emeni-q5atj7

Emericella nidulans (Aspergillus nidulans) Non-reducing polyketide synthase ausA

Comment

(from Uniprot) Non-reducing polyketide synthase\; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional. Other strains: Emericella nidulans (strain FGSC A4 \/ ATCC 38163 \/ CBS 112.46 \/ NRRL 194 \/ M139) (Aspergillus nidulans) || Only 2404-2445\/ 2476 residu a\/b hydrolase

Relationship

Family : BD-FAE

Block : H

Position in NCBI Life Tree : Aspergillus nidulans FGSC A4

Molecular evidence

No mutation

No structure

No kinetic

No disease

No substrate

No inhibitor

Database

Sequence

Peptide

EQTVLYNTRD GLELFADIYY PEKTDRSGAK RPIALLIHGG GHIMLSRKEI HHEQVRMLFD MGFLPVSIDY RLCPEVSLLD GPMQDACDAL AWARNKLPQL QLQRRDILPD GNNVVAVGWS TGGHLAMTLA WTAPARGVSA PEAILSFYSP TDYTDPFWSK PNFPYRVDVS TSDIQTGNPL DALQDAPISG YNPPPSKRAL GGWMAPSDPR SRIALYMNWT GQTLPVLFYG CNYRARAAES GQDYEVVLPE PILSEVQKVC PFSQISAGSY RAPTFLIHGT LDDLIPVQQA QRTHDKMQAC GVDSDLRIVR DGLHLFDLEA NFAGNQHAFQ AVVDGYEFLR RHVGL

References

Title : Spiro-ring formation is catalyzed by a multifunctional dioxygenase in austinol biosynthesis - Matsuda_2013_J.Am.Chem.Soc_135_10962
Author(s) : Matsuda Y , Awakawa T , Wakimoto T , Abe I
Ref : Journal of the American Chemical Society , 135 :10962 , 2013
Abstract : Matsuda_2013_J.Am.Chem.Soc_135_10962
ESTHER : Matsuda_2013_J.Am.Chem.Soc_135_10962
PubMedSearch : Matsuda_2013_J.Am.Chem.Soc_135_10962
PubMedID: 23865690
Gene_locus related to this paper: emeni-q5atj7

Title : Two separate gene clusters encode the biosynthetic pathway for the meroterpenoids austinol and dehydroaustinol in Aspergillus nidulans - Lo_2012_J.Am.Chem.Soc_134_4709
Author(s) : Lo HC , Entwistle R , Guo CJ , Ahuja M , Szewczyk E , Hung JH , Chiang YM , Oakley BR , Wang CC
Ref : Journal of the American Chemical Society , 134 :4709 , 2012
Abstract : Lo_2012_J.Am.Chem.Soc_134_4709
ESTHER : Lo_2012_J.Am.Chem.Soc_134_4709
PubMedSearch : Lo_2012_J.Am.Chem.Soc_134_4709
PubMedID: 22329759
Gene_locus related to this paper: emeni-q5atj7