A0A0D2YG02 · FUB7_FUSO4
- ProteinSulfhydrylase FUB7
- GeneFUB7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids433 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Sulfhydrylase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:25372119).
L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity).
The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity).
FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity).
Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity).
Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity).
The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity).
FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity).
Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity).
Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
Cofactor
Biotechnology
Fusaric acid is phytotoxic to plants such as cotton and banana (PubMed:20955724, PubMed:23922960).
It has been shown to induce programmed cell death in plants (PubMed:16868776, PubMed:23838885).
In addition to a mild toxicity to animals, fusaric acid exhibits acanthamoebicidal, antioomycete, and antimycobacterial activities (PubMed:17927749, PubMed:21811925, PubMed:22864988).
It has been shown to induce programmed cell death in plants (PubMed:16868776, PubMed:23838885).
In addition to a mild toxicity to animals, fusaric acid exhibits acanthamoebicidal, antioomycete, and antimycobacterial activities (PubMed:17927749, PubMed:21811925, PubMed:22864988).
Pathway
Mycotoxin biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | transferase activity, transferring alkyl or aryl (other than methyl) groups | |
Biological Process | transsulfuration |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSulfhydrylase FUB7
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium > Fusarium oxysporum species complex
Accessions
- Primary accessionA0A0D2YG02
Proteomes
Organism-specific databases
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000437338 | 1-433 | Sulfhydrylase FUB7 | |||
Sequence: MAEQVFQNFETLQLHAGYTPDPHTRSTAVPIYATSSYTFNDSAHGARLFGLKELGNIYSRLMNPTVDVFEKRIAALEGGIAAAATSSGQAAQFLTIATLAKAGDNIVASSHLYGGTYNQLNVLLPRFGIKTKFVRSGKLEDYAAAIDDQTRAIYVESMSNPDYVVPDFEGIAKIAHEHGIPLVVDNTLGAGGYYIRPIEHGADIVVHSATKWIGGHGTTIGGVIVDSGRFNWNKHSERFPEMVEPSPSYHGLKYWEAFGPATFITRIRVEMLRDIGACLSPFSAQQLLLGIETLGLRAERHAQNTEKLAKYFESSPNVSWVLWPGSESHPTYAQAKKYLTRGFGAMLSIGVKGDASAGSKVVDGLKLVSNLANVGDAKSLAIHPWSTTHEQLSEDERLASGVTEDMIRISVGIEHVDDIIADFEQSFQKAYGS | ||||||
Modified residue | 211 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length433
- Mass (Da)47,110
- Last updated2015-04-29 v1
- Checksum6C1F64DEABE346F0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS231721 EMBL· GenBank· DDBJ | KNB17098.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17099.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17100.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17101.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17102.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17103.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17104.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17105.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17106.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17107.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17108.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17109.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17110.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17111.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DS231721 EMBL· GenBank· DDBJ | KNB17112.1 EMBL· GenBank· DDBJ | Genomic DNA |