MDPJ_EMENI
ID MDPJ_EMENI Reviewed; 210 AA.
AC C8VQ63;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Glutathione S-transferase mdpJ {ECO:0000303|PubMed:22730213};
DE EC=2.5.1.- {ECO:0000305|PubMed:22730213};
DE AltName: Full=Monodictyphenone synthesis protein J {ECO:0000303|PubMed:20139316};
GN Name=mdpJ {ECO:0000303|PubMed:20139316}; ORFNames=ANIA_10038;
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, AND DISRUPTION PHENOTYPE.
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, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Glutathione S-transferase; part of the gene cluster that
CC mediates the biosynthesis of monodictyphenone, a prenyl xanthone
CC derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213). The
CC pathway begins with the synthesis of atrochrysone thioester by the
CC polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone
CC carboxyl ACP thioesterase mdpF then breaks the thioester bond and
CC releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316).
CC The atrochrysone carboxylic acid is then converted to atrochrysone
CC which is further transformed into emodin anthrone (PubMed:20139316).
CC The next step is performed by the anthrone oxygenase mdpH that
CC catalyzes the oxidation of emodinanthrone to emodin (By similarity).
CC Emodin is further modified to yield monodictyphenone via several steps
CC involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316,
CC PubMed:21351751). These enzymes with xptA, xptB and xptC are also
CC proposed to be involved in the synthesis of shamixanthone from emodin
CC (PubMed:22730213). Especially, direct reduction of emodin by the short
CC chain dehydrogenase mdpC followed by dehydration catalyzed by the
CC 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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751,
CC ECO:0000269|PubMed:22730213}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of monodictyphenone. but
CC still enables the production of intermediates untill emodin.
CC {ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751,
CC ECO:0000269|PubMed:22730213}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; BN001308; CBF90092.1; -; Genomic_DNA.
DR AlphaFoldDB; C8VQ63; -.
DR SMR; C8VQ63; -.
DR STRING; 162425.CADANIAP00002590; -.
DR EnsemblFungi; CBF90092; CBF90092; ANIA_10038.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_3_2_1; -.
DR InParanoid; C8VQ63; -.
DR OMA; FGTIYTH; -.
DR OrthoDB; 1341490at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Reference proteome; Transferase.
FT CHAIN 1..210
FT /note="Glutathione S-transferase mdpJ"
FT /id="PRO_0000437068"
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 77..200
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
SQ SEQUENCE 210 AA; 23726 MW; D2F834C4BBA22C99 CRC64;
MSFGTLYTHN PTPRSTTLIA LAKLHNLDVK IIHAEKKNKE AFEELCRYNP LGQVPTFVGA
DGFVLSECIP LTLYCNDERS SLRILQWMSF ANSDLFPAVG GVFLPRIGQR QIIQQDDGDS
LRAMLQRCKY LDEHLKRSRY LVGESITIAD FFAASLLMGA FAAFRRSMQE RFGALCSWYD
GVLEIGWFKK VAGGVPDLGL ELEIPEDIKW
