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MDPK_EMENI
ID   MDPK_EMENI              Reviewed;         265 AA.
AC   C8VQ62; Q5BH28;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Oxidoreductase mdpK {ECO:0000303|PubMed:21351751};
DE            EC=1.-.-.- {ECO:0000305|PubMed:22730213};
DE   AltName: Full=Monodictyphenone synthesis protein k {ECO:0000303|PubMed:20139316};
GN   Name=mdpK {ECO:0000303|PubMed:20139316}; ORFNames=ANIA_10044;
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: Oxidoreductase; part of the gene cluster that mediates the
CC       biosynthesis of monodictyphenone, a prenyl xanthone derivative
CC       (PubMed:20139316, PubMed:21351751, PubMed:22730213). The pathway begins
CC       with the synthesis of atrochrysone thioester by the polyketide synthase
CC       (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP
CC       thioesterase mdpF then breaks the thioester bond and releases the
CC       atrochrysone carboxylic acid from mdpG (PubMed:20139316). The
CC       atrochrysone carboxylic acid is then converted to atrochrysone which is
CC       further transformed into emodin anthrone (PubMed:20139316). The next
CC       step is performed by the anthrone oxygenase mdpH that catalyzes the
CC       oxidation of emodinanthrone to emodin (By similarity). Emodin is
CC       further modified to yield monodictyphenone via several steps involving
CC       mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751).
CC       These enzymes with xptA, xptB and xptC are also proposed to be involved
CC       in the synthesis of shamixanthone from emodin (PubMed:22730213).
CC       Especially, direct reduction of emodin by the short chain dehydrogenase
CC       mdpC followed by dehydration catalyzed by the scytalone dehydratase-
CC       like protein mdpB gives loss of oxygen and formation of chrysophanol
CC       intermediate in two simple steps (PubMed:22730213).
CC       {ECO:0000250|UniProtKB:Q0CCY3, ECO:0000269|PubMed:20139316,
CC       ECO:0000269|PubMed:21351751, ECO:0000269|PubMed:22730213}.
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 avfA 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; CBF90090.1; -; Genomic_DNA.
DR   EMBL; AACD01000005; EAA66025.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; C8VQ62; -.
DR   SMR; C8VQ62; -.
DR   STRING; 162425.CADANIAP00002589; -.
DR   EnsemblFungi; CBF90090; CBF90090; ANIA_10044.
DR   EnsemblFungi; EAA66025; EAA66025; AN0152.2.
DR   VEuPathDB; FungiDB:AN10044; -.
DR   eggNOG; ENOG502SM0C; Eukaryota.
DR   HOGENOM; CLU_090039_1_0_1; -.
DR   InParanoid; C8VQ62; -.
DR   OMA; AYCRNKA; -.
DR   OrthoDB; 1166292at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase 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; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF13460; NAD_binding_10; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..265
FT                   /note="Oxidoreductase mdpK"
FT                   /id="PRO_0000437063"
SQ   SEQUENCE   265 AA;  28877 MW;  8DFE9CA6D8B37725 CRC64;
     MPLATYAVLG ATGNTGTALI QNLLSPPSSE MHINAYCRNK PKLLNLLPEL NDTKNVTIFE
     GSITDLSLIT ACIRNTRAVF LTVTSNDNIP GCRLSQDSVQ TVLEALKQIR TAEPNAVVPK
     LVLLSSATID PHLSRKMPSW FLPIMKTAAS NVYADLIKAE EMLRANESWV TSIFIKPAGL
     SVDIQRGHKL DFDEQESFIS YLDLAAAMLE AANDTDGRYD GRNVSVVNTG GKARFPPGTP
     KCIIVGLLRH FFPGLHRFLP TTGPS
 
 
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