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Anthrone oxygenase (EC 1.-.-.-) (Monodictyphenone synthesis protein H)

 MDPH_EMENI              Reviewed;         383 AA.
C8VQ65; Q5BH29;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 1.
20-JUN-2018, entry version 40.
RecName: Full=Anthrone oxygenase {ECO:0000250|UniProtKB:Q0CCX7};
EC=1.-.-.- {ECO:0000250|UniProtKB:Q0CCX7};
AltName: Full=Monodictyphenone synthesis protein H {ECO:0000303|PubMed:20139316};
Name=mdpH {ECO:0000303|PubMed:20139316}; ORFNames=ANIA_10022;
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: Anthrone oxygenase; 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:Q0CCX7, ECO:0000269|PubMed:20139316,
ECO:0000269|PubMed:21351751}.
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
protein {ECO:0000255}.
-!- DISRUPTION PHENOTYPE: Impairs the production of monodictyphenone,
but leads to the accumulation of endocrocin (PubMed:20139316,
PubMed:21351751). {ECO:0000269|PubMed:20139316,
ECO:0000269|PubMed:21351751}.
-!- SIMILARITY: Belongs to the anthrone oxygenase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAA66024.1; Type=Erroneous gene model prediction; Note=The predicted gene AN0151 has been split into 2 genes: ANIA_10022 and ANIA_10035.; Evidence={ECO:0000305};
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EMBL; BN001308; CBF90095.1; -; Genomic_DNA.
EMBL; AACD01000005; EAA66024.1; ALT_SEQ; Genomic_DNA.
RefSeq; XP_657755.1; XM_652663.1.
EnsemblFungi; CBF90095; CBF90095; ANIA_10022.
EnsemblFungi; EAA66024; EAA66024; AN0151.2.
GeneID; 2875926; -.
KEGG; ani:AN0151.2; -.
OrthoDB; EOG092C5MO8; -.
Proteomes; UP000000560; Chromosome VIII.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:1900815; P:monodictyphenone biosynthetic process; IMP:AspGD.
InterPro; IPR011008; Dimeric_a/b-barrel.
InterPro; IPR009799; EthD_dom.
Pfam; PF07110; EthD; 1.
SUPFAM; SSF54909; SSF54909; 1.
3: Inferred from homology;
Complete proteome; Glycoprotein; Membrane; Monooxygenase;
Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 383 Anthrone oxygenase.
/FTId=PRO_0000437097.
TRANSMEM 203 223 Helical. {ECO:0000255}.
TRANSMEM 245 265 Helical. {ECO:0000255}.
TRANSMEM 277 297 Helical. {ECO:0000255}.
TRANSMEM 363 383 Helical. {ECO:0000255}.
CARBOHYD 10 10 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
SEQUENCE 383 AA; 42867 MW; 922874ECA49822D0 CRC64;
MSTPNPPATN STTSEDRLLC LTILGYRKQG MSEEAYRKHM IEHSAPLTKD LMIKYGILRW
TVKCPDRSKI HNPTETRELM YEIMDPQMAN IADYDCFSQV VFRNFEDYKK IKDDPWYKEH
LVGDHENFAD TKRSKMTIGW ITQFIDRGVV TEGFEGFPGP KNLAGFSQTN SFILHISASS
NLSANIKYSL IMASLTTLKN TAIVTGSFLS GAMITLSTIT VPVLLETSTH PPQLLHQWVR
TYHYGHISLP TISIATAILY FYIAAYQGAR EQPWRKAALV GFLTIVMVPF TWIVMSSTNG
MLFGLEAGNR DHSQFFEQGA NRSGLKGANS SQSHGLGNVS VGIGVEMATL EGVRELLVRW
KWMHLVRSLF PLMAAVLGVG ICV


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