MDPH1_EMENI
ID MDPH1_EMENI Reviewed; 161 AA.
AC P9WEV8; C8VQ65; Q5BH29;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 25-MAY-2022, entry version 7.
DE RecName: Full=Decarboxylase {ECO:0000250|UniProtKB:P0DOB3};
DE EC=4.1.1.- {ECO:0000250|UniProtKB:P0DOB3};
DE AltName: Full=Monodictyphenone synthesis protein H-1 {ECO:0000303|PubMed:20139316};
GN Name=mdpH-1 {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).
RN [6]
RP FUNCTION.
RX PubMed=22909031; DOI=10.1021/ja307151x;
RA Schaetzle M.A., Husain S.M., Ferlaino S., Mueller M.;
RT "Tautomers of anthrahydroquinones: enzymatic reduction and implications for
RT chrysophanol, monodictyphenone, and related xanthone biosyntheses.";
RL J. Am. Chem. Soc. 134:14742-14745(2012).
RN [7]
RP FUNCTION.
RX PubMed=26266881; DOI=10.1021/jacs.5b06770;
RA Conradt D., Schaetzle M.A., Haas J., Townsend C.A., Mueller M.;
RT "New Insights into the Conversion of Versicolorin A in the Biosynthesis of
RT Aflatoxin B1.";
RL J. Am. Chem. Soc. 137:10867-10869(2015).
CC -!- FUNCTION: Decarboxylase; part of the gene cluster that mediates the
CC 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=atrochrysone carboxylate + H(+) = atrochrysone + CO2;
CC Xref=Rhea:RHEA:64264, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:149713, ChEBI:CHEBI:150016;
CC Evidence={ECO:0000250|UniProtKB:P0DOB3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64265;
CC Evidence={ECO:0000250|UniProtKB:P0DOB3};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751}.
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 tpcK 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 AlphaFoldDB; P9WEV8; -.
DR EnsemblFungi; CBF90095; CBF90095; ANIA_10022.
DR EnsemblFungi; EAA66024; EAA66024; AN0151.2.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR009799; EthD_dom.
DR Pfam; PF07110; EthD; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
PE 3: Inferred from homology;
KW Lyase; Reference proteome.
FT CHAIN 1..161
FT /note="Decarboxylase"
FT /id="PRO_0000437097"
FT DOMAIN 29..131
FT /note="EthD"
FT /evidence="ECO:0000255"
SQ SEQUENCE 161 AA; 18773 MW; ED12D0306528BFC7 CRC64;
MSTPNPPATN STTSEDRLLC LTILGYRKQG MSEEAYRKHM IEHSAPLTKD LMIKYGILRW
TVKCPDRSKI HNPTETRELM YEIMDPQMAN IADYDCFSQV VFRNFEDYKK IKDDPWYKEH
LVGDHENFAD TKRSKMTIGW ITQFIDRGVV TEGFEGFPGP K
