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PIG13_CLAP2
ID   PIG13_CLAP2             Reviewed;         174 AA.
AC   M1VWN5;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Anthrone oxygenase CPUR_05435 {ECO:0000303|PubMed:28955461};
DE            EC=1.10.3.- {ECO:0000305|PubMed:28955461};
DE   AltName: Full=Ergochrome gene cluster protein CPUR_05435 {ECO:0000303|PubMed:28955461};
GN   ORFNames=CPUR_05435;
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: Anthrone oxygenase; part of the ergochrome gene cluster
CC       responsible for the typical purple-black color of the ergot sclerotia
CC       (PubMed:28955461). The ergochrome gene cluster produces several ergot
CC       pigments including the yellow ergochrome secalonic acid and its
CC       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 decarboxylase CPUR_05434 then
CC       catalyzes the concerted decarboxylation-elimination required to convert
CC       atochrysone carboxylic acid into emodin anthrone, which is further
CC       oxidized to emodin by the anthrone oxygenase CPUR_05435 (By
CC       similarity). Emodin is further modified to yield monodictyphenone via
CC       several steps involving CPUR_05427, CPUR_05428, CPUR_05429 and
CC       CPUR_05430 (By similarity). The short chain dehydrogenase/reductase
CC       CPUR_05418 then catalyzes the C-5 ketoreduction to give the xanthone
CC       skeleton of the monomeric units (PubMed:32105084). Ergochromes
CC       formation requires further dimerization steps of different xanthone
CC       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:A4DA85,
CC       ECO:0000250|UniProtKB:Q5BH30, ECO:0000269|PubMed:28955461,
CC       ECO:0000269|PubMed:32105084}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=emodin anthrone + O2 = emodin + H(+) + H2O;
CC         Xref=Rhea:RHEA:64268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:77659, ChEBI:CHEBI:150013;
CC         Evidence={ECO:0000305|PubMed:28955461};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64269;
CC         Evidence={ECO:0000305|PubMed:28955461};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
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 anthrone oxygenase family. {ECO:0000305}.
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DR   EMBL; CAGA01000032; CCE31582.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1VWN5; -.
DR   EnsemblFungi; CCE31582; CCE31582; CPUR_05435.
DR   VEuPathDB; FungiDB:CPUR_05435; -.
DR   eggNOG; ENOG502R15X; Eukaryota.
DR   HOGENOM; CLU_105974_0_0_1; -.
DR   OrthoDB; 1517224at2759; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..174
FT                   /note="Anthrone oxygenase CPUR_05435"
FT                   /id="PRO_0000443984"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   174 AA;  18156 MW;  42CB033AE736E621 CRC64;
     MLRGFAPTGV HVVALASGVF LSGAMFSVSA IMIPTLLDTN KEPAGLTTQW ARLYHYGSVL
     MPSMSVAIAA VYGFASTQYR QSPQGMRCLA AGALTLAIAP YTWLAMIPTN NALFAMAASA
     PGFAGMQDAN EKARDLVMKW VVLHSIRSIL PLAGAIMGFT GISSGQEGVV GSAN
 
 
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