ID   PYVB_ASPV1              Reviewed;         487 AA.
AC   A0A2V5GZ95; A0A7M4B2W8;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Cytochrome P450 monooxygenase pyvB {ECO:0000303|PubMed:33117309};
DE            EC=1.14.14.- {ECO:0000305|PubMed:33117309};
DE   AltName: Full=Pyranoviolin A biosynthesis cluster protein B {ECO:0000303|PubMed:33117309};
GN   Name=pyvB {ECO:0000303|PubMed:33117309}; ORFNames=BO99DRAFT_407314;
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: Cytochrome P450 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=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:33117309}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; BR001648; FAA01292.1; -; Genomic_DNA.
DR   EMBL; KZ825234; PYI13693.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5GZ95; -.
DR   SMR; A0A2V5GZ95; -.
DR   Proteomes; UP000249829; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..487
FT                   /note="Cytochrome P450 monooxygenase pyvB"
FT                   /id="PRO_0000452817"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         426
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
SQ   SEQUENCE   487 AA;  55126 MW;  29A0B5528F2ABDB6 CRC64;
     MIASHLLSPL IFLEQQPAYS SVVIGALVVC LVCLVWPTES AKRAPPAPNF GVPRIGDAAA
     FLADPVSFVQ KATQKCGSIF QIKLLVANLV YLRGVKLNRM YTDVKEDTWS FGGGIGLFLR
     KIAKPGYFDH LRTLVNSLNR GVNRKAALEH YFQLIEEEAG KALQGWSQRG AVPVFEETSR
     FVHRVIVRCL MGQDFYDHRL DELYEILHHM EADIGHPFNL LLPDWIPHPA ARRLEQNRDR
     FAQIFEQQVA DRRRNPEIWR DSLDYISFTL EDPRTAHLEG YLPSHHTVLM FAAHTSTVAS
     ISWTILELLR NPDYLAQLRQ SLAAHPDARK CPELLAGIKE TGRHYSGVHM FRTTHRAVEL
     EGGKYLVPPN WIVSISPYLT HHDPEIFHTP QHWIPERWLQ PDDRMQNLNN PREAAFLQFG
     AGCHRCPGEA LAGIIAQGLL ATLVRRYDMV WGKEGPPTDL TALDFSKVGS PWLEGDASIA
     IRPKVAE