ID   PC16_PENCR              Reviewed;         494 AA.
AC   A0A0E3D8P9;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=O-acetyltransferase PC-16 {ECO:0000303|PubMed:26213965};
DE            EC=2.3.1.- {ECO:0000305|PubMed:26213965};
DE   AltName: Full=Penitrem biosynthesis cluster protein PC-16 {ECO:0000303|PubMed:26213965};
GN   Name=PC-16 {ECO:0000303|PubMed:26213965};
OS   Penicillium crustosum (Blue mold fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC   STRAIN=PN2402;
RX   PubMed=26213965; DOI=10.3390/toxins7082701;
RA   Nicholson M.J., Eaton C.J., Starkel C., Tapper B.A., Cox M.P., Scott B.;
RT   "Molecular cloning and functional analysis of gene clusters for the
RT   biosynthesis of indole-diterpenes in Penicillium crustosum and P.
RT   janthinellum.";
RL   Toxins 7:2701-2722(2015).
CC   -!- FUNCTION: O-acetyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of the indole diterpenes penitrems (PubMed:26213965).
CC       The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first
CC       step in penitrem biosynthesis via conversion of farnesyl pyrophosphate
CC       and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP)
CC       (Probable). Condensation of indole-3-glycerol phosphate with GGPP by
CC       the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI)
CC       (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads
CC       to a epoxidized-GGI that is substrate of the terpene cyclase penB for
CC       cyclization to yield paspaline (Probable). Paspaline is subsequently
CC       converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase
CC       penP, the latter being then converted to paxilline by the cytochrome
CC       P450 monooxygenase penQ (PubMed:26213965). Paxilline is converted to
CC       beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase
CC       PC-15 which can be monoprenylated at the C-20 by the indole diterpene
CC       prenyltransferase penD (Probable). A two-step elimination (acetylation
CC       and elimination) process performed by the O-acetyltransferase PC-16 and
CC       the P.simplicissimum ptmI-ortholog not yet identified in P.crustosum,
CC       leads to the production of the prenylated form of penijanthine
CC       (Probable). The FAD-linked oxidoreductase ptmO then converts the
CC       prenylated form of penijanthine into PC-M5 which is in turn transformed
CC       into PC-M4 by the aromatic dimethylallyltransferase PC-22 (Probable). A
CC       series of oxidation steps involving 4 cytochrome P450 monooxygenases
CC       (PC-21, PC-05, PC-23, PC-20) and a FAD-dependent monooxygenase (PC-14)
CC       are required for the transformation of PC-M4 to penitrems A and E.
CC       Synthesis of these final products is proposed to proceed via penitrems
CC       D and C (PC-21, PC-05, PC-14) and penitrems B and F (PC-21, PC-05, PC-
CC       14, PC-23) (Probable). {ECO:0000269|PubMed:26213965,
CC       ECO:0000305|PubMed:26213965}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:26213965}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q4WZ64}.
CC   -!- SIMILARITY: Belongs to the fumigaclavine B O-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KC963408; AGZ20197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3D8P9; -.
DR   SMR; A0A0E3D8P9; -.
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; Transferase.
FT   CHAIN           1..494
FT                   /note="O-acetyltransferase PC-16"
FT                   /id="PRO_0000446596"
SQ   SEQUENCE   494 AA;  54647 MW;  81B9B983346579B2 CRC64;
     MSKPLFEAYP LTGLDHTIPP CYVRFFLTFP VPDVALAVNQ PQKGADNFIE KLPFLAGYLA
     PCETPGVRPG QLEIRPPAEE GIPVCLVAHH SNSCLADSSA TSTTEQLGTA NENYLPVPFF
     PELDKPVPIF RVKVNAMTDG IILGFAFHHS VIDATGIGTI VRDFARCCRG PDGGPLEISL
     ESQNDSREKL RHCGGPPDPR FDHNKEYPLV ASLPADLEGM KQVLIQTARL MSTQYFRIPA
     SLVNALKETC NHMLRESPAL KDEGENPWIS SNDLVVSLLW LCLNRVRYPA ENNNVIPPSD
     SSVCMAVNIR GRMKSPINPG YVGNAIVLLR ESVGMSAFLH KLGDGDPLGA QCYETAKRLG
     RETWEAALVR IALAIRRKLN TINDSYVRSV ISYLEGVPDL STVAFGQTDY HISSWRDIGV
     YEADFGGHMG HPSDMRVPDG MVDGMFYILP RRQGTHPCWE IHVTIHQDTM KRLIADPVWA
     RYTAGKTPSL CRDE