AUSQ_PENBI
ID AUSQ_PENBI Reviewed; 516 AA.
AC A0A0F7TSZ1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=O-acyltransferase ausQ {ECO:0000303|PubMed:29076725};
DE EC=2.3.1.- {ECO:0000305|PubMed:29076725};
DE AltName: Full=Austinoid biosynthesis clusters protein Q {ECO:0000303|PubMed:29076725};
GN Name=ausQ {ECO:0000303|PubMed:29076725}; ORFNames=PMG11_06812;
OS Penicillium brasilianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=104259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG11;
RX PubMed=26337871; DOI=10.1128/genomea.00724-15;
RA Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Brakhage A.A.,
RA Valiante V.;
RT "Draft genome sequence of the fungus Penicillium brasilianum MG11.";
RL Genome Announc. 3:0-0(2015).
RN [2]
RP FUNCTION.
RX PubMed=27602587; DOI=10.1021/jacs.6b08424;
RA Matsuda Y., Iwabuchi T., Fujimoto T., Awakawa T., Nakashima Y., Mori T.,
RA Zhang H., Hayashi F., Abe I.;
RT "Discovery of key dioxygenases that diverged the paraherquonin and
RT acetoxydehydroaustin pathways in Penicillium brasilianum.";
RL J. Am. Chem. Soc. 138:12671-12677(2016).
RN [3]
RP FUNCTION.
RX PubMed=29076725; DOI=10.1021/acschembio.7b00814;
RA Mattern D.J., Valiante V., Horn F., Petzke L., Brakhage A.A.;
RT "Rewiring of the austinoid biosynthetic pathway in filamentous fungi.";
RL ACS Chem. Biol. 12:2927-2933(2017).
CC -!- FUNCTION: O-acyltransferase; part of the gene cluster B that mediates
CC the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin
CC (PubMed:29076725). The first step of the pathway is the synthesis of
CC 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By
CC similarity). 3,5-dimethylorsellinic acid is then prenylated by the
CC polyprenyl transferase ausN (By similarity). Further epoxidation by the
CC FAD-dependent monooxygenase ausM and cyclization by the probable
CC terpene cyclase ausL lead to the formation of protoaustinoid A (By
CC similarity). Protoaustinoid A is then oxidized to spiro-lactone
CC preaustinoid A3 by the combined action of the FAD-binding
CC monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity).
CC Acid-catalyzed keto-rearrangement and ring contraction of the
CC tetraketide portion of preaustinoid A3 by ausJ lead to the formation of
CC preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the
CC help of ausH, is involved in the next step by transforming preaustinoid
CC A4 into isoaustinone which is in turn hydroxylated by the P450
CC monooxygenase ausI to form austinolide (By similarity). The cytochrome
CC P450 monooxygenase ausG then modifies austinolide to austinol (By
CC similarity). Austinol is further acetylated to austin by the O-
CC acetyltransferase ausP, which spontaneously changes to dehydroaustin
CC (PubMed:29076725). The cytochrome P450 monooxygenase then converts
CC dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725). The
CC hydroxylation catalyzed by ausR permits the second O-acetyltransferase
CC ausQ to add an additional acetyl group to the molecule, leading to the
CC formation of acetoxydehydroaustin (PubMed:29076725). Due to genetic
CC rearrangements of the clusters and the subsequent loss of some enzymes,
CC the end product of the Penicillium brasilianum austinoid biosynthesis
CC clusters is acetoxydehydroaustin (PubMed:29076725).
CC {ECO:0000250|UniProtKB:A0A1U8QLK0, ECO:0000269|PubMed:29076725}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:29076725}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q4WZ64}.
CC -!- MISCELLANEOUS: In A.calidoustus, the austinoid gene cluster lies on a
CC contiguous DNA region, while clusters from E.nidulans and P.brasilianum
CC are split in their respective genomes. Genetic rearrangements provoked
CC variability among the clusters and E.nidulans produces the least number
CC of austionoid derivatives with the end products austinol and
CC dehydroaustinol, while P.brasilianum can produce until
CC acetoxydehydroaustin, and A.calidoustus produces the highest number of
CC identified derivatives. {ECO:0000305|PubMed:29076725}.
CC -!- SIMILARITY: Belongs to the fumigaclavine B O-acetyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CDHK01000006; CEJ58142.1; -; Genomic_DNA.
DR SMR; A0A0F7TSZ1; -.
DR EnsemblFungi; CEJ58142; CEJ58142; PMG11_06812.
DR OrthoDB; 1130893at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000042958; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 3: Inferred from homology;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..516
FT /note="O-acyltransferase ausQ"
FT /id="PRO_0000453869"
SQ SEQUENCE 516 AA; 56187 MW; 9B1B59C18DF3F048 CRC64;
MPSSSDFEAF ALTPLDQANG QVFFFYSISY QVQNEASALR TIHNGIDVLL ERVPFLNGEI
AFAAAVPGAN NILTVRPPTA NSKDQVPLVK VKRHSNRTLP VEKLEQSPFN VPRNLPLDGL
FNPLAAFPTP DRPTPVIRFQ INLVNDGLIL TLAFNHAVFD ALGAAVIVKL LAESCRNQEN
IGMAGSMGIP STQARVQSPL LALSSRLKKH NHVHANAPSS SEVSETISQR PVTAPPPLTD
ECFVFCAEKL QQLRIACASI LGKLNENQKS RAGQGDIRFL SSNDVLTALI CESIAQARHA
AKHTCRDEDL HAKSSVSECL MAVNLRKFVE PPLPDDYMGN AGIPLRFEVR TQRQAAPDFH
PAIREVPPGL NTSSFLAIAK TAYTIRAKLA RFGESYIDSL SSFLNADESQ TAVNVLPACA
IVSSLRHIKT YELQFGVELG EIQTFETGTP WVNGSCMILP LCANSSDVAG SAPWNVRITL
DEGTMDCFKN EPALRWALWD QAKSKVPGSC NCMTDA
