J4UHQ6 · OPS1_BEAB2
- ProteinOrsellinic acid synthase
- GeneOpS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2211 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects (PubMed:26305932).
The non-reducing polyketide synthase OpS1 produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:26305932).
Orsellinic acid is then hydroxylated to benzenetriol by the hydroxylase OpS4 (PubMed:26305932).
The intermediate is oxidized either nonenzymatically to 5,5'-dideoxy-oosporein or enzymatically to benzenetetrol by the oxidoreductase OpS7 (PubMed:26305932).
The latter is further dimerized to oosporein by the catalase OpS5 (PubMed:26305932).
OpS6 probably functions en route for protecting cells against oxidative stress by scavenging any leaked free radical form of benzenetetrol by activating the thiol group of glutathione (PubMed:26305932).
The non-reducing polyketide synthase OpS1 produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:26305932).
Orsellinic acid is then hydroxylated to benzenetriol by the hydroxylase OpS4 (PubMed:26305932).
The intermediate is oxidized either nonenzymatically to 5,5'-dideoxy-oosporein or enzymatically to benzenetetrol by the oxidoreductase OpS7 (PubMed:26305932).
The latter is further dimerized to oosporein by the catalase OpS5 (PubMed:26305932).
OpS6 probably functions en route for protecting cells against oxidative stress by scavenging any leaked free radical form of benzenetetrol by activating the thiol group of glutathione (PubMed:26305932).
Catalytic activity
- 3 malonyl-CoA + acetyl-CoA + 2 H+ = orsellinate + 3 CO2 + 4 CoAThis reaction proceeds in the forward direction.
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 549 | For beta-ketoacyl synthase activity | ||||
Sequence: C | ||||||
Active site | 684 | For beta-ketoacyl synthase activity | ||||
Sequence: H | ||||||
Active site | 724 | For beta-ketoacyl synthase activity | ||||
Sequence: H | ||||||
Active site | 1006 | For acyl/malonyl transferase activity | ||||
Sequence: S | ||||||
Active site | 1339 | Proton acceptor; for dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1537 | Proton donor; for dehydratase activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fatty acid synthase complex | |
Molecular Function | 3-oxoacyl-[acyl-carrier-protein] synthase activity | |
Molecular Function | fatty acid synthase activity | |
Molecular Function | phosphopantetheine binding | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | secondary metabolite biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameOrsellinic acid synthase
- EC number
- Short namesOAS
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Cordycipitaceae > Beauveria
Accessions
- Primary accessionJ4UHQ6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000438571 | 1-2211 | Orsellinic acid synthase | |||
Sequence: MPSFFPVFSGLGSGSVFSEENVGRAEENALSPECAVLLQSCHRTFREQVSDAIARNILPEDSIDLDDFAEPASLIRPLSKYSRNVVMQHAALYLHQILAYMTSQKELGNLIGSAGFCTGLLPAAVAAASQTSVITLISQSHHFFQVALWIGIRSEQYRVDHLTNDTQDADGESMLPCSYVLEGVSEAAAQDLLHKTNMGNEVFVSAILSPTRVTISGIPTKLSTFISKHLPANCRTTVAVVHSLYHHESLLEVRNLVMADLERQDTLLQARVELSAPILSTKTGKPLALSSVTTLEQVACAILDLIFIEKVDWLNLQQSIVSHTSQDALDRPINIVNYGPGLGMAPSAFAQAQEKDVCIMDAAKISKGSFQNSGASRLAWDDIAIVGMAVELPGASDADTLWQNLVDGYQACSEIPPSRFNVNDYNNGKGSRTLNTKYGNFLENPFLFDAEHFGISRREAKSMDPQQRILLQTAYRALEDAGYVPDTTTSSARDTFGCWIGNATLDYVDNLRSDIDVYYSTGTLRAFLSARISYVFGWSGPSITLDTACSSSIVALHQAARSILAGDCRSALVGAANTITSPDMYLGLDRAHFLSPSGQCKAFDASADGYCRAEGCGVFVIKRLSDALAEGDRIHGVIKAIEINQSGNTHSITHPHVPTQEALFDKMFRESRINPHEISVVEMHGTGTQAGDPNEVESVRRALCKARSPLNPVYLTSLKANIGHAEAVSGIAGLAKLILMTRNGYIPPQVSLKTLNPRIRPLGVDGAAIDANGTEWPRAGPKKARMSMLNNFGAGGSNAAVIIGEHLSQDESEAQQPACGATIFVCGVSAKNDRALVKLQETVADYLTSAGQSRKPPSLADVCATLTSRRQMYNHRVAVVASSLEELAENLRSASSHNVSKSICEAPEAVFIFSGQGSQYLGMGRELIEQYEDFAHTVNVCDGWLVKNNYPSCLAVITGEQRESEDDKVDAHTWQSFQSAIYVIEVALAKLLESWGIRPQAVAGHSLGEYAALVTAGVIRLMDGLKLVAHRAKLMMEQCDLGQTSMLAVNCSAAVITSIIEASTDFEGLAISCNNSETDCVVGGPVPQLVLLKKHLTDRAQVRSKLLDVPMAFHTAAMDPILEEFTAFAAREVRVFPPTLPVVSNVLGRTVAVGEQAFSPEYFAKQCRGTVAFDDGIKHFLALGDCESTPYRWIEIGPHPSVQPMLRGRLGKAATSHIQLTTLKKNVPPASTLSQLLSHFYQTSSGVNWRSVFSRNAHRRFKLIQLPGMPFFPSEFHVPYREMAGEPASTSQSSGDAASNVVPNSFAVHAIQKLSHGASNSCAIYETPAVLLKEFIEGHLVCGYALCPASVYHEMVLAALNDCQSAAGSSVVWGLSKVSYCAPMVYDGNSNQVLRVVITPRLTLPDRYDFAVMSYVAGTDPNERSTVHCRGVVKQSNMASAELKYSRLQASMKGSMDGLKHVGQLGAPAASCVQVFSKRAMYEKIFTRVVEYSDPYQKVETIRIREDTGEALATCVSPAPYLARDSSIPASHAIFMDVLLHVAGFVSNLNLPNDVMGICKEVGGATTLRAPVVRDGACAPFDVYCSTFDTQDSDGRSFTISNAYAVDSSGVMAVFKGMVFQHVKIPLIEQALKRATRSSPNAAVSASHPAQPKRRNDVTSFVNAQSVERMALPRAAAPVRAAPEVSVPELVAKVCGLDAGQLGVDSRLDAHGVDSLMGIEIAAALSSALGVDVLPDTLGSCDTVGDIERLCEALSPTPVGNDVDNDSPTPGSERGSDSAISTPASVSTVDASSIDMVQIVAELCGARAEAVSPDSELRALGVDSLMFLELADRLQDLDRGIALSSNDLADCQTIGDIERLIVKRPGTPAYQSGISTKIYPEAVHASSEAVRLSAQQPATQISLLASEEAVLPQIERLLHLSQQPEEIQVGSLDRKFSGKSPLFLIHDGSGICTHYRGLRPLGRRVLALHDPKFLIQSSKQRSWASLTTMANEYASSISSTMGMTGGEDCILGGWSFGGVVAFEAARILMSRGHRVKGVVLIDSPPPIGHIPLSESIISAVTAQPAEKDAAAGSTTASKCVSPVASAIRKLVQQSFRICAGLIGDFGTSAELQQRGLSNKPVGPVPRVILLRSAVGWTPPRGYTGAAVEEMENPWLQDRRDRSLATAGWEILTGGPIQCLDIPGNHFQVFDAPNIAAVSAALVDACSEFELK | ||||||
Modified residue | 1715 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S | ||||||
Modified residue | 1824 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
Expression
Induction
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 44-246 | N-terminal acylcarrier protein transacylase domain (SAT) | ||||
Sequence: TFREQVSDAIARNILPEDSIDLDDFAEPASLIRPLSKYSRNVVMQHAALYLHQILAYMTSQKELGNLIGSAGFCTGLLPAAVAAASQTSVITLISQSHHFFQVALWIGIRSEQYRVDHLTNDTQDADGESMLPCSYVLEGVSEAAAQDLLHKTNMGNEVFVSAILSPTRVTISGIPTKLSTFISKHLPANCRTTVAVVHSLYH | ||||||
Domain | 380-805 | Ketosynthase family 3 (KS3) | ||||
Sequence: WDDIAIVGMAVELPGASDADTLWQNLVDGYQACSEIPPSRFNVNDYNNGKGSRTLNTKYGNFLENPFLFDAEHFGISRREAKSMDPQQRILLQTAYRALEDAGYVPDTTTSSARDTFGCWIGNATLDYVDNLRSDIDVYYSTGTLRAFLSARISYVFGWSGPSITLDTACSSSIVALHQAARSILAGDCRSALVGAANTITSPDMYLGLDRAHFLSPSGQCKAFDASADGYCRAEGCGVFVIKRLSDALAEGDRIHGVIKAIEINQSGNTHSITHPHVPTQEALFDKMFRESRINPHEISVVEMHGTGTQAGDPNEVESVRRALCKARSPLNPVYLTSLKANIGHAEAVSGIAGLAKLILMTRNGYIPPQVSLKTLNPRIRPLGVDGAAIDANGTEWPRAGPKKARMSMLNNFGAGGSNAAVIIGE | ||||||
Region | 910-1228 | Malonyl-CoA:ACP transacylase (MAT) domain | ||||
Sequence: VFIFSGQGSQYLGMGRELIEQYEDFAHTVNVCDGWLVKNNYPSCLAVITGEQRESEDDKVDAHTWQSFQSAIYVIEVALAKLLESWGIRPQAVAGHSLGEYAALVTAGVIRLMDGLKLVAHRAKLMMEQCDLGQTSMLAVNCSAAVITSIIEASTDFEGLAISCNNSETDCVVGGPVPQLVLLKKHLTDRAQVRSKLLDVPMAFHTAAMDPILEEFTAFAAREVRVFPPTLPVVSNVLGRTVAVGEQAFSPEYFAKQCRGTVAFDDGIKHFLALGDCESTPYRWIEIGPHPSVQPMLRGRLGKAATSHIQLTTLKKNVP | ||||||
Region | 1309-1440 | N-terminal hotdog fold | ||||
Sequence: HAIQKLSHGASNSCAIYETPAVLLKEFIEGHLVCGYALCPASVYHEMVLAALNDCQSAAGSSVVWGLSKVSYCAPMVYDGNSNQVLRVVITPRLTLPDRYDFAVMSYVAGTDPNERSTVHCRGVVKQSNMAS | ||||||
Domain | 1309-1629 | PKS/mFAS DH | ||||
Sequence: HAIQKLSHGASNSCAIYETPAVLLKEFIEGHLVCGYALCPASVYHEMVLAALNDCQSAAGSSVVWGLSKVSYCAPMVYDGNSNQVLRVVITPRLTLPDRYDFAVMSYVAGTDPNERSTVHCRGVVKQSNMASAELKYSRLQASMKGSMDGLKHVGQLGAPAASCVQVFSKRAMYEKIFTRVVEYSDPYQKVETIRIREDTGEALATCVSPAPYLARDSSIPASHAIFMDVLLHVAGFVSNLNLPNDVMGICKEVGGATTLRAPVVRDGACAPFDVYCSTFDTQDSDGRSFTISNAYAVDSSGVMAVFKGMVFQHVKIPLIE | ||||||
Region | 1334-1573 | Product template (PT) domain | ||||
Sequence: EFIEGHLVCGYALCPASVYHEMVLAALNDCQSAAGSSVVWGLSKVSYCAPMVYDGNSNQVLRVVITPRLTLPDRYDFAVMSYVAGTDPNERSTVHCRGVVKQSNMASAELKYSRLQASMKGSMDGLKHVGQLGAPAASCVQVFSKRAMYEKIFTRVVEYSDPYQKVETIRIREDTGEALATCVSPAPYLARDSSIPASHAIFMDVLLHVAGFVSNLNLPNDVMGICKEVGGATTLRAPVV | ||||||
Region | 1473-1629 | C-terminal hotdog fold | ||||
Sequence: VQVFSKRAMYEKIFTRVVEYSDPYQKVETIRIREDTGEALATCVSPAPYLARDSSIPASHAIFMDVLLHVAGFVSNLNLPNDVMGICKEVGGATTLRAPVVRDGACAPFDVYCSTFDTQDSDGRSFTISNAYAVDSSGVMAVFKGMVFQHVKIPLIE | ||||||
Domain | 1681-1755 | Carrier 1 | ||||
Sequence: AAPEVSVPELVAKVCGLDAGQLGVDSRLDAHGVDSLMGIEIAAALSSALGVDVLPDTLGSCDTVGDIERLCEALS | ||||||
Region | 1755-1786 | Disordered | ||||
Sequence: SPTPVGNDVDNDSPTPGSERGSDSAISTPASV | ||||||
Compositional bias | 1760-1786 | Polar residues | ||||
Sequence: GNDVDNDSPTPGSERGSDSAISTPASV | ||||||
Domain | 1787-1865 | Carrier 2 | ||||
Sequence: STVDASSIDMVQIVAELCGARAEAVSPDSELRALGVDSLMFLELADRLQDLDRGIALSSNDLADCQTIGDIERLIVKRP | ||||||
Region | 1937-2204 | Thioesterase (TE) domain | ||||
Sequence: SGKSPLFLIHDGSGICTHYRGLRPLGRRVLALHDPKFLIQSSKQRSWASLTTMANEYASSISSTMGMTGGEDCILGGWSFGGVVAFEAARILMSRGHRVKGVVLIDSPPPIGHIPLSESIISAVTAQPAEKDAAAGSTTASKCVSPVASAIRKLVQQSFRICAGLIGDFGTSAELQQRGLSNKPVGPVPRVILLRSAVGWTPPRGYTGAAVEEMENPWLQDRRDRSLATAGWEILTGGPIQCLDIPGNHFQVFDAPNIAAVSAALVDA |
Domain
Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm (By similarity).
The release of the polyketide chain from the non-reducing polyketide synthase is mediated by the thioesterase (TE) domain localized at the C-ter of the protein (By similarity).
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,211
- Mass (Da)237,462
- Last updated2012-10-31 v1
- ChecksumED327AD168F62FA7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1760-1786 | Polar residues | ||||
Sequence: GNDVDNDSPTPGSERGSDSAISTPASV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JH725181 EMBL· GenBank· DDBJ | EJP62792.1 EMBL· GenBank· DDBJ | Genomic DNA |