ID   AUSQ_ASPCI              Reviewed;         502 AA.
AC   A0A0U5GJY1;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=O-acyltransferase ausQ {ECO:0000303|PubMed:28233494};
DE            EC=2.3.1.- {ECO:0000269|PubMed:28233494};
DE   AltName: Full=Austinoid biosynthesis cluster protein Q {ECO:0000303|PubMed:28233494};
GN   Name=ausQ {ECO:0000303|PubMed:28233494}; ORFNames=ASPCAL14359;
OS   Aspergillus calidoustus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=454130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF006504;
RX   PubMed=26966204; DOI=10.1128/genomea.00102-16;
RA   Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Scherlach K.,
RA   Martin K., Brakhage A.A., Petzke L., Valiante V.;
RT   "Draft genome sequences of fungus Aspergillus calidoustus.";
RL   Genome Announc. 4:0-0(2016).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=28233494; DOI=10.1021/acschembio.7b00003;
RA   Valiante V., Mattern D.J., Schueffler A., Horn F., Walther G.,
RA   Scherlach K., Petzke L., Dickhaut J., Guthke R., Hertweck C., Nett M.,
RA   Thines E., Brakhage A.A.;
RT   "Discovery of an Extended Austinoid Biosynthetic Pathway in Aspergillus
RT   calidoustus.";
RL   ACS Chem. Biol. 12:1227-1234(2017).
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 that mediates the
CC       biosynthesis of calidodehydroaustin, a fungal meroterpenoid
CC       (PubMed:28233494, PubMed:29076725). The first step of the pathway is
CC       the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase
CC       ausA (PubMed:28233494). 3,5-dimethylorsellinic acid is then prenylated
CC       by the polyprenyl transferase ausN (PubMed:28233494). 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 (By similarity). Protoaustinoid A is then oxidized to
CC       spiro-lactone 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 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:28233494). The cytochrome P450 monooxygenase ausR then converts
CC       dehydroaustin is into 7-dehydrodehydroaustin (PubMed:28233494). The
CC       hydroxylation catalyzed by ausR permits the O-acetyltransferase ausQ to
CC       add an additional acetyl group to the molecule, leading to the
CC       formation of acetoxydehydroaustin (PubMed:28233494). The short chain
CC       dehydrogenase ausT catalyzes the reduction of the double bond present
CC       between carbon atoms 1 and 2 to convert 7-dehydrodehydroaustin into
CC       1,2-dihydro-7-hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes
CC       not only an acetylation reaction but also the addition of the PKS ausV
CC       diketide product to 1,2-dihydro-7-hydroxydehydroaustin, forming
CC       precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha-
CC       ketoglutarate-dependent dioxygenase converts precalidodehydroaustin
CC       into calidodehydroaustin (PubMed:28233494).
CC       {ECO:0000250|UniProtKB:A0A1U8QLK0, ECO:0000269|PubMed:28233494,
CC       ECO:0000269|PubMed:29076725}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:28233494}.
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; CDMC01000024; CEL11256.1; -; Genomic_DNA.
DR   SMR; A0A0U5GJY1; -.
DR   EnsemblFungi; CEL11256; CEL11256; ASPCAL14359.
DR   OrthoDB; 1130893at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000054771; 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..502
FT                   /note="O-acyltransferase ausQ"
FT                   /id="PRO_0000453868"
SQ   SEQUENCE   502 AA;  55185 MW;  A36697BA3C258ED6 CRC64;
     MPSSSDFEAF TLTPLDQANG QVFFFYSLSY RVQDEASALH TIHKAIDLLL EKAPFLNGEI
     VFATDGLEVR PPTTDSEDRV PLVQVKRHSN RTLPVEKLGQ SPFNVPRNFP LDALFNPLAA
     LPTPDRPTPV IRFQVNLVND GLVLTIGFNH AVFDALGAAV IVKLLAESCR NPANVGREGS
     LEIASTQSRV RSPLLALTSR WKKLDRVRAD APSSPEVTAV PPPLTDECFV FCADKLQRLR
     AACNSILCQL NENQKLLAGQ PDVRFLSTND VLTALICETI AQARHAARHT CRDEGLHPES
     TVSECLMAVN IRKFVDPPLP DDYMGNAGIP LRFQIETRRD AEPDLPRAFQ EANPGLNTSS
     FLAIAETAYT IRIKLASFGD SYIDSLRSFL NADESQTAVH VLPACAIVSS LRHIKTYELQ
     FGAELGEIRT FETGIPWVNG SCVILPLCAN SSEVAGSAPW NVRITLDEGT MYCFKNEPAL
     RWALWEQGRS KVPGSCDCKA DA