc...) asparagine
Glycosylation266N-linked (GlcNAc...) asparagine
Glycosylation312N-linked (GlcNAc...) asparagine
Glycosylation363N-linked (GlcNAc...) asparagine
Glycosylation384N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain126-305FAD-binding PCMH-type

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    574
  • Mass (Da)
    60,910
  • Last updated
    2011-10-19 v1
  • Checksum
    C42A715A9828DD06
MYAPPFVRAFGIAVLAVLPSFSSPATAASLKSSGSSSSCRCFPGDACWPSPADWKAFNQSVGGRLIATVPLGSVCHGTTYDAARCADVKAAWPYADTHTDSSSSVLAPFFANQSCDPFLPRETPCVIGTYVQYAVNVSSVADIQKTLAFSQKKNLRLVVRNTGHDYFGKSTGAGGLGLWMHNLKTYDIHDYKSAAYTGKAVTMGAGIQAGESAATAFKQGLTIVSGICPTVGLAGGYTQGGGLGPLTTRYGLGADQVLEWHAVLANGSEITATPTKNSDLYWALTGGGGGTYAVVYSMTVKAHANEKTTGANLTFPNAGSEDVFFQGVQAFHDIIPAISDAGGTAVWTVLSKALSVGPVTGPNMTKATMDSIFQPVLQKLDALNITYSYSSGEFSSFYESNAAYDPPVVSNGLQIGGRLVKRSDFTGNPDGFIQAIRGIADQGGLVTGASYQLSSSLQHPPNSVNPELRKSLISFQIGVPWINTDWATDLHNQDLITNSFVPALAALLPSGGSAYLNQADFREPGWQQVFYGENYEKLLELKDVYDPNGVFWGRTTVGSERWAETEDKRLCRVS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL985056
EMBL· GenBank· DDBJ
EGR52692.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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