ID   MDPL_EMENI              Reviewed;         446 AA.
AC   C8VQ61; Q5BH28;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Baeyer-Villiger oxidase mdpL {ECO:0000303|PubMed:22730213};
DE            EC=1.-.-.- {ECO:0000305|PubMed:22730213};
DE   AltName: Full=Monodictyphenone synthesis protein L {ECO:0000303|PubMed:20139316};
GN   Name=mdpL {ECO:0000303|PubMed:20139316};
GN   Synonyms=tynL {ECO:0000303|PubMed:20139316}; ORFNames=ANIA_10023;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=20139316; DOI=10.1128/aem.02187-09;
RA   Chiang Y.M., Szewczyk E., Davidson A.D., Entwistle R., Keller N.P.,
RA   Wang C.C., Oakley B.R.;
RT   "Characterization of the Aspergillus nidulans monodictyphenone gene
RT   cluster.";
RL   Appl. Environ. Microbiol. 76:2067-2074(2010).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=21351751; DOI=10.1021/ja1096682;
RA   Sanchez J.F., Entwistle R., Hung J.H., Yaegashi J., Jain S., Chiang Y.M.,
RA   Wang C.C., Oakley B.R.;
RT   "Genome-based deletion analysis reveals the prenyl xanthone biosynthesis
RT   pathway in Aspergillus nidulans.";
RL   J. Am. Chem. Soc. 133:4010-4017(2011).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=22730213; DOI=10.1002/cbic.201200014;
RA   Simpson T.J.;
RT   "Genetic and biosynthetic studies of the fungal prenylated xanthone
RT   shamixanthone and related metabolites in Aspergillus spp. revisited.";
RL   ChemBioChem 13:1680-1688(2012).
CC   -!- FUNCTION: Baeyer-Villiger oxidase; part of the gene cluster that
CC       mediates the biosynthesis of monodictyphenone, a prenyl xanthone
CC       derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213). The
CC       pathway begins with the synthesis of atrochrysone thioester by the
CC       polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone
CC       carboxyl ACP thioesterase mdpF then breaks the thioester bond and
CC       releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316).
CC       The atrochrysone carboxylic acid is then converted to atrochrysone
CC       which is further transformed into emodin anthrone (PubMed:20139316).
CC       The next step is performed by the anthrone oxygenase mdpH that
CC       catalyzes the oxidation of emodinanthrone to emodin (By similarity).
CC       Emodin is further modified to yield monodictyphenone via several steps
CC       involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316,
CC       PubMed:21351751). These enzymes with xptA, xptB and xptC are also
CC       proposed to be involved in the synthesis of shamixanthone from emodin
CC       (PubMed:22730213). Especially, direct reduction of emodin by the short
CC       chain dehydrogenase mdpC followed by dehydration catalyzed by the
CC       scytalone dehydratase-like protein mdpB gives loss of oxygen and
CC       formation of chrysophanol intermediate in two simple steps
CC       (PubMed:22730213). {ECO:0000250|UniProtKB:Q0CCY3,
CC       ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751,
CC       ECO:0000269|PubMed:22730213}.
CC   -!- COFACTOR:
CC       Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC         Evidence={ECO:0000250|UniProtKB:Q0CCX5};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751,
CC       ECO:0000269|PubMed:22730213}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of monodictyphenone, but
CC       still enables the synthesis of intermediates until emodin
CC       (PubMed:20139316, PubMed:21351751). Results in major accumulation of
CC       chrysophanol and its 6-hydroxymethyl shunt product aloe-emodin
CC       (PubMed:22730213). {ECO:0000269|PubMed:20139316,
CC       ECO:0000269|PubMed:21351751, ECO:0000269|PubMed:22730213}.
CC   -!- SIMILARITY: Belongs to the AflY oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA66025.1; Type=Erroneous gene model prediction; Note=The predicted gene AN0152 has been split into 2 genes: ANIA_10044 and ANIA_10023.; Evidence={ECO:0000305};
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DR   EMBL; BN001308; CBF90088.1; -; Genomic_DNA.
DR   EMBL; AACD01000005; EAA66025.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_657756.1; XM_652664.1.
DR   AlphaFoldDB; C8VQ61; -.
DR   STRING; 162425.CADANIAP00002588; -.
DR   EnsemblFungi; CBF90088; CBF90088; ANIA_10023.
DR   EnsemblFungi; EAA66025; EAA66025; AN0152.2.
DR   GeneID; 2875925; -.
DR   KEGG; ani:AN0152.2; -.
DR   VEuPathDB; FungiDB:AN10023; -.
DR   eggNOG; ENOG502S69W; Eukaryota.
DR   HOGENOM; CLU_019145_2_1_1; -.
DR   InParanoid; C8VQ61; -.
DR   OMA; IDFFYMH; -.
DR   OrthoDB; 614605at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:1900815; P:monodictyphenone biosynthetic process; IMP:AspGD.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
DR   GO; GO:2001307; P:xanthone-containing compound biosynthetic process; IMP:AspGD.
DR   InterPro; IPR025337; Questin_oxidase-like.
DR   PANTHER; PTHR35870; PTHR35870; 1.
DR   Pfam; PF14027; Questin_oxidase; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..446
FT                   /note="Baeyer-Villiger oxidase mdpL"
FT                   /id="PRO_0000437100"
SQ   SEQUENCE   446 AA;  51019 MW;  8F04AB8FA8088C17 CRC64;
     MSSSINILST KLGQNIYAQT PPSQTLTLTN HLLQKNHDTL HIFFRNLNGH NHLVHNLLTR
     LVLGATPEQL QTAYDDDLPT QRAMPPLVPS IVERLSDNSY FESQITQIDQ YTNFLRFFEA
     EIDRRDSWKD VVIEYVFSRS PIAEKILPLM YDGAFHSIIH LGLGVEFEQP GIIAEALAQA
     AAHDSFGTDY FFLTAEKRAA GRNEEGETLV NLLQKIRDTP KLVEAGRVQG LIGTMKMRKS
     ILVNAADEII DIASRFKVTE ETLARKTAEM LNLCAYLAGA SQRTKDGYEP KIDFFFMHCV
     TSSIFFSILG RQDWISMRDR VRLVEWKGRL DLMWYALCGV PELDFEFVRT YRGERTGTMS
     WKELFAIVNE QHDDGHVAKF VRALKNGQEV CGQFEDGEEF MVKGDMWLRI ARMAYETTIE
     TNMQNRWVVM AGMDGAWKDF KVQSSD