ID   PTMV_PENSI              Reviewed;         494 AA.
AC   A0A140JWS4;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=O-acetyltransferase ptmV {ECO:0000303|PubMed:25831977};
DE            EC=2.3.1.- {ECO:0000269|PubMed:25831977};
DE   AltName: Full=Penitrem biosynthesis cluster 1 protein V {ECO:0000303|PubMed:25831977};
GN   Name=ptmV {ECO:0000303|PubMed:25831977};
OS   Penicillium simplicissimum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC   STRAIN=AK-40;
RX   PubMed=25831977; DOI=10.1002/anie.201501072;
RA   Liu C., Tagami K., Minami A., Matsumoto T., Frisvad J.C., Suzuki H.,
RA   Ishikawa J., Gomi K., Oikawa H.;
RT   "Reconstitution of biosynthetic machinery for the synthesis of the highly
RT   elaborated indole diterpene penitrem.";
RL   Angew. Chem. Int. Ed. 54:5748-5752(2015).
CC   -!- FUNCTION: O-acetyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of the indole diterpenes penitrems (PubMed:25831977).
CC       The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first
CC       step in penitrem biosynthesis via conversion of farnesyl pyrophosphate
CC       and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP)
CC       (PubMed:25831977). Condensation of indole-3-glycerol phosphate with
CC       GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole
CC       (3-GGI) (PubMed:25831977). Epoxidation by the FAD-dependent
CC       monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the
CC       terpene cyclase ptmB for cyclization to yield paspaline
CC       (PubMed:25831977). Paspaline is subsequently converted to 13-
CC       desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter
CC       being then converted to paxilline by the cytochrome P450 monooxygenase
CC       ptmQ (PubMed:25831977). Paxilline is converted to beta-paxitriol via C-
CC       10 ketoreduction by the short-chain dehydrogenase ptmH which can be
CC       monoprenylated at the C-20 by the indole diterpene prenyltransferase
CC       ptmD (PubMed:25831977). A two-step elimination (acetylation and
CC       elimination) process performed by the O-acetyltransferase ptmV and ptmI
CC       leads to the production of the prenylated form of penijanthine
CC       (PubMed:25831977). 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 ptmE
CC       (PubMed:25831977). Five sequential oxidative transformations performed
CC       by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ
CC       yield the various penitrem compounds. PtmK, ptmU and ptmM are involved
CC       in the formation of the key bicyclic ring of penitrem C via the
CC       formation of the intermediates secopenitrem D and penitrem D. PtmL
CC       catalyzes the epoxidation of penitrem D and C to yield penitrem B and
CC       F, respectively. PtmJ catalyzes the last benzylic hydroxylation to
CC       convert penitrem B to prenitrem E and penitrem F to penitrem A
CC       (PubMed:25831977). {ECO:0000269|PubMed:25831977}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:25831977}.
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; LC027936; BAU61551.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A140JWS4; -.
DR   SMR; A0A140JWS4; -.
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 ptmV"
FT                   /id="PRO_0000446595"
FT   REGION          181..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  54945 MW;  C22E79229B44547A CRC64;
     MSKPLFEAYP LTGLDHTIPP CYVRFLLTFP VPDVALAVNQ LQKGAENLIE KLPFLAGYLA
     SCETPGVRPG QLEIRPPAGE RRPVCLVAHH SNSYLADSSA TSTTEQLGTA NENYLPVPFF
     PELDKPVPIF RVKVNAMTDG IILGFAFHHS VIDATGMGTI VRDFARCCRG PDGGPLEISL
     ESQQDSREKL RHSGGPPDPR FDHNGEYPLV ASLPADLEAM KQVLIQTARL MSTQYFRIPA
     SLVNTLKESC NRMLRESPAL RDEGENPWIS SNDLVVSLLW LCLNRVRYPE DNTNVIPPSD
     SSVCMAVNIR GRLQSPIDPG YVGNAIVLLR ESVGMNAFLH KPGDDDPLGA QCYETAKRLG
     REAWEAALVR IALAIRRKLN TINASYVRSV ISYLEDVPDL STVAFGQTDY HISSWRDIGV
     YEADFGGHMG HPSEMRVPDG MVDGMFYILP RRQGTHPCWE IHVTIHQDTM KRLIADPVWA
     RYTVRKPSSL CRDE