J4UHQ6 · OPS1_BEAB2

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).

Catalytic activity

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site549For beta-ketoacyl synthase activity
Active site684For beta-ketoacyl synthase activity
Active site724For beta-ketoacyl synthase activity
Active site1006For acyl/malonyl transferase activity
Active site1339Proton acceptor; for dehydratase activity
Active site1537Proton donor; for dehydratase activity

GO annotations

AspectTerm
Cellular Componentfatty acid synthase complex
Molecular Function3-oxoacyl-[acyl-carrier-protein] synthase activity
Molecular Functionfatty acid synthase activity
Molecular Functionphosphopantetheine binding
Biological Processfatty acid biosynthetic process
Biological Processsecondary metabolite biosynthetic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Orsellinic acid synthase
  • EC number
  • Short names
    OAS
  • Alternative names
    • Non-reducing polyketide synthase OpS1
    • Oosporein biosynthesis protein 1
    • Oosporein synthase

Gene names

    • Name
      OpS1
    • Synonyms
      PKS9
    • ORF names
      BBA_08179

Organism names

Accessions

  • Primary accession
    J4UHQ6

Proteomes

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Leads to the loss of oosporein production (PubMed:26305932).

Miscellaneous

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004385711-2211Orsellinic acid synthase
Modified residue1715O-(pantetheine 4'-phosphoryl)serine
Modified residue1824O-(pantetheine 4'-phosphoryl)serine

Keywords

Expression

Induction

Expression is positively regulated by the oosporein cluster specific regulator OpS3 that binds the promoter at a 5'-CGGA-3' motif (PubMed:26305932).
Expression is negatively regulated by the global transcription factor Msn2 that binds the stress-response element 5'-AGGGG-3' (PubMed:26305932).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region44-246N-terminal acylcarrier protein transacylase domain (SAT)
Domain380-805Ketosynthase family 3 (KS3)
Region910-1228Malonyl-CoA:ACP transacylase (MAT) domain
Region1309-1440N-terminal hotdog fold
Domain1309-1629PKS/mFAS DH
Region1334-1573Product template (PT) domain
Region1473-1629C-terminal hotdog fold
Domain1681-1755Carrier 1
Region1755-1786Disordered
Compositional bias1760-1786Polar residues
Domain1787-1865Carrier 2
Region1937-2204Thioesterase (TE) domain

