MDPH2_EMENI
ID MDPH2_EMENI Reviewed; 192 AA.
AC P9WEV9; C8VQ65; Q5BH29;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=Anthrone oxygenase {ECO:0000250|UniProtKB:P0DOB2};
DE EC=1.10.3.- {ECO:0000250|UniProtKB:P0DOB2};
DE AltName: Full=Monodictyphenone synthesis protein H-2 {ECO:0000303|PubMed:20139316};
GN Name=mdpH-2 {ECO:0000303|PubMed:20139316}; ORFNames=ANIA_10022;
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.
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: Anthrone oxygenase; part of the gene cluster that mediates
CC the 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 by mdpH-1 and mdpH-2
CC (PubMed:20139316). Emodin is further modified to yield monodictyphenone
CC via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL
CC (PubMed:20139316, PubMed:21351751). These enzymes with xptA, xptB and
CC xptC are also proposed to be involved in the synthesis of shamixanthone
CC from emodin (PubMed:22730213). Especially, direct reduction of emodin
CC by the short chain dehydrogenase mdpC followed by dehydration catalyzed
CC by the 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 -!- CATALYTIC ACTIVITY:
CC Reaction=emodin anthrone + O2 = emodin + H(+) + H2O;
CC Xref=Rhea:RHEA:64268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:77659, ChEBI:CHEBI:150013;
CC Evidence={ECO:0000250|UniProtKB:P0DOB2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64269;
CC Evidence={ECO:0000250|UniProtKB:P0DOB2};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of monodictyphenone, but
CC leads to the accumulation of endocrocin (PubMed:20139316,
CC PubMed:21351751). {ECO:0000269|PubMed:20139316,
CC ECO:0000269|PubMed:21351751}.
CC -!- SIMILARITY: Belongs to the anthrone oxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF90095.1; Type=Erroneous gene model prediction; Note=The predicted gene ANIA_10022 has been split into 2 genes: mdpH-1 and mdpH-2.; Evidence={ECO:0000305};
CC Sequence=EAA66024.1; Type=Erroneous gene model prediction; Note=The predicted gene AN0151 has been split into 2 genes: ANIA_10022 and ANIA_10035. ANIA_10022 has been further split into mdpH-1 and mdpH-2.; Evidence={ECO:0000305};
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DR EMBL; BN001308; CBF90095.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000005; EAA66024.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_657755.1; XM_652663.1.
DR AlphaFoldDB; P9WEV9; -.
DR GeneID; 2875926; -.
DR KEGG; ani:AN0151.2; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Monooxygenase; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..192
FT /note="Anthrone oxygenase"
FT /id="PRO_0000450871"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 192 AA; 20918 MW; 2814E86A18EA220E CRC64;
MASLTTLKNT AIVTGSFLSG AMITLSTITV PVLLETSTHP PQLLHQWVRT YHYGHISLPT
ISIATAILYF YIAAYQGARE QPWRKAALVG FLTIVMVPFT WIVMSSTNGM LFGLEAGNRD
HSQFFEQGAN RSGLKGANSS QSHGLGNVSV GIGVEMATLE GVRELLVRWK WMHLVRSLFP
LMAAVLGVGI CV
