ID   AURC_CALAK              Reviewed;         484 AA.
AC   A0A0M3STX4;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=FAD-dependent monooxygenase aurC {ECO:0000303|PubMed:26340065};
DE            EC=1.-.-.- {ECO:0000269|PubMed:26340065};
DE   AltName: Full=Aurovertin biosynthesis cluster protein C {ECO:0000303|PubMed:26340065};
DE   Flags: Precursor;
GN   Name=aurC {ECO:0000303|PubMed:26340065};
OS   Calcarisporium arbuscula (Dendryphion arbuscula).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Calcarisporium.
OX   NCBI_TaxID=240499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=26340065; DOI=10.1021/jacs.5b07816;
RA   Mao X.M., Zhan Z.J., Grayson M.N., Tang M.C., Xu W., Li Y.Q., Yin W.B.,
RA   Lin H.C., Chooi Y.H., Houk K.N., Tang Y.;
RT   "Efficient biosynthesis of fungal polyketides containing the dioxabicyclo-
RT   octane ring system.";
RL   J. Am. Chem. Soc. 137:11904-11907(2015).
CC   -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of aurovertins, fungal polyketides that
CC       exhibit potent inhibition of adenosine triphosphate synthase
CC       (PubMed:26340065). Tha biosynthesis starts with the HR-PKS aurA that
CC       selects propionate as the starter unit; synthesizes a hexa-ene chain
CC       through the repeated functions of the KR and DH domains in the first
CC       six iterations; selectively introduces three alpha-methyl substitutions
CC       at C4, C6, and C16 using the S-adensylmethionine-dependent cMET; and
CC       shuts off KR and DH in the last three iterations to afford a 1,3,5-
CC       triketo portion that can undergo intramolecular cyclization to yield
CC       the alpha-pyrone intermediate (PubMed:26340065). AurE may act as a
CC       cyclase and enhances the rate of pyrone formation and product release
CC       of aurA (PubMed:26340065). The methyltransferase aurB then methylates
CC       the C17 hydroxyl group (PubMed:26340065). C17 methylation is required
CC       to initiate epoxidation by the downstream monooxygenase aurC
CC       (PubMed:26340065). The monooxygenase aurC and the epoxide hydrolase
CC       aurD can iteratively transform the terminal triene portion of the
CC       methylated precursor into the dioxabicyclo[3.2.1]octane scaffold of
CC       aurovertin E. Epoxidation modifications of the precursor occur in two
CC       separate steps; bis-epoxidation of the two terminal olefins takes place
CC       first, followed by another epoxidation that occurs at C7-C8 after
CC       tetrahydrofuran formation (PubMed:26340065). The O-acyltransferase aurG
CC       converts aurovertin E to aurovertin A (PubMed:26340065).
CC       {ECO:0000269|PubMed:26340065}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:26340065}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; KT581576; ALD83629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M3STX4; -.
DR   SMR; A0A0M3STX4; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Membrane; Monooxygenase; Oxidoreductase; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..484
FT                   /note="FAD-dependent monooxygenase aurC"
FT                   /id="PRO_0000443967"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         36..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         131
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
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   484 AA;  54178 MW;  25585AB122C006F5 CRC64;
     MGAYSFRVII VGGSITGMTL AHCLDRAGID YVILEKHKDI FAEPGISIGL MPNGSRILEQ
     LGIYSDVHAL FEGIKKIYQY MPDGYCIETD SPVNIVDRFG LPFCVIDRYQ FLKVLYSKFE
     DKSRFHMNKK VTSICHGKSD VSVTTADGET YHGDLVVGAD GVHSVVRSEM WRIGNLARPG
     FVTEREKSEL AAEFACVFGV AKAVPGQGRW EHILRYNEDF CFMFFPASGT DVFFNVIYKL
     NQKYVYPDIP RFTKEEGIEV CESVGDFPVW EDVKFRDIWA QRIAFTCVPL EEHMFKNWHH
     RRIICVGDSV SKMSPNMGQG GNTAIESAAA LTNGLRKLVT SNYPDKPSER QLSNTLETFN
     RNQFKRLNTV HGDARYVTRL EALDGTLKRV FARYVMGHCG DLLVGNLARI VAGGGVLDFI
     PLTARSGKDW PPCPWQHSWG ISESIDFCKK FAVASLIVLI VVLARALDSP AGLSSGIRSS
     SWSF