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FAD-dependent monooxygenase mdpD (EC 1.-.-.-) (Monodictyphenone synthesis protein D)

 MDPD_EMENI              Reviewed;         521 AA.
Q5BH33; C8VQ69;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
05-DEC-2018, entry version 97.
RecName: Full=FAD-dependent monooxygenase mdpD {ECO:0000303|PubMed:20139316};
EC=1.-.-.- {ECO:0000305|PubMed:20139316};
AltName: Full=Monodictyphenone synthesis protein D {ECO:0000303|PubMed:20139316};
Name=mdpD {ECO:0000303|PubMed:20139316}; ORFNames=AN0147;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[2]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20139316; DOI=10.1128/AEM.02187-09;
Chiang Y.M., Szewczyk E., Davidson A.D., Entwistle R., Keller N.P.,
Wang C.C., Oakley B.R.;
"Characterization of the Aspergillus nidulans monodictyphenone gene
cluster.";
Appl. Environ. Microbiol. 76:2067-2074(2010).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21351751; DOI=10.1021/ja1096682;
Sanchez J.F., Entwistle R., Hung J.H., Yaegashi J., Jain S.,
Chiang Y.M., Wang C.C., Oakley B.R.;
"Genome-based deletion analysis reveals the prenyl xanthone
biosynthesis pathway in Aspergillus nidulans.";
J. Am. Chem. Soc. 133:4010-4017(2011).
-!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster
that mediates the biosynthesis of monodictyphenone, a prenyl
xanthone derivative (PubMed:20139316, PubMed:21351751). The
pathway begins with the synthesis of atrochrysone thioester by the
polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone
carboxyl ACP thioesterase mdpF then breaks the thioester bond and
releases the atrochrysone carboxylic acid from mdpG
(PubMed:20139316). The atrochrysone carboxylic acid is then
converted to atrochrysone which is further transformed into emodin
anthrone (PubMed:20139316). The next step is performed by the
anthrone oxygenase mdpH that catalyzes the oxidation of
emodinanthrone to emodin (By similarity). Emodin is further
modified to yield monodictyphenone via several steps involving
mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751).
{ECO:0000250|UniProtKB:Q0CCY3, ECO:0000269|PubMed:20139316,
ECO:0000269|PubMed:21351751}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751}.
-!- DISRUPTION PHENOTYPE: Impairs the production of monodictyphenone,
but still enables the synthesis of intermediates until emodin
(PubMed:20139316, PubMed:21351751). {ECO:0000269|PubMed:20139316,
ECO:0000269|PubMed:21351751}.
-!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BN001308; CBF90103.1; -; Genomic_DNA.
EMBL; AACD01000005; EAA66020.1; -; Genomic_DNA.
RefSeq; XP_657751.1; XM_652659.1.
ProteinModelPortal; Q5BH33; -.
EnsemblFungi; CBF90103; CBF90103; ANIA_00147.
EnsemblFungi; EAA66020; EAA66020; AN0147.2.
GeneID; 2875917; -.
KEGG; ani:AN0147.2; -.
HOGENOM; HOG000202905; -.
InParanoid; Q5BH33; -.
OMA; YFMGLSA; -.
OrthoDB; EOG092C1CBE; -.
Proteomes; UP000000560; Chromosome VIII.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
GO; GO:1900815; P:monodictyphenone biosynthetic process; IMP:AspGD.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR002938; FAD-bd.
InterPro; IPR036188; FAD/NAD-bd_sf.
Pfam; PF01494; FAD_binding_3; 1.
SUPFAM; SSF51905; SSF51905; 1.
3: Inferred from homology;
Complete proteome; FAD; Flavoprotein; Monooxygenase; Oxidoreductase;
Reference proteome.
CHAIN 1 521 FAD-dependent monooxygenase mdpD.
/FTId=PRO_0000437106.
NP_BIND 81 82 FAD. {ECO:0000250|UniProtKB:A6T923}.
NP_BIND 379 383 FAD. {ECO:0000250|UniProtKB:A6T923}.
BINDING 61 61 FAD; via amide nitrogen.
{ECO:0000250|UniProtKB:A6T923}.
BINDING 369 369 FAD. {ECO:0000250|UniProtKB:A6T923}.
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


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