MDPF_EMENI
ID MDPF_EMENI Reviewed; 307 AA.
AC Q5BH31; C8VQ67;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Atrochrysone carboxyl ACP thioesterase {ECO:0000303|PubMed:20139316};
DE Short=ACTE {ECO:0000303|PubMed:20139316};
DE EC=3.1.2.- {ECO:0000305|PubMed:20139316};
DE AltName: Full=Monodictyphenone synthesis protein F {ECO:0000303|PubMed:20139316};
GN Name=mdpF {ECO:0000303|PubMed:20139316}; ORFNames=AN0149;
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: Atrochrysone carboxyl ACP thioesterase; part of the gene
CC cluster that mediates the biosynthesis of monodictyphenone, a prenyl
CC xanthone derivative (PubMed:20139316, PubMed:21351751). The pathway
CC begins with the synthesis of atrochrysone thioester by the polyketide
CC synthase (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 (PubMed:20139316). The next
CC step is performed by the anthrone oxygenase mdpH that catalyzes the
CC oxidation of emodinanthrone to emodin (By similarity). Emodin is
CC further modified to yield monodictyphenone via several steps involving
CC mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751,
CC PubMed:22909031). The short chain dehydrogenase mdpC converts the
CC tautomers of emodin hydroquinone into the 3-hydroxy-3,4-dihydroan-
CC thracen-1(2H)-one derivative (PubMed:22909031, PubMed:26266881). These
CC enzymes with xptA, xptB and xptC are also proposed to be involved in
CC the synthesis of shamixanthone from emodin (PubMed:22730213).
CC Especially, direct reduction of emodin by the short chain dehydrogenase
CC mdpC followed by dehydration catalyzed by the scytalone dehydratase-
CC like protein mdpB gives loss of oxygen and formation of chrysophanol
CC intermediate in two simple steps (PubMed:22730213).
CC {ECO:0000250|UniProtKB:Q0CCY3, ECO:0000269|PubMed:20139316,
CC ECO:0000269|PubMed:21351751, ECO:0000269|PubMed:22730213,
CC ECO:0000269|PubMed:22909031, ECO:0000269|PubMed:26266881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=atrochrysone carboxyl-[ACP] + H2O = atrochrysone carboxylate +
CC H(+) + holo-[ACP]; Xref=Rhea:RHEA:64236, Rhea:RHEA-COMP:9685,
CC Rhea:RHEA-COMP:16552, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:149712, ChEBI:CHEBI:149713;
CC Evidence={ECO:0000305|PubMed:20139316};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64237;
CC Evidence={ECO:0000305|PubMed:20139316};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q988B9};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q988B9};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:20139316}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of monodictyphenone and
CC any of the intermediates of the pathway (PubMed:20139316,
CC PubMed:21351751). {ECO:0000269|PubMed:20139316,
CC ECO:0000269|PubMed:21351751}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; BN001308; CBF90099.1; -; Genomic_DNA.
DR EMBL; AACD01000005; EAA66022.1; -; Genomic_DNA.
DR RefSeq; XP_657753.1; XM_652661.1.
DR AlphaFoldDB; Q5BH31; -.
DR SMR; Q5BH31; -.
DR STRING; 162425.CADANIAP00002594; -.
DR EnsemblFungi; CBF90099; CBF90099; ANIA_00149.
DR EnsemblFungi; EAA66022; EAA66022; AN0149.2.
DR GeneID; 2875922; -.
DR KEGG; ani:AN0149.2; -.
DR VEuPathDB; FungiDB:AN0149; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR InParanoid; Q5BH31; -.
DR OMA; EGGYRQI; -.
DR OrthoDB; 576967at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1900815; P:monodictyphenone biosynthetic process; IMP:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..307
FT /note="Atrochrysone carboxyl ACP thioesterase"
FT /id="PRO_0000437055"
FT ACT_SITE 108
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
SQ SEQUENCE 307 AA; 33839 MW; 21F320C217C4CAB3 CRC64;
MAQPQQHKGG YKQINKALNI CAFEDYLSAQ LKHLPQLADV EQLSPRVIRV LGQNAGKGTN
TYIVGTGPQR LIIDTGQGIP EWADILDATL KERSISLSHV FLSHWHGDHT GGVPDLLRLY
PNLAGAIYKN SPGSDQQPID DGQVFRVEGA TIRAVHGPGH SHDHMCFILE EENAMFTGDN
VLGHGTSAVE ELGVYMETLR KLNSHHCAVG YPAHGDVITN LPAKIAGELA QKMRREKQVL
LTLDRINKES RRTGQVVLVH GDGIDEEVRK MALEPFIDEV LRKLAEDGKV AFEMRGGVKR
WFGVGVL
