ID   PYVC_ASPV1              Reviewed;         427 AA.
AC   A0A2V5GWU4; A0A7M4B3C4;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=FAD-dependent monooxygenase pyvC {ECO:0000303|PubMed:33117309};
DE            EC=1.-.-.- {ECO:0000305|PubMed:33117309};
DE   AltName: Full=Pyranoviolin A biosynthesis cluster protein A {ECO:0000303|PubMed:33117309};
GN   Name=pyvC {ECO:0000303|PubMed:33117309}; ORFNames=BO99DRAFT_396260;
OS   Aspergillus violaceofuscus (strain CBS 115571).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=33117309; DOI=10.3389/fmicb.2020.562063;
RA   Wei X., Chen L., Tang J.W., Matsuda Y.;
RT   "Discovery of pyranoviolin A and its biosynthetic gene cluster in
RT   Aspergillus violaceofuscus.";
RL   Front. Microbiol. 11:562063-562063(2020).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115571;
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of pyranoviolin A, a pyranonigrin analog with
CC       a C-3 methoxy group (PubMed:33117309). Initially, the PKS portion of
CC       pyvA synthesizes C-10 carbon chain from 5 molecules of malonyl-CoA,
CC       which is then condensed with the thiolation (T) domain-bound glycine
CC       activated by the adenylation (A) domain (PubMed:33117309). The
CC       subsequent chain release by Dieckmann condensation (DKC) could be
CC       catalyzed by the TE domain present at the C-terminus of pyvA and/or the
CC       alpha/beta hydrolase pyvD, installing the tetramic acid moiety
CC       (Probable). The FAD-dependent monooxygenase pyvC next epoxidizes one of
CC       the olefins of the polyketide part, and the epoxide ring-opening
CC       induces the dihydro-gamma-pyrone ring formation (Probable). The
CC       cytochrome P450 monooxygeanse pyvB would be responsible for the 2
CC       consecutive reactions, in which the dihydro-gamma-pyrone is oxidized to
CC       gamma-pyrone and C-7 is hydroxylated to yield pyranonigrin F
CC       (Probable). Finally, the O-methyltransferase pyvH methylates the C-3
CC       hydroxy group to complete the biosynthesis (Probable).
CC       {ECO:0000269|PubMed:33117309, ECO:0000305|PubMed:33117309}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:A6T923};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:33117309}.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; BR001648; FAA01293.1; -; Genomic_DNA.
DR   EMBL; KZ825234; PYI13692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5GWU4; -.
DR   SMR; A0A2V5GWU4; -.
DR   STRING; 1450538.A0A2V5GWU4; -.
DR   Proteomes; UP000249829; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..427
FT                   /note="FAD-dependent monooxygenase pyvC"
FT                   /id="PRO_0000452818"
FT   BINDING         20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         39..40
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         132
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         233..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         308
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         318..322
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
SQ   SEQUENCE   427 AA;  47331 MW;  4E386311BC4E6082 CRC64;
     MEQASATTTV DVLIVGGGIG GLTLAGICKK LGITYKVLER SAEITPVGAG ISLAPNCLRI
     LEQLGHLDFI RRKGQPLRKI QIFRNSTPWS LVDYDWVQEK FGYSVYSIER HSMHQVLYQG
     AGPEHVLLDA EVVDIEDVPT APSVQVRLAD GRQLAGQLVV GADGIRSATR RILAATQGLE
     GANTIRFTGR THMTGYTHPL QHLGPADLGV ATWVFYDDSI LTSWPCIDNR QWFVGVKSSE
     LKNPTRSSWK NATQAIINDV YGDRFHPFGE HHRVRDVVNL AERVTASDVF EETTFPAMAC
     GRVALVGDSA HSMTSFIGQG ACQAIEDAGE LANALHAYFA SQSPSPQMLR ERLEEYRHRR
     EARARYVFSF SSLFAQLHTG RLWSPMGPLL RWVAFVCAPM WCWHRALTPL YGYQPVVHAL
     VDAPHAN