ID   AUSQ_EMENI              Reviewed;         516 AA.
AC   A0A1U8QLK0; C8VQ87; Q5AR30;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=O-acyltransferase ausQ {ECO:0000303|PubMed:29076725};
DE            EC=2.3.1.- {ECO:0000269|PubMed:29076725};
DE   AltName: Full=Austinoid biosynthesis clusters protein Q {ECO:0000303|PubMed:29076725};
GN   Name=ausQ {ECO:0000303|PubMed:29076725}; ORFNames=AN9250, ANIA_09250;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   FUNCTION.
RX   PubMed=22234162; DOI=10.1021/cb200455u;
RA   Rodriguez-Urra A.B., Jimenez C., Nieto M.I., Rodriguez J., Hayashi H.,
RA   Ugalde U.;
RT   "Signaling the induction of sporulation involves the interaction of two
RT   secondary metabolites in Aspergillus nidulans.";
RL   ACS Chem. Biol. 7:599-606(2012).
RN   [4]
RP   FUNCTION.
RX   PubMed=22329759; DOI=10.1021/ja209809t;
RA   Lo H.C., Entwistle R., Guo C.J., Ahuja M., Szewczyk E., Hung J.H.,
RA   Chiang Y.M., Oakley B.R., Wang C.C.;
RT   "Two separate gene clusters encode the biosynthetic pathway for the
RT   meroterpenoids austinol and dehydroaustinol in Aspergillus nidulans.";
RL   J. Am. Chem. Soc. 134:4709-4720(2012).
RN   [5]
RP   FUNCTION.
RX   PubMed=23865690; DOI=10.1021/ja405518u;
RA   Matsuda Y., Awakawa T., Wakimoto T., Abe I.;
RT   "Spiro-ring formation is catalyzed by a multifunctional dioxygenase in
RT   austinol biosynthesis.";
RL   J. Am. Chem. Soc. 135:10962-10965(2013).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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 austinol and dehydroaustinol, two fungal
CC       meroterpenoids (PubMed:22329759). The first step of the pathway is the
CC       synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase
CC       ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated
CC       by the polyprenyl transferase ausN (PubMed:22329759). Further
CC       epoxidation by the FAD-dependent monooxygenase ausM and cyclization by
CC       the probable terpene cyclase ausL lead to the formation of
CC       protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized
CC       to spiro-lactone preaustinoid A3 by the combined action of the FAD-
CC       binding monooxygenases ausB and ausC, and the dioxygenase ausE
CC       (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement
CC       and ring contraction of the tetraketide portion of preaustinoid A3 by
CC       ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The
CC       aldo-keto reductase ausK, with the help of ausH, is involved in the
CC       next step by transforming preaustinoid A4 into isoaustinone which is in
CC       turn hydroxylated by the P450 monooxygenase ausI to form austinolide
CC       (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG
CC       modifies austinolide to austinol (PubMed:22329759). Austinol can be
CC       further modified to dehydroaustinol which forms a diffusible complex
CC       with diorcinol that initiates conidiation (PubMed:22234162,
CC       PubMed:22329759). Due to genetic rearrangements of the clusters and the
CC       subsequent loss of some enzymes, the end products of the Emericella
CC       nidulans austinoid biosynthesis clusters are austinol and
CC       dehydroaustinol, even if additional enzymes, such as the O-
CC       acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are
CC       still functional (PubMed:29076725). {ECO:0000269|PubMed:22234162,
CC       ECO:0000269|PubMed:22329759, ECO:0000269|PubMed:23865690,
CC       ECO:0000269|PubMed:29076725}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|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}.
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DR   EMBL; BN001308; CBF87247.1; -; Genomic_DNA.
DR   EMBL; AACD01000172; EAA66317.1; -; Genomic_DNA.
DR   RefSeq; XP_682519.1; XM_677427.1.
DR   SMR; A0A1U8QLK0; -.
DR   EnsemblFungi; CBF87247; CBF87247; ANIA_09250.
DR   EnsemblFungi; EAA66317; EAA66317; AN9250.2.
DR   GeneID; 2867897; -.
DR   KEGG; ani:AN9250.2; -.
DR   VEuPathDB; FungiDB:AN9250; -.
DR   eggNOG; ENOG502RS2N; Eukaryota.
DR   HOGENOM; CLU_026450_1_1_1; -.
DR   OMA; ILPRMYF; -.
DR   OrthoDB; 1130893at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; 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   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..516
FT                   /note="O-acyltransferase ausQ"
FT                   /id="PRO_0000453867"
SQ   SEQUENCE   516 AA;  56838 MW;  8EA7601B7770E8E7 CRC64;
     MPPSPDFEAF SLTPIDQANG QVFFFYNISY RVRNEASALQ TIHNAIDVLL EKVPFLNGEI
     AFPAPVPDAN NVLIVRPPRA KSEDQVPLVQ VKRHSNCALP VKKLEQSPFN VPSSLPLNGL
     FNPLAAYPTP NRPTPVIRFQ INLVNDGLIL TLAFNHAVFD ALGAAVIVKL LAESCRNQDK
     IGMDGRLGIP STQARVRSPL LALSSRLKKN NRARVDAPSP SEFSENISHR PVAAPPPLKD
     ECFVFCAEKL QQLRIACTSI LEKLHENQKS VTGQGDVRFL SINDVLTALI CESIAQARHA
     AKHPYRDEKL HAKPSVSECL MAVDLRKFVE PPLPHDYMGN AAIPLRFEVS SQRHASPDFH
     RAVREVPTGL NTSFFLAIAK TAYTIRAKLA RFGESYIDSL SSFLNAHEEQ KAVNILPACA
     IVSSLRHIKT YELQFGAELG EIQAFETGIP WVNGSCIILP LCANSSDVAG SAPWNVRITL
     DESTMYCFKN EPALRWALLE QGKSKVLGPC DCKADV