MDPD_EMENI
ID MDPD_EMENI Reviewed; 521 AA.
AC Q5BH33; C8VQ69;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=FAD-dependent monooxygenase mdpD {ECO:0000303|PubMed:20139316};
DE EC=1.-.-.- {ECO:0000305|PubMed:20139316};
DE AltName: Full=Monodictyphenone synthesis protein D {ECO:0000303|PubMed:20139316};
GN Name=mdpD {ECO:0000303|PubMed:20139316}; ORFNames=AN0147;
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: FAD-dependent monooxygenase; 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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
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 {ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751,
CC ECO:0000269|PubMed:22730213}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; BN001308; CBF90103.1; -; Genomic_DNA.
DR EMBL; AACD01000005; EAA66020.1; -; Genomic_DNA.
DR RefSeq; XP_657751.1; XM_652659.1.
DR AlphaFoldDB; Q5BH33; -.
DR SMR; Q5BH33; -.
DR STRING; 162425.CADANIAP00002596; -.
DR EnsemblFungi; CBF90103; CBF90103; ANIA_00147.
DR EnsemblFungi; EAA66020; EAA66020; AN0147.2.
DR GeneID; 2875917; -.
DR KEGG; ani:AN0147.2; -.
DR VEuPathDB; FungiDB:AN0147; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_1_1; -.
DR InParanoid; Q5BH33; -.
DR OMA; PKWVFRH; -.
DR OrthoDB; 462247at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:1900815; P:monodictyphenone biosynthetic process; IMP:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
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; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..521
FT /note="FAD-dependent monooxygenase mdpD"
FT /id="PRO_0000437106"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 81..82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 379..383
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 521 AA; 57864 MW; 352125DD929A214A CRC64;
MTHFPVNIAS DKQEFDPERW AKTPTTESSV NGENGTAPTS GLPSRHPSTG ISVLIVGAGM
GGLMTALECW RKGHDVAGIL ERSEGPVYSG DIIVMQPSAV SIIRHWPDML HDMKAEQVHA
VVSYETHDGR HIYGPTVPSF NDPEHLETRK GPFVAPAQVR RKFYRMLLRQ VARCGLRVEY
GKTVKSYFED EKDGKGGVII ATTGEAEVRV ADIVVAADGL KSPSEILIAG QHVPPRSSGL
SIYRTAFPKD LAMQNELVRK RWSDSPPIWE YWLGPGMYLG VFVGDDIISF GFTPRDDIVE
GTATESWEPD TDPETVAQAM LSGAGDWDPA VLALIRSAPK GAIVHWPLLW RDLRREWTSP
AGRVVQVGDS AHSFIPTSGN GGSQALEDAI TLATCLQLAG SSQRAYLGTK IYNLLRYERV
SCAQKMSFVN SQLKTGTDWD AIWKDPAKIR TRFPKWIFQH DPEAYAYEKF GEAFAHLLDG
REFVNTNYPP GHEFRAWTVE EVWRNIADGK RVEDLLDGDW S
