MDPC_EMENI
ID MDPC_EMENI Reviewed; 265 AA.
AC Q5BH34; C8VQ70;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Short chain dehydrogenase mdpC {ECO:0000303|PubMed:20139316};
DE EC=1.3.1.- {ECO:0000269|PubMed:22909031, ECO:0000269|PubMed:26266881};
DE AltName: Full=Monodictyphenone synthesis protein C {ECO:0000303|PubMed:20139316};
GN Name=mdpC {ECO:0000303|PubMed:20139316}; ORFNames=AN0146;
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, DISRUPTION PHENOTYPE, AND PATHWAY.
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, CATALYTIC ACTIVITY, AND PATHWAY.
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, CATALYTIC ACTIVITY, AND PATHWAY.
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: Short chain dehydrogenase; part of the gene cluster that
CC mediates the biosynthesis of monodictyphenone, a prenyl xanthone
CC derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213,
CC PubMed:22909031, PubMed:26266881). The pathway begins with the
CC synthesis of atrochrysone thioester by the polyketide synthase (PKS)
CC mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF
CC then breaks the thioester bond and releases the atrochrysone carboxylic
CC acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is
CC then converted to atrochrysone which is further transformed into emodin
CC anthrone (PubMed:20139316). The next step is performed by the anthrone
CC oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin
CC (By similarity). Emodin is further modified to yield monodictyphenone
CC via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL
CC (PubMed:20139316, PubMed:21351751, PubMed:22909031). The short chain
CC dehydrogenase mdpC converts the tautomers of emodin hydroquinone into
CC the 3-hydroxy-3,4-dihydroan-thracen-1(2H)-one derivative
CC (PubMed:22909031, PubMed:26266881). 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, ECO:0000269|PubMed:22909031,
CC ECO:0000269|PubMed:26266881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,8,9,10-tetrahydroxy-6-methyl-1,4-dihydroanthracen-1-one +
CC H(+) + NADPH = (3R)-3,8,9,10-tetrahydroxy-6-methyl-1,2,3,4-
CC tetrahydroanthracen-1-one + NADP(+); Xref=Rhea:RHEA:64292,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:150020, ChEBI:CHEBI:150021;
CC Evidence={ECO:0000269|PubMed:22909031, ECO:0000269|PubMed:26266881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64293;
CC Evidence={ECO:0000269|PubMed:22909031};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751,
CC ECO:0000269|PubMed:22730213, ECO:0000269|PubMed:22909031,
CC ECO:0000269|PubMed:26266881}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of monodictyphenone, but
CC still enables the synthesis of intermediates until emodin.
CC {ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751,
CC ECO:0000269|PubMed:22730213}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BN001308; CBF90105.1; -; Genomic_DNA.
DR EMBL; AACD01000005; EAA66019.1; -; Genomic_DNA.
DR RefSeq; XP_657750.1; XM_652658.1.
DR AlphaFoldDB; Q5BH34; -.
DR SMR; Q5BH34; -.
DR STRING; 162425.CADANIAP00002597; -.
DR EnsemblFungi; CBF90105; CBF90105; ANIA_00146.
DR EnsemblFungi; EAA66019; EAA66019; AN0146.2.
DR GeneID; 2875920; -.
DR KEGG; ani:AN0146.2; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR InParanoid; Q5BH34; -.
DR OMA; NAAHAHR; -.
DR OrthoDB; 913128at2759; -.
DR BioCyc; MetaCyc:MON-21290; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..265
FT /note="Short chain dehydrogenase mdpC"
FT /id="PRO_0000437105"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 17..25
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 44..45
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 70..72
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 162..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 195..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 265 AA; 28448 MW; 4FE607E41DCD0FC7 CRC64;
MTATTHAPYR LEGKVALVTG SGRGIGAAMA LELGRLGAKV VVNYANSREP AEKLVQEIKE
LGTDAIALQA NIRNVSEIVR VMDDAVAHFG GLDIVCSNAG VVSFGHLGEV TEEEFDRVFS
LNTRAQFFVA REAYRHLNTH GRIILMSSNT AKEFSVPRHS VYSGSKGAIE SFVRVMAKDC
GDKQITVNAV APGGTVTDMF YDVAQHYIPN GEKHSAEELQ KMAATVSPLK RNGFPVDIAK
VVGFLASREA EWVNGKIITV DGGAA