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 status
    Complete
  • Length
    2,211
  • Mass (Da)
    237,462
  • Last updated
    2012-10-31 v1
  • Checksum
    ED327AD168F62FA7
MPSFFPVFSGLGSGSVFSEENVGRAEENALSPECAVLLQSCHRTFREQVSDAIARNILPEDSIDLDDFAEPASLIRPLSKYSRNVVMQHAALYLHQILAYMTSQKELGNLIGSAGFCTGLLPAAVAAASQTSVITLISQSHHFFQVALWIGIRSEQYRVDHLTNDTQDADGESMLPCSYVLEGVSEAAAQDLLHKTNMGNEVFVSAILSPTRVTISGIPTKLSTFISKHLPANCRTTVAVVHSLYHHESLLEVRNLVMADLERQDTLLQARVELSAPILSTKTGKPLALSSVTTLEQVACAILDLIFIEKVDWLNLQQSIVSHTSQDALDRPINIVNYGPGLGMAPSAFAQAQEKDVCIMDAAKISKGSFQNSGASRLAWDDIAIVGMAVELPGASDADTLWQNLVDGYQACSEIPPSRFNVNDYNNGKGSRTLNTKYGNFLENPFLFDAEHFGISRREAKSMDPQQRILLQTAYRALEDAGYVPDTTTSSARDTFGCWIGNATLDYVDNLRSDIDVYYSTGTLRAFLSARISYVFGWSGPSITLDTACSSSIVALHQAARSILAGDCRSALVGAANTITSPDMYLGLDRAHFLSPSGQCKAFDASADGYCRAEGCGVFVIKRLSDALAEGDRIHGVIKAIEINQSGNTHSITHPHVPTQEALFDKMFRESRINPHEISVVEMHGTGTQAGDPNEVESVRRALCKARSPLNPVYLTSLKANIGHAEAVSGIAGLAKLILMTRNGYIPPQVSLKTLNPRIRPLGVDGAAIDANGTEWPRAGPKKARMSMLNNFGAGGSNAAVIIGEHLSQDESEAQQPACGATIFVCGVSAKNDRALVKLQETVADYLTSAGQSRKPPSLADVCATLTSRRQMYNHRVAVVASSLEELAENLRSASSHNVSKSICEAPEAVFIFSGQGSQYLGMGRELIEQYEDFAHTVNVCDGWLVKNNYPSCLAVITGEQRESEDDKVDAHTWQSFQSAIYVIEVALAKLLESWGIRPQAVAGHSLGEYAALVTAGVIRLMDGLKLVAHRAKLMMEQCDLGQTSMLAVNCSAAVITSIIEASTDFEGLAISCNNSETDCVVGGPVPQLVLLKKHLTDRAQVRSKLLDVPMAFHTAAMDPILEEFTAFAAREVRVFPPTLPVVSNVLGRTVAVGEQAFSPEYFAKQCRGTVAFDDGIKHFLALGDCESTPYRWIEIGPHPSVQPMLRGRLGKAATSHIQLTTLKKNVPPASTLSQLLSHFYQTSSGVNWRSVFSRNAHRRFKLIQLPGMPFFPSEFHVPYREMAGEPASTSQSSGDAASNVVPNSFAVHAIQKLSHGASNSCAIYETPAVLLKEFIEGHLVCGYALCPASVYHEMVLAALNDCQSAAGSSVVWGLSKVSYCAPMVYDGNSNQVLRVVITPRLTLPDRYDFAVMSYVAGTDPNERSTVHCRGVVKQSNMASAELKYSRLQASMKGSMDGLKHVGQLGAPAASCVQVFSKRAMYEKIFTRVVEYSDPYQKVETIRIREDTGEALATCVSPAPYLARDSSIPASHAIFMDVLLHVAGFVSNLNLPNDVMGICKEVGGATTLRAPVVRDGACAPFDVYCSTFDTQDSDGRSFTISNAYAVDSSGVMAVFKGMVFQHVKIPLIEQALKRATRSSPNAAVSASHPAQPKRRNDVTSFVNAQSVERMALPRAAAPVRAAPEVSVPELVAKVCGLDAGQLGVDSRLDAHGVDSLMGIEIAAALSSALGVDVLPDTLGSCDTVGDIERLCEALSPTPVGNDVDNDSPTPGSERGSDSAISTPASVSTVDASSIDMVQIVAELCGARAEAVSPDSELRALGVDSLMFLELADRLQDLDRGIALSSNDLADCQTIGDIERLIVKRPGTPAYQSGISTKIYPEAVHASSEAVRLSAQQPATQISLLASEEAVLPQIERLLHLSQQPEEIQVGSLDRKFSGKSPLFLIHDGSGICTHYRGLRPLGRRVLALHDPKFLIQSSKQRSWASLTTMANEYASSISSTMGMTGGEDCILGGWSFGGVVAFEAARILMSRGHRVKGVVLIDSPPPIGHIPLSESIISAVTAQPAEKDAAAGSTTASKCVSPVASAIRKLVQQSFRICAGLIGDFGTSAELQQRGLSNKPVGPVPRVILLRSAVGWTPPRGYTGAAVEEMENPWLQDRRDRSLATAGWEILTGGPIQCLDIPGNHFQVFDAPNIAAVSAALVDACSEFELK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1760-1786Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JH725181
EMBL· GenBank· DDBJ
EJP62792.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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