ID   EPAC_ASPNC              Reviewed;         461 AA.
AC   A2QTE3;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=O-acetyltransferase epaC {ECO:0000303|PubMed:30384904};
DE            EC=2.3.1.- {ECO:0000305|PubMed:30384904};
DE   AltName: Full=Pestalamide A biosynthesis cluster protein C {ECO:0000303|PubMed:30384904};
GN   Name=epaC {ECO:0000303|PubMed:30384904}; ORFNames=An09g01800;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
RN   [2]
RP   IDENTIFICATION, FUNCTION, AND PATHWAY.
RX   PubMed=30384904; DOI=10.1016/j.micres.2018.10.004;
RA   Wang B., Li X., Yu D., Chen X., Tabudravu J., Deng H., Pan L.;
RT   "Deletion of the epigenetic regulator GcnE in Aspergillus niger FGSC A1279
RT   activates the production of multiple polyketide metabolites.";
RL   Microbiol. Res. 217:101-107(2018).
CC   -!- FUNCTION: O-acetyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of nigerpyrone and its derivatives carbonarone A and
CC       pestalamide A (PubMed:30384904). The biosynthesis pathway begins with
CC       the polyketide assembly by epaA to form phenylacetyl triketide
CC       precursor from successive condensation of two malonyl-CoA, presumably
CC       with one phenylacetyl-CoA starter unit produced by the phenylacetyl-CoA
CC       ligase epaB (PubMed:30384904). For the nigerpyrone biosynthesis, the
CC       reactive polyketide chain is released as an aldehyde through the R-
CC       domain. A nonenzymatic cyclization and dehydration may create
CC       nigerpyrone (PubMed:30384904). For the biosynthesis of carbonarone A
CC       and pestalamide A, an extra methyl group is added through the C-
CC       methyltransferase domain. Several further steps involving the
CC       dehydrogenase orf1, the cytochrome P450 monooxygenase orf2 and the FAD-
CC       dependent monooxygenase orf3 are required to form a carbonarone A
CC       precursor which is converted to carbonarone A via cyclization
CC       (PubMed:30384904). The O-acetyltransferase epaC could catalyze the
CC       transfer of 2-methylsuccinyl-CoA, a common intermediate in the
CC       ethylmalonyl-CoA pathway, to generate the final product pestalamide A
CC       (Probable). {ECO:0000269|PubMed:30384904, ECO:0000305|PubMed:30384904}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:30384904}.
CC   -!- SIMILARITY: Belongs to the trichothecene 3-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; AM270194; CAK40118.1; -; Genomic_DNA.
DR   RefSeq; XP_001393495.1; XM_001393458.1.
DR   AlphaFoldDB; A2QTE3; -.
DR   SMR; A2QTE3; -.
DR   PaxDb; A2QTE3; -.
DR   EnsemblFungi; CAK40118; CAK40118; An09g01800.
DR   GeneID; 4983711; -.
DR   KEGG; ang:ANI_1_1120084; -.
DR   VEuPathDB; FungiDB:An09g01800; -.
DR   HOGENOM; CLU_026450_5_0_1; -.
DR   Proteomes; UP000006706; Chromosome 1L.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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..461
FT                   /note="O-acetyltransferase epaC"
FT                   /id="PRO_0000446156"
SQ   SEQUENCE   461 AA;  52228 MW;  93486C846A9A9989 CRC64;
     MATNGFRPEY EDLGRYEDIL GQLPMLQVYS HIMLPFAMPE GLSRDTIIAD LEAAVRQIRA
     HVPWMAGKVV NVGKGPDNSG RYIVVPCPPP DPLIVVRDVT HAFPPYKEIQ RLKAPNSMLD
     SRLLAPTNAF PQRFEDSEED PFRVIRLQAS FVDGGVFLDF VTQHNMTDAG GLFGFARLVA
     MAMRGEQFSE SLLEQVNRDR RNIIPLLTPD EPMLDHSHHI RPPITDAQPV VRPDPARWHF
     LRFTAAKLAE LKDLASQTMT PDPEVPYITT DDAVSAFCWK KYITVRHRRR NTPDARSRFS
     RAMDGRKVLG IPAEYMGDLV HNVTTWLTFR ELVDLPLGEI ARHMRRELNR ANTAYHVRSF
     ATFIAQEPDK STIAYGGRFN PDTDVGSSSV LRVDLFPVFG KLGRPDFIRR PNFPGIPFPS
     LLYFFPQNPQ GDCDSLTCLT DADMEALNQD SEWTSMVEYI G