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Questin oxidase (EC 1.-.-.-) (Monodictyphenone synthesis protein L)

 MDPL_EMENI              Reviewed;         446 AA.
C8VQ61; Q5BH28;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 1.
20-JUN-2018, entry version 39.
RecName: Full=Questin oxidase {ECO:0000250|UniProtKB:Q0CCX5};
EC=1.-.-.- {ECO:0000250|UniProtKB:Q0CCX5};
AltName: Full=Monodictyphenone synthesis protein L {ECO:0000303|PubMed:20139316};
Name=mdpL {ECO:0000303|PubMed:20139316};
Synonyms=tynL {ECO:0000303|PubMed:20139316}; ORFNames=ANIA_10023;
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: Non-reducing polyketide synthase; 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 gedC
(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=NADPH; Xref=ChEBI:CHEBI:57783;
Evidence={ECO:0000250|UniProtKB:Q0CCX5};
-!- 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 AflY oxidoreductase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
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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EMBL; BN001308; CBF90088.1; -; Genomic_DNA.
EMBL; AACD01000005; EAA66025.1; ALT_SEQ; Genomic_DNA.
RefSeq; XP_657756.1; XM_652664.1.
STRING; 162425.CADANIAP00002588; -.
EnsemblFungi; CBF90088; CBF90088; ANIA_10023.
EnsemblFungi; EAA66025; EAA66025; AN0152.2.
GeneID; 2875925; -.
KEGG; ani:AN0152.2; -.
HOGENOM; HOG000160151; -.
InParanoid; C8VQ61; -.
OMA; MGWKELY; -.
OrthoDB; EOG092C1PZR; -.
Proteomes; UP000000560; Chromosome VIII.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:1900815; P:monodictyphenone biosynthetic process; IMP:AspGD.
GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
GO; GO:2001307; P:xanthone-containing compound biosynthetic process; IMP:AspGD.
InterPro; IPR025337; Questin_oxidase-like.
PANTHER; PTHR35870; PTHR35870; 1.
Pfam; PF14027; DUF4243; 1.
3: Inferred from homology;
Complete proteome; Oxidoreductase; Reference proteome.
CHAIN 1 446 Questin oxidase.
/FTId=PRO_0000437100.
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


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