G4N4J5 · LIDS_PYRO7
- Protein7,8-linoleate diol synthase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1171 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)-octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE).
Catalytic activity
- (9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoateThis reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 213 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 214 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 229 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 231 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 233 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 235 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 385 | |||||
Sequence: Y | ||||||
Binding site | 388 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 1089 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | dioxygenase activity | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Molecular Function | isomerase activity | |
Molecular Function | monooxygenase activity | |
Molecular Function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | |
Molecular Function | peroxidase activity | |
Biological Process | fatty acid metabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended name7,8-linoleate diol synthase
- Short namesLDS
Including 2 domains:
- Recommended nameLinoleate 8R-lipoxygenase
- EC number
- Recommended name9,12-octadecadienoate 8-hydroperoxide 8R-isomerase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Magnaporthales > Pyriculariaceae > Pyricularia
Accessions
- Primary accessionG4N4J5
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Impairs the production of 8-hydroperoxy-8(E),12(Z)-octadecadienoic acid (8-HPODE) and 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE) (PubMed:20023302).
Does not affect appressoria and conidia formation, nor the infection of rice leaves and roots (PubMed:20023302).
Does not affect appressoria and conidia formation, nor the infection of rice leaves and roots (PubMed:20023302).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 350 | Does not affect the enzymatic oxidation of linoleic acid (18:2n-6). | ||||
Sequence: S → D | ||||||
Mutagenesis | 753 | Does not affect the enzymatic oxidation of linoleic acid (18:2n-6). | ||||
Sequence: S → E | ||||||
Mutagenesis | 946 | Forms only small amounts of the 7,8-diol. | ||||
Sequence: N → V | ||||||
Mutagenesis | 975 | Does not affect the enzymatic oxidation of linoleic acid (18:2n-6). | ||||
Sequence: S → D | ||||||
Mutagenesis | 998 | Does not affect the enzymatic oxidation of linoleic acid (18:2n-6). | ||||
Sequence: T → E | ||||||
Mutagenesis | 1098 | Does not affect the enzymatic oxidation of linoleic acid (18:2n-6). | ||||
Sequence: T → D |
Miscellaneous
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458149 | 1-1171 | 7,8-linoleate diol synthase | |||
Sequence: MASSSSSGSSTRSSSPSDPPSSFFQKLGAFLGLFSKPQPPRPDYPHAPGNSAREEQTDITEDIQKLGFKDVETLLLYLNSSVKGVNDDKQLLLERLIQLLSKLPPTSTNGKKVTDGLITGLWESLDHPPVSSLGEKYRFREADGSNNNIHNPTLGVAGSHYARSAKPMVYQNPNPPAPETIFDTLMARDPAKFRPHPNQISSVLFYFATIITHDIFQTSSRDPSINLTSSYLDLSPLYGRNLEEQLSVRAMKDGLLKPDTFCSKRVHGFPPGVGVLLIMFNRFHNYVVTSLAKINEGNRFKKPVGDDTAAWEKYDNDLFQTGRLITCGLYVNIVLVDYVRTILNLNRVDSSWILDPRTEEGKSLLSKPTPEAVGNQVSVEFNLIYRWHCGMSQRDDKWTTDMLTEALGGKDPATATLPEFFGALGRFESSFPNEPEKRTLAGLKRQEDGSFEDEGLIKIMQESIEEVAGAFGPNHVPACMRAIEILGMNQARSWNVATLNEFREFIGLKRYDTFEDINPDPKVANLLAEFYGSPDAVELYPGINAEAPKPVIVPGSGLCPPSTTGRAILSDAVTLVRGDRFFTVDYTPRNLTNFGYQEAATDKSVDNGNVIYKLFFRAFPNHYAQNSIYAHFPFVIPSENKKIMESLGLADKYSWQPPQRKPATQMIRSHAAAVKILNNQKDFKVVWGESIGFLTKFPTGENPGLGFALAGDAPANQQSRDQLMKCIFSPKAWEDEVRQFCEATTWDLLRRYSAKVQDKGPHLKVHTHEIDVIRDVISLANARFFAAVYSLPLKTENGDDGVYSDHEMYRSLMLIFSAIFWDNDVSKSFKLRRDARAATQKLGALVEKHIVEMGSLFHSFKHSHSAVSDKTNGLANGGANGHANGNANGHTNGNGIHQNGGAAPSMLRSYGDLMLRRMIEAYGEGKSVKEAVYGQIMPSIAAGTANQTQIMAQCLDYYMSDDGAEHLPEMKRLASLETPEAFNTLMKYLFEGARIRNTTAVPRLVATDQTVEDNIPCLPDPKDSTFLRPIPNPQQAETTRTVKLSRGSMVLVDLTVAAHDATAFPDPEKVRLDRDLDSYTFFGLGPHRCAGDKVVRITMTAVFKVLLQLDGLRRAEGGRGVFKSLPASQWNGQAGRVAGEKPQWSGLRTYVNADESAFSQTPMNMKIRWDD |
Interaction
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MASSSSSGSSTRSSSPSDPPSS | ||||||
Region | 1-56 | Disordered | ||||
Sequence: MASSSSSGSSTRSSSPSDPPSSFFQKLGAFLGLFSKPQPPRPDYPHAPGNSAREEQ | ||||||
Region | 114-457 | Fatty acid alpha-dioxygenase | ||||
Sequence: TDGLITGLWESLDHPPVSSLGEKYRFREADGSNNNIHNPTLGVAGSHYARSAKPMVYQNPNPPAPETIFDTLMARDPAKFRPHPNQISSVLFYFATIITHDIFQTSSRDPSINLTSSYLDLSPLYGRNLEEQLSVRAMKDGLLKPDTFCSKRVHGFPPGVGVLLIMFNRFHNYVVTSLAKINEGNRFKKPVGDDTAAWEKYDNDLFQTGRLITCGLYVNIVLVDYVRTILNLNRVDSSWILDPRTEEGKSLLSKPTPEAVGNQVSVEFNLIYRWHCGMSQRDDKWTTDMLTEALGGKDPATATLPEFFGALGRFESSFPNEPEKRTLAGLKRQEDGSFEDEGLI | ||||||
Region | 675-1171 | Epoxy alcohol synthase | ||||
Sequence: KILNNQKDFKVVWGESIGFLTKFPTGENPGLGFALAGDAPANQQSRDQLMKCIFSPKAWEDEVRQFCEATTWDLLRRYSAKVQDKGPHLKVHTHEIDVIRDVISLANARFFAAVYSLPLKTENGDDGVYSDHEMYRSLMLIFSAIFWDNDVSKSFKLRRDARAATQKLGALVEKHIVEMGSLFHSFKHSHSAVSDKTNGLANGGANGHANGNANGHTNGNGIHQNGGAAPSMLRSYGDLMLRRMIEAYGEGKSVKEAVYGQIMPSIAAGTANQTQIMAQCLDYYMSDDGAEHLPEMKRLASLETPEAFNTLMKYLFEGARIRNTTAVPRLVATDQTVEDNIPCLPDPKDSTFLRPIPNPQQAETTRTVKLSRGSMVLVDLTVAAHDATAFPDPEKVRLDRDLDSYTFFGLGPHRCAGDKVVRITMTAVFKVLLQLDGLRRAEGGRGVFKSLPASQWNGQAGRVAGEKPQWSGLRTYVNADESAFSQTPMNMKIRWDD | ||||||
Compositional bias | 873-899 | Polar residues | ||||
Sequence: GLANGGANGHANGNANGHTNGNGIHQN | ||||||
Region | 873-900 | Disordered | ||||
Sequence: GLANGGANGHANGNANGHTNGNGIHQNG |
Sequence similarities
In the N-terminal section; belongs to the peroxidase family.
In the C-terminal section; belongs to the cytochrome P450 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,171
- Mass (Da)129,879
- Last updated2011-12-14 v1
- Checksum0CB47BAF1CE97EAF
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MASSSSSGSSTRSSSPSDPPSS | ||||||
Compositional bias | 873-899 | Polar residues | ||||
Sequence: GLANGGANGHANGNANGHTNGNGIHQN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM001233 EMBL· GenBank· DDBJ | EHA52010.1 EMBL· GenBank· DDBJ | Genomic DNA |