MDPB_EMENI
ID MDPB_EMENI Reviewed; 214 AA.
AC C8VQ71; Q5BH35;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Scytalone dehydratase-like protein mdpB {ECO:0000303|PubMed:20139316};
DE EC=4.2.1.- {ECO:0000269|PubMed:20139316};
DE AltName: Full=Monodictyphenone synthesis protein B {ECO:0000303|PubMed:20139316};
GN Name=mdpB {ECO:0000303|PubMed:20139316}; ORFNames=ANIA_10049;
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).
CC -!- FUNCTION: Scytalone dehydratase-like protein; part of the gene cluster
CC that 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 synthesis of intermediates until emodin.
CC {ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751,
CC ECO:0000269|PubMed:22730213}.
CC -!- SIMILARITY: Belongs to the scytalone dehydratase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA66018.1; Type=Erroneous gene model prediction; Note=The predicted gene AN0145 has been split into 2 genes: ANIA_10021 and ANIA_10049.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BN001308; CBF90107.1; -; Genomic_DNA.
DR EMBL; AACD01000005; EAA66018.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_657749.1; XM_652657.1.
DR AlphaFoldDB; C8VQ71; -.
DR SMR; C8VQ71; -.
DR STRING; 162425.CADANIAP00002598; -.
DR EnsemblFungi; CBF90107; CBF90107; ANIA_10049.
DR EnsemblFungi; EAA66018; EAA66018; AN0145.2.
DR GeneID; 2875924; -.
DR KEGG; ani:AN0145.2; -.
DR VEuPathDB; FungiDB:AN10049; -.
DR eggNOG; ENOG502SNND; Eukaryota.
DR HOGENOM; CLU_101889_1_0_1; -.
DR InParanoid; C8VQ71; -.
DR OMA; RKCIAPT; -.
DR OrthoDB; 1377897at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0030411; F:scytalone dehydratase activity; IEA:InterPro.
DR GO; GO:0006582; P:melanin metabolic process; IEA:InterPro.
DR GO; GO:1900815; P:monodictyphenone biosynthetic process; IMP:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
DR GO; GO:2001307; P:xanthone-containing compound biosynthetic process; IMP:AspGD.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR004235; Scytalone_dehydratase.
DR Pfam; PF02982; Scytalone_dh; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 3: Inferred from homology;
KW Lyase; Reference proteome.
FT CHAIN 1..214
FT /note="Scytalone dehydratase-like protein mdpB"
FT /id="PRO_0000437107"
FT ACT_SITE 95
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT ACT_SITE 120
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
SQ SEQUENCE 214 AA; 24307 MW; 1C2ED4EEE9DD69FF CRC64;
MTLQPTFEGR TPEQCLNVHT DSHPDITGCQ AALFEWAESY DSKDWDRLKQ CIAPFLRIDY
RAFLDKLWEK MPAEEFVAMV SHPHFLGNPL LKTQHFVGTM KWEKVDDSKI VGYHQMRVAH
QKHLDSQMKE VVAKGHGHGS ATVTYRKING EWKFAGIEPN IRWTEFGGEG IFGPPEKEEN
GVAADDQVMN SNGSSEVEER NGHVVNKAVE VRSV
