ID   AUSP_ASPCI              Reviewed;         480 AA.
AC   A0A0U5GIM7;
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 ausP {ECO:0000303|PubMed:28233494};
DE            EC=2.3.1.- {ECO:0000269|PubMed:28233494};
DE   AltName: Full=Austinoid biosynthesis cluster protein P {ECO:0000303|PubMed:28233494};
GN   Name=ausP {ECO:0000303|PubMed:28233494}; ORFNames=ASPCAL14358;
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, DISRUPTION PHENOTYPE, 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:Q5ATJ7, 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:Q70PR7}.
CC   -!- DISRUPTION PHENOTYPE: Leads to complete loss of production of austin.
CC       {ECO:0000269|PubMed:28233494}.
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 plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; CDMC01000024; CEL11255.1; -; Genomic_DNA.
DR   SMR; A0A0U5GIM7; -.
DR   EnsemblFungi; CEL11255; CEL11255; ASPCAL14358.
DR   OrthoDB; 643224at2759; -.
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..480
FT                   /note="O-acyltransferase ausP"
FT                   /id="PRO_0000453865"
FT   ACT_SITE        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT   ACT_SITE        412
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q70PR7"
SQ   SEQUENCE   480 AA;  54572 MW;  D1839669E5EF580A CRC64;
     MEVVRYFTSN QKQPPATGPK DSIVQLPDIP PVYECNVEVA LRFDSVLDPE KLQQSLKRLL
     EIGNWRQLGG RLRRRDTNSD ACGYDLHVPV EFTTERPAFI YKTLESPAAV DEHPVACKMP
     QPTDPNKILF YNVRDALTPS MTRTHHPRKA QEWAESDLPP LSFEQLNFRD GTIILLLFPH
     ILMDATGYGL FLKAWTCVLQ GRMDDVPQCC GFSESITDML CHKTPAESFT WHNHLLKGLD
     RLRFTARLLW ENICGKEERI IRVPGKFITQ TRDKTLADLS TSQDSPFVSH SDVLVAWFVR
     VVLASLNPQH QRTLVLTNAF DIRHMLPPER AYLQNSVFLA HTMLPVGEVV SNPASFLANE
     IRRSLVRERT EEQVQARCAW AKDVGIMPLL GSSDMLLCNV SNWSKGGLLD LDFGPAAITQ
     RPGPCVPSSI LNCSQMRGVT PEYGIILGKD SQDGWWMQWR LSKFCWAMIE RELDTINQTR