ID   PIG1_CLAP2              Reviewed;         514 AA.
AC   M1W850;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=FAD-dependent monooxygenase CPUR_05423 {ECO:0000303|PubMed:28955461};
DE            EC=1.-.-.- {ECO:0000305|PubMed:28955461};
DE   AltName: Full=Ergochrome gene cluster protein CPUR_05423 {ECO:0000303|PubMed:28955461};
GN   ORFNames=CPUR_05423;
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1;
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=28955461; DOI=10.1186/s40694-016-0020-z;
RA   Neubauer L., Dopstadt J., Humpf H.U., Tudzynski P.;
RT   "Identification and characterization of the ergochrome gene cluster in the
RT   plant pathogenic fungus Claviceps purpurea.";
RL   Fungal Biol. Biotechnol. 3:2-2(2016).
RN   [3]
RP   FUNCTION.
RX   PubMed=32105084; DOI=10.1021/acs.orglett.0c00285;
RA   Wei X., Matsuda Y.;
RT   "Unraveling the fungal strategy for tetrahydroxanthone biosynthesis and
RT   diversification.";
RL   Org. Lett. 22:1919-1923(2020).
CC   -!- FUNCTION: FAD-dependent monooxygenase; part of the ergochrome gene
CC       cluster responsible for the typical purple-black color of the ergot
CC       sclerotia (PubMed:28955461). The ergochrome gene cluster produces
CC       several ergot pigments including the yellow ergochrome secalonic acid
CC       and its derivatives, as well as the red anthraquinones endocrocin and
CC       clavorubin (PubMed:28955461). The pathway begins with the synthesis of
CC       atrochrysone thioester by the polyketide synthase (PKS) CPUR_05437 (By
CC       similarity). The atrochrysone carboxyl ACP thioesterase CPUR_05436 then
CC       breaks the thioester bond and releases the atrochrysone carboxylic acid
CC       from CPUR_05437 (By similarity). The atrochrysone carboxylic acid is
CC       then converted to atrochrysone which is further transformed into emodin
CC       anthrone (By similarity). The next step is performed by the anthrone
CC       oxygenase CPUR_05434 that catalyzes the oxidation of emodinanthrone to
CC       emodin (By similarity). Emodin is further modified to yield
CC       monodictyphenone via several steps involving CPUR_05427, CPUR_05428,
CC       CPUR_05429 and CPUR_05430 (By similarity). The short chain
CC       dehydrogenase/reductase CPUR_05418 then catalyzes the C-5 ketoreduction
CC       to give the xanthone skeleton of the monomeric units (PubMed:32105084).
CC       Ergochromes formation requires further dimerization steps of different
CC       xanthone units, probably catalyzed by the cytochrome P450 monooxygenase
CC       CPUR_05419 (PubMed:28955461). CPUR_05425, CPUR_05426 and CPUR_05431 are
CC       unique to Claviceps, thus it is likely that they are involved in
CC       further modification of xanthone units or in their dimerization
CC       (PubMed:28955461). The yellow ergochromes and the red anthraquinone
CC       pigments endocrocin and clavorubin are products from the same PKS
CC       derived precursors and the latter are likely shunt products in the
CC       pathway of xanthone biosynthesis (PubMed:28955461). It is proposed that
CC       atrochrysone carboxylic acid released from the PKS CPUR_05437 can also
CC       be converted to endocrocin anthrone which is further oxidized into
CC       endocrocin by CPUR_05435 (By similarity). Endocrocin could be then
CC       modified to clavorubin, possibly by CPUR_05423 and CPUR_05431
CC       (PubMed:28955461). Clavorubin is the principal anthraquinone metabolite
CC       produced by the cluster with a much higher yield compared to endocrocin
CC       (PubMed:28955461). {ECO:0000250|UniProtKB:Q4W944,
CC       ECO:0000250|UniProtKB:Q5BH33, ECO:0000269|PubMed:28955461,
CC       ECO:0000269|PubMed:32105084}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Pigment biosynthesis. {ECO:0000305|PubMed:28955461}.
CC   -!- INDUCTION: Expression correlates with the formation of the sclerotia
CC       and thus the pigment production and is directly regulated by the
CC       cluster-specific activator CPUR_05433 (PubMed:28955461).
CC       {ECO:0000269|PubMed:28955461}.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; CAGA01000032; CCE31570.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1W850; -.
DR   SMR; M1W850; -.
DR   STRING; 5111.M1W850; -.
DR   EnsemblFungi; CCE31570; CCE31570; CPUR_05423.
DR   VEuPathDB; FungiDB:CPUR_05423; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_009665_19_1_1; -.
DR   OrthoDB; 462247at2759; -.
DR   PhylomeDB; M1W850; -.
DR   Proteomes; UP000016801; 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   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..514
FT                   /note="FAD-dependent monooxygenase CPUR_05423"
FT                   /id="PRO_0000443972"
FT   BINDING         66..67
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         358
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         368..372
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
SQ   SEQUENCE   514 AA;  57641 MW;  1B970DFF2A7D640E CRC64;
     MVDKFLIETD QNEFQPNLWK NGDSDRLPNR CPETQLNVLV VGAGPSGLMT ALECWRKGHN
     VVKILERSNS PVFTGDVIVI GPSALRAFRH WPDMCAELEK SKMDSIMYYR KHNGELILGP
     TSLGHNDPEY TAAWKGIPFA APHQIRKDFY RMLLRQVARV GIRVEYGQRV EKYFDDEAAM
     LGGVITDQGT IMFADLVVAA DANRTRSDLL IAGAHTPSRS SGMSVYRTAF PTERALQDEA
     FRTRWGDAIE KGISHHEFWM GPGMHLGLFI SPEFVAFGLT PRDSFLHEGG NEPIESWEPD
     VDPEEVTKVL NRVPDWNPVI KSLVKNTQRG SIVHWPLLWR NLRREWTSKS GRVVQAGDAA
     HSSIPASISG GTLALEDAVT LASCLHLSCS SAGSKGAPLG ARIYNLLRYQ RVSCVQKMSF
     VNAEGLSGSS MEDAIKENPE SVRVRFPRWL YRHDPEAYVY EKYGQAFAHL VEGTDFENTN
     LPPGHTFEPW TIEQIHKDMM AGKRVADFLD GDWS