G0R6T3 · SORD_HYPJQ
- ProteinFAD-linked oxidoreductase sor8
- Genesor8
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids574 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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).
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
Pathway
Secondary metabolite biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | FAD binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFAD-linked oxidoreductase sor8
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma
Accessions
- Primary accessionG0R6T3
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MYAPPFVRAFGIAVLAVLPSFSSPATA | ||||||
Chain | PRO_5003408468 | 28-574 | FAD-linked oxidoreductase sor8 | |||
Sequence: ASLKSSGSSSSCRCFPGDACWPSPADWKAFNQSVGGRLIATVPLGSVCHGTTYDAARCADVKAAWPYADTHTDSSSSVLAPFFANQSCDPFLPRETPCVIGTYVQYAVNVSSVADIQKTLAFSQKKNLRLVVRNTGHDYFGKSTGAGGLGLWMHNLKTYDIHDYKSAAYTGKAVTMGAGIQAGESAATAFKQGLTIVSGICPTVGLAGGYTQGGGLGPLTTRYGLGADQVLEWHAVLANGSEITATPTKNSDLYWALTGGGGGTYAVVYSMTVKAHANEKTTGANLTFPNAGSEDVFFQGVQAFHDIIPAISDAGGTAVWTVLSKALSVGPVTGPNMTKATMDSIFQPVLQKLDALNITYSYSSGEFSSFYESNAAYDPPVVSNGLQIGGRLVKRSDFTGNPDGFIQAIRGIADQGGLVTGASYQLSSSLQHPPNSVNPELRKSLISFQIGVPWINTDWATDLHNQDLITNSFVPALAALLPSGGSAYLNQADFREPGWQQVFYGENYEKLLELKDVYDPNGVFWGRTTVGSERWAETEDKRLCRVS | ||||||
Glycosylation | 58 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 112 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 136 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 266 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 312 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 363 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 384 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 126-305 | FAD-binding PCMH-type | ||||
Sequence: VIGTYVQYAVNVSSVADIQKTLAFSQKKNLRLVVRNTGHDYFGKSTGAGGLGLWMHNLKTYDIHDYKSAAYTGKAVTMGAGIQAGESAATAFKQGLTIVSGICPTVGLAGGYTQGGGLGPLTTRYGLGADQVLEWHAVLANGSEITATPTKNSDLYWALTGGGGGTYAVVYSMTVKAHAN |
Sequence similarities
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length574
- Mass (Da)60,910
- Last updated2011-10-19 v1
- ChecksumC42A715A9828DD06
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL985056 EMBL· GenBank· DDBJ | EGR52692.1 EMBL· GenBank· DDBJ | Genomic DNA |