ID   PYVE_ASPV1              Reviewed;         452 AA.
AC   A0A2V5HCN7; A0A7M4B3W3;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=FAD-linked oxidoreductase pyvE {ECO:0000303|PubMed:33117309};
DE            EC=1.1.1.- {ECO:0000305|PubMed:33117309};
DE   AltName: Full=Pyranoviolin A biosynthesis cluster protein E {ECO:0000303|PubMed:33117309};
GN   Name=pyvE {ECO:0000303|PubMed:33117309}; ORFNames=BO99DRAFT_407312;
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-linked oxidoreductase; 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:Q5BEJ5};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:33117309}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; BR001648; FAA01295.1; -; Genomic_DNA.
DR   EMBL; KZ825234; PYI13690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5HCN7; -.
DR   SMR; A0A2V5HCN7; -.
DR   Proteomes; UP000249829; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..452
FT                   /note="FAD-linked oxidoreductase pyvE"
FT                   /id="PRO_0000452820"
FT   DOMAIN          34..204
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   452 AA;  48871 MW;  DC5CA26131F8D816 CRC64;
     MDDLRQHLRG TTALVLTPDS PGYAESIKRW SDTCEKKAAA VVLPTTAEEV SLAVGFATAH
     HIPLVVHNGG HSTSGASASE GGLVISLARM RGVVVDPAAK TITAQGGTIW EDVDRAAAVH
     GLATVGGTVN HTGVGGLTLG GGYGWLTGRH GLTIDNLLAA TVVLADGRIL RASETANADL
     FWALRGAGHN FGVVTEFVFR AYDQPNEVYA GLLSYPTHRL PEILAFVNTF EDEGPAQQDQ
     GIFFGFSGDS ILAAIFYNGP RAAAERHFAP LLALQPTVNT VTMIPYEQLN TIQNPFATYG
     GRKSFSGAFV RLPLEVGFFQ ELLDDYQAMI QTYPEASRTA VLFELVSHTA VLRVPQAAMA
     YATRGPFYNV GCVFRWENPG LDQTMRAMQQ AMMRKVGDRA GAGAHARAYA NYSHHDGRVK
     DVFGENLPRL QQLKGKYDPN NVFKKWLNLL PN